|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
227-331 |
1.38e-74 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 243.85 E-value: 1.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 227 DRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 306
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1207141740 307 RNDDIADGNPKLTLGLIWTIILHFQ 331
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
224-342 |
4.85e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 240.31 E-value: 4.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 224 DERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 303
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141740 304 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 342
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
344-449 |
2.70e-71 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 234.53 E-value: 2.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1207141740 424 PEDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
216-340 |
1.35e-69 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 230.64 E-value: 1.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 216 ERAVIRIADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDF 295
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDY 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207141740 296 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 340
Cdd:cd21236 84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
345-449 |
1.02e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.41 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1207141740 425 EDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
224-341 |
1.51e-61 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 207.19 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 224 DERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 303
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141740 304 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 341
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
345-449 |
9.69e-59 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 198.67 E-value: 9.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 424
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1207141740 425 EDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
343-449 |
6.23e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 176.39 E-value: 6.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 343 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLL 422
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1207141740 423 DPEDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
229-332 |
2.92e-50 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 174.49 E-value: 2.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 229 VQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 307
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1207141740 308 NDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
216-328 |
4.54e-50 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 174.48 E-value: 4.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 216 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 293
Cdd:cd21246 2 ERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 294 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21246 82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
345-445 |
7.72e-48 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 167.59 E-value: 7.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1207141740 425 EDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
345-445 |
6.90e-46 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 161.79 E-value: 6.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141740 425 EDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
216-328 |
6.28e-45 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 159.38 E-value: 6.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 216 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 293
Cdd:cd21193 2 EKGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 294 DFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21193 82 AFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
225-332 |
3.25e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.54 E-value: 3.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 225 ERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 300
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1207141740 301 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
223-445 |
1.66e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 170.89 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 223 ADERDRVQKKTFTKWVNKHLVKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHR 299
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 300 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGRL 378
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 379 FNAIIHKHRPNLIDINKVYRQTNLE--NLEQAFSIAERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 445
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
222-328 |
4.09e-43 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 155.18 E-value: 4.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 222 IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQ 300
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQR 110
|
90 100
....*....|....*....|....*...
gi 1207141740 301 VKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21318 111 VHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
216-328 |
3.90e-42 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 152.13 E-value: 3.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 216 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 293
Cdd:cd21317 17 ERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 294 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21317 97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
225-332 |
5.92e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 148.10 E-value: 5.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 225 ERDRVQKKTFTKWVNKHLVKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 300
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1207141740 301 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
332-445 |
6.15e-40 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 145.20 E-value: 6.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 332 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 412 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
344-449 |
8.68e-40 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 144.77 E-value: 8.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1207141740 424 PEDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
345-445 |
2.24e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 143.61 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1207141740 425 EDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1091-1168 |
1.63e-38 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 139.66 E-value: 1.63e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 1091 LSWQYLMRDITLINSWNFIMFKTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRS 1168
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
229-330 |
3.10e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.23 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 229 VQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 306
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1207141740 307 RNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
227-328 |
3.81e-38 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 139.83 E-value: 3.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 227 DRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 305
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1207141740 306 IRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
344-445 |
4.05e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 140.00 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1207141740 424 PEDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
225-332 |
5.10e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 139.58 E-value: 5.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 225 ERDRVQKKTFTKWVNKHLVKAQ--RHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 302
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1207141740 303 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
341-445 |
7.98e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.42 E-value: 7.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 341 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 420
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1207141740 421 LLDPEDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
348-449 |
8.93e-37 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 135.63 E-value: 8.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 348 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141740 427 VDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
329-445 |
4.79e-36 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 134.80 E-value: 4.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 329 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQA 408
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141740 409 FSIAERDLGVTRLLDPEDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
224-332 |
8.04e-36 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 133.51 E-value: 8.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 224 DERDRVQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 302
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1207141740 303 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1963-2808 |
1.32e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 151.06 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1963 QQKSKAEKETmsnTEKSKQLLESEAAKMRELAEEATKLRSV---AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 2039
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2040 TRLKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--------KIGQLKKSSDTELDRQKKIVEETL 2111
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2112 KQ----RKVVEEEIHILKLNFEKASSGKQELELELKKlkgiADETQKSKAkaeeeaekFRKLALEEEKKRKEAEAKVKQI 2187
Cdd:PTZ00121 1237 KDaeeaKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKADE--------LKKAEEKKKADEAKKAEEKKKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2188 QAAEEEAARQHKAAQeevgrLMKLAEEAKKQKEIAEKEAEkqvilvqEAAQKCSAAEQKAQnvlvqqnkdsmaqdKLKEE 2267
Cdd:PTZ00121 1305 DEAKKKAEEAKKADE-----AKKKAEEAKKKADAAKKKAE-------EAKKAAEAAKAEAE--------------AAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2268 FEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEasrraeaeaaalKLKQE 2347
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK------------------ADEAKKKAEED------------KKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2348 ADSEMAKYKKLAEKtLKQKSSVEEELVKVKVQLDETDKQKsvldvELKRLKQEVSDA--IKQKAQVEDELSKVKIQMEDL 2425
Cdd:PTZ00121 1409 ELKKAAAAKKKADE-AKKKAEEKKKADEAKKKAEEAKKAD-----EAKKKAEEAKKAeeAKKKAEEAKKADEAKKKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2426 LKLklkiekenQELMKKDKDNTKKlleeeAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2505
Cdd:PTZ00121 1483 KKA--------DEAKKKAEEAKKK-----ADEAKKAAEAKKK----ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2506 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQE--------TEGFQKSLEAERKRQLEITAEAEKLKVKVTQL 2577
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2578 SdaqsKAEEEAKK---FKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEkeklkkeAADL 2654
Cdd:PTZ00121 1626 K----KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-------AEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2655 QKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2734
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEK------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 2735 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEE 2808
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAniiEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
345-445 |
3.75e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 131.37 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141740 425 EDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
216-328 |
5.82e-35 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 132.47 E-value: 5.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 216 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 293
Cdd:cd21316 39 ERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKAL 118
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 294 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21316 119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1802-2594 |
7.00e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 148.75 E-value: 7.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1802 EEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQ- 1880
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEi 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1881 -KEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEEELIKVRKEME 1959
Cdd:PTZ00121 1157 aRKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA--EAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1960 ILLQQKSKAEKETMSNTEKSKQLLESEAAKM--RELAEEATKLRSvAEEAKKQRQIAEEEAARQRAEAEKI--LKEKLTA 2035
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFarRQAAIKAEEARK-ADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2036 INEATRLKTEAEIALKEKEAendrLKRKAEEEGYQ---RKVLEDQAAQHKQAIEEKigqlKKSSDTELDRQKKIVEETLK 2112
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADA----AKKKAEEAKKAaeaAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2113 QRKVVEEEIHILKlnfeKASSGKQElelelkklkgiADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEE 2192
Cdd:PTZ00121 1386 KAEEKKKADEAKK----KAEEDKKK-----------ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2193 EAARQHKAAQEevgrLMKLAEEAKKQKEIAEKEAEKQVilVQEAAQKCSAAEQKAQNVlvqqnKDSMAQDKLKEEFEKAK 2272
Cdd:PTZ00121 1451 KKAEEAKKAEE----AKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEA-----KKAAEAKKKADEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2273 KlAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEM 2352
Cdd:PTZ00121 1520 E-AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2353 AKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVldvelKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKI 2432
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2433 EKENQELMKKDKDNTKK--LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKL 2510
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2511 KAEAEKLQKQKDQAQVEAQKLLEAKKE-MQQRLDQETE---------------GFQKSLEAERKRQLEITAEAEKLKVKV 2574
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEEDEkrrmevdkkikdifdNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
810 820
....*....|....*....|
gi 1207141740 2575 TQLSDAQSKAEEEAKKFKKQ 2594
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKH 1852
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
228-333 |
1.11e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 124.87 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 304
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
332-445 |
1.69e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 124.18 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 332 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 412 AERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 445
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
344-442 |
2.14e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 123.30 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1207141740 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
348-450 |
5.28e-32 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 122.34 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 348 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLDPE 425
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1207141740 426 DVDVPHPDEKSIITYVSSMYDVMPR 450
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1542-2418 |
8.98e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 138.35 E-value: 8.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1542 QDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQE 1621
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1622 LKTLSEQEIKAKSQQVEEAllsrtRIEEEIHiirlqlettmkqkntaetELLQLRaKAVDADKLRNAaqEEAEKLRKqvA 1701
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAA-----RKAEEVR------------------KAEELR-KAEDARKAEAA--RKAEEERK--A 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1702 EETqkkRKAEEELKRKSEAEkdaakekkkaledLEKFKLQAEEAERHLKQAELEKQRQIQ--VVEEVAKKTAATQLESKQ 1779
Cdd:PTZ00121 1215 EEA---RKAEDAKKAEAVKK-------------AEEAKKDAEEAKKAEEERNNEEIRKFEeaRMAHFARRQAAIKAEEAR 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1780 VALTAR-LEESLKNEQVMVIQLQEEAEHLKKQQAEADKArEQAEKELETWRQKANEALRlrlqAEEEANKKtaaqeeaek 1858
Cdd:PTZ00121 1279 KADELKkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKK----KAEEAKKA--------- 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1859 qKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEEtAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVN 1938
Cdd:PTZ00121 1345 -AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEEDKKKA----DELKKAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1939 SAVKQKKELEEelikVRKEMEIllqqKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlrsvAEEAKKQRQIAEE-E 2017
Cdd:PTZ00121 1419 KADEAKKKAEE----KKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAKKKAEEAKKaD 1486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2018 AARQRAEAEKILKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--KIGQLKKS 2095
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADElkKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2096 SDTELDRQKKIVEETLKQ--------RKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKaeeeaekfR 2167
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--------K 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2168 KLALEEEKKRKEAEAKVKQIQAAEEE----AARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCS 2241
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2242 AAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEkaKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAE 2321
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2322 KLRKEAEKEASRRAEAEAAAlklkQEADSEMAKYKKLAEKTlkQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLK 2398
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDNFANI----IEGGKEGNLVINDSKEM--EDSAIKEVADSKNMQLEEADafeKHKFNKNNENGEDG 1864
|
890 900
....*....|....*....|
gi 1207141740 2399 QEVSDAIKQKAQVEDELSKV 2418
Cdd:PTZ00121 1865 NKEADFNKEKDLKEDDEEEI 1884
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
344-442 |
1.90e-31 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 120.71 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1207141740 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
229-332 |
1.96e-31 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 120.88 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 229 VQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 307
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1207141740 308 NDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1511-2087 |
2.41e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 136.22 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1511 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANE 1589
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1590 LKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKsQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1669
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1670 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledLEKFKLQAEEAERHL 1749
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER------------------LEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1750 KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1829
Cdd:COG1196 434 EEEEEEEEEALE--EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1830 QKANEALR------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM----AEETA 1899
Cdd:COG1196 512 AALLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIraraALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1900 KQKLAAEQELIRLRADFEHAEQQRTVLDDEL---QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnT 1976
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----R 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1977 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 2056
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
570 580 590
....*....|....*....|....*....|.
gi 1207141740 2057 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 2087
Cdd:COG1196 748 LEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
229-332 |
6.00e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 119.31 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 229 VQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 306
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1207141740 307 RNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
348-449 |
9.85e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 118.52 E-value: 9.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 348 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141740 427 VDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
350-445 |
1.70e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 117.83 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 350 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 428
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1207141740 429 VPHPDEKSIITYVSSMY 445
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
225-334 |
2.43e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.68 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 225 ERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 300
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1207141740 301 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 334
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1560-2762 |
8.12e-30 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 131.49 E-value: 8.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1560 AEMQAELEkqkqlAETHAKAIAKAEQEANEL-------KTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKA 1632
Cdd:NF041483 111 AEHQARLQ-----AELHTEAVQRRQQLDQELaerrqtvESHVNENVAWAEQLRARTESQA---RRLLDESRAEAEQALAA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1633 KSQQVEeallsrtRIEEEIHIiRLQLETtmkQKNTAETELLQLRAKAvDADKLRNAAQEEA-------EKLRKQVAEETQ 1705
Cdd:NF041483 183 ARAEAE-------RLAEEARQ-RLGSEA---ESARAEAEAILRRARK-DAERLLNAASTQAqeatdhaEQLRSSTAAESD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1706 KKRKAEEELKRKSEAekdaakekkkaledlekfklQAEEAERHLKQAELEKQRqiqVVEEvAKKTAATQLESKQVALTAR 1785
Cdd:NF041483 251 QARRQAAELSRAAEQ--------------------RMQEAEEALREARAEAEK---VVAE-AKEAAAKQLASAESANEQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1786 LEESLKNEQVMVIQLQEEAEHLKkqqAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKR 1865
Cdd:NF041483 307 TRTAKEEIARLVGEATKEAEALK---AEAEQALADARAEAEKLVAEAAEKAR-TVAAEDTAAQLAKAARTAEEVLTKASE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1866 EAKK--RAKAEEAALKQKEAaEMELGNQRKMAEETAKQ-KLAA--------------EQELIRLRADfehAEQQRTVLDD 1928
Cdd:NF041483 383 DAKAttRAAAEEAERIRREA-EAEADRLRGEAADQAEQlKGAAkddtkeyraktvelQEEARRLRGE---AEQLRAEAVA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1929 ELQRLKNDV-NSAVKQKKE----LEEELIKVRKEMEILLQQ-KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRS 2002
Cdd:NF041483 459 EGERIRGEArREAVQQIEEaartAEELLTKAKADADELRSTaTAESERVRTEAIERATTLRRQAEETLERTRAEAERLRA 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2003 VAEE-AKKQRQIAEEEAARQRAEAEK-ILKEKLTAINEATRLKTEAE-------IALKEKEAENDRLKRKAEEEGYQrkv 2073
Cdd:NF041483 539 EAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEerltaaeEALADARAEAERIRREAAEETER--- 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2074 LEDQAAqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHIlKLNFEKASSGKQelelelkklkgIADETQ 2153
Cdd:NF041483 616 LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAV-RLRSEAAAEAER-----------LKSEAQ 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2154 KSKAkaeeeaekfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE-----------EVGRLMKLAEE--AKKQKE 2220
Cdd:NF041483 677 ESAD---------RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraeadqERERAREQSEEllASARKR 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2221 IAEKEAEKQViLVQEAAQKC----SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAAllhk 2294
Cdd:NF041483 748 VEEAQAEAQR-LVEEADRRAtelvSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEAQ---- 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2295 kaEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELv 2374
Cdd:NF041483 815 --EEADRVRS--------------DAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL- 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2375 kvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKL 2450
Cdd:NF041483 868 ----RSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDE 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2451 LEEEAENMK-KLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEA 2528
Cdd:NF041483 944 ARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEA 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2529 QKLL-EAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEK 2607
Cdd:NF041483 1018 DRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAE 1089
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2608 HTSEKHTVVEK----------------------LEVQRLQSKQEADGLH-KAIADLEKEKEKLKKEAADLQKQSKEManv 2664
Cdd:NF041483 1090 ATVEGNSLVEKartdadellvgarrdatairerAEELRDRITGEIEELHeRARRESAEQMKSAGERCDALVKAAEEQ--- 1166
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2665 QQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKlqsAMDAAIKKQ 2744
Cdd:NF041483 1167 LAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTVEEGKR---ELDVLVRRR 1243
|
1290
....*....|....*...
gi 1207141740 2745 KEAEEEMNGKQKEMQDLE 2762
Cdd:NF041483 1244 EDINAEISRVQDVLEALE 1261
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
228-330 |
1.34e-29 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 115.66 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1737-2329 |
7.81e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.66 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1737 KFKLQAEEAERHLKQA------------ELEKQR---QIQVveEVAKK--TAATQLESKQVALTA----RLEESLKNEQV 1795
Cdd:COG1196 169 KYKERKEEAERKLEATeenlerledilgELERQLeplERQA--EKAERyrELKEELKELEAELLLlklrELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1796 MVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE 1875
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1876 AALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR 1955
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1956 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 2035
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2036 INEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRK-----VLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEET 2110
Cdd:COG1196 487 AEAAARLLLLLE-AEADYEGFLEGVKAALLLAGLRGLagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2111 LKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIADEtqkskakaeEEAEKFRKLALEEEKKRKEAEAKVKQIQAA 2190
Cdd:COG1196 566 LKAAK--AGRATFLPLDKIRARAALAAALARGAIGAAVDLV---------ASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2191 EEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKLKEEFEK 2270
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2271 AKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2329
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
348-447 |
1.01e-27 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 110.07 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 348 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED- 426
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1207141740 427 VDVPHPDEKSIITYVSSMYDV 447
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1535-2154 |
2.94e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.33 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1535 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1614
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1615 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEeihiirlqlettmkQKNTAEtellQLRAKAVDADKLRNAAQEEAE 1694
Cdd:PTZ00121 1294 EAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEE--------------AKKKAD----AAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1695 KLRKQvAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER---HLKQAELEKQRQIQVVEEVAKKTA 1771
Cdd:PTZ00121 1354 AAADE-AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkadELKKAAAAKKKADEAKKKAEEKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1772 ATQLESKqvALTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRlrlqAEEEANKKTA 1851
Cdd:PTZ00121 1433 ADEAKKK--AEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKK----KAEEAKKKAD 1500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1852 aqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlddelq 1931
Cdd:PTZ00121 1501 --------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-------- 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1932 rlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 2011
Cdd:PTZ00121 1559 --KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2012 QIAEEEA--------ARQRAEAEKILKEKLTAINEATRLKTE-----------AEIALKEKEAEN---DRLKRKAEEEgy 2069
Cdd:PTZ00121 1637 QLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEeakkaeedekkAAEALKKEAEEAkkaEELKKKEAEE-- 1714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2070 QRKVLEDQAAQHKQAIeeKIGQLKKSSDTELDRQKKIVEETLKQRKV----VEEEIHILKLNFEKASSGKQELELELKKL 2145
Cdd:PTZ00121 1715 KKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlkKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
....*....
gi 1207141740 2146 KGIADETQK 2154
Cdd:PTZ00121 1793 RMEVDKKIK 1801
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
330-445 |
3.22e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 109.40 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 330 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAF 409
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141740 410 SIAERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
228-330 |
4.06e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 108.34 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
221-332 |
1.15e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 107.92 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 221 RIADERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLK 297
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1207141740 298 HR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21247 92 TKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1535-2119 |
1.30e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.40 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1535 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1614
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1615 IQRELQELKTLSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNA-----A 1689
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEA---KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelkkA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1690 QE--EAEKLRK----QVAEETQKK----RKAEE------ELKRKSEAEKD----AAKEKKKALEDLEKFKLQAEEAERHL 1749
Cdd:PTZ00121 1287 EEkkKADEAKKaeekKKADEAKKKaeeaKKADEakkkaeEAKKKADAAKKkaeeAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1750 KQAELEKQRQIQVVEEVAKKT----AATQLESKQVALTARLEESLKNEQVmviqlQEEAEHLKKQQAE---ADKAREQAE 1822
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAeekkKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEkkkADEAKKKAE 1441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1823 --KELETWRQKANEALR---LRLQAEE-----EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR 1892
Cdd:PTZ00121 1442 eaKKADEAKKKAEEAKKaeeAKKKAEEakkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1893 KMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQrlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET 1972
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKA--EELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1973 MSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRaEAEKILKE----KLTAINEATRLKTEAEI 2048
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAeeenKIKAAEEAKKAEEDKKK 1676
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2049 ALKEKEAENDrlKRKAEEEGYQRKVLEDQAAQHKQAIEE---KIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 2119
Cdd:PTZ00121 1677 AEEAKKAEED--EKKAAEALKKEAEEAKKAEELKKKEAEekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
228-333 |
1.42e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.42 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1564-2129 |
1.97e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 120.04 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1564 AELEKQ-KQLAEthaKAiAKAEQeANELKTKMKDevsKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALL 1642
Cdd:COG1196 196 GELERQlEPLER---QA-EKAER-YRELKEELKE---LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1643 SRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEK 1722
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1723 DAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQE 1802
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLE----RLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1803 EAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1882
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1883 AAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1962
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1963 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEakkqRQIAEEEAARQRAEAEKILKEKLTAINEATRL 2042
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2043 KTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIH 2122
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
....*..
gi 1207141740 2123 ILKLNFE 2129
Cdd:COG1196 737 LLEELLE 743
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
332-445 |
6.44e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 105.55 E-value: 6.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 332 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 412 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
350-445 |
1.09e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 104.16 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 350 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 428
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1207141740 429 VPHPDEKSIITYVSSMY 445
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
332-445 |
2.72e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 103.65 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 332 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 412 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1695-2599 |
1.09e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.38 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1695 KLRKqvaEETQKK-RKAEEELKRkseaekdAAKEKKKALEDLEKFKLQAEEAERH--LKQAELEKQRQIQVVEEVAKKTA 1771
Cdd:TIGR02168 171 KERR---KETERKlERTRENLDR-------LEDILNELERQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1772 ATQLESKQvaltARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEA-LRLRLQAEEEANkkt 1850
Cdd:TIGR02168 241 LEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLAN--- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1851 aaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDEL 1930
Cdd:TIGR02168 314 ------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1931 QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEketmsnTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQ 2010
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ------QEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2011 RQIAEEEAARQRAEaekilkekltaINEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKVLedQAAQHKQAIEEKI 2089
Cdd:TIGR02168 456 LERLEEALEELREE-----------LEEAEQALDAAERELAQLQARLDSLERLQENlEGFSEGVK--ALLKNQSGLSGIL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2090 GQLKKSSDTELDRQKKIV---EETLKQRKVVEEEIHILKLNF-EKASSGKQELELELKKLkgiADETQKSKAKAEEEAEK 2165
Cdd:TIGR02168 523 GVLSELISVDEGYEAAIEaalGGRLQAVVVENLNAAKKAIAFlKQNELGRVTFLPLDSIK---GTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2166 FRKLALEEEKKRKEAEAK----------VKQIQAAEEEAARQH---------------------KAAQEEVGRLMKLAEE 2214
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2215 AKKQKEIAekeaekqvilvqEAAQKCSAAEQKAQNVLVQqnkdsmaQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHK 2294
Cdd:TIGR02168 680 EELEEKIE------------ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2295 KAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2374
Cdd:TIGR02168 741 EVEQLEE--------------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2375 KVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkdkdntKKLLEEE 2454
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------------------AAEIEEL 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2455 AENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA 2534
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2535 KKEMQQRLDQETEGFQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2599
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1865-2551 |
1.21e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.26 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1865 REAKK----RAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1940
Cdd:COG1196 207 RQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1941 VKQKKELEEELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 2020
Cdd:COG1196 287 QAEEYELLAELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2021 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLKKSSDTEL 2100
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA-------LLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2101 DRQKKIVEETLKQRKVVEEEIHILKLnfekassgkqelelelkklkgIADETQKskakaeeeaekfRKLALEEEKKRKEA 2180
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLEL---------------------LAELLEE------------AALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2181 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEkeaEKQVILVQEAAQKCSAAEQKAQNVLvqqnkdsma 2260
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---LIGVEAAYEAALEAALAAALQNIVV--------- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2261 qdklkeefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAA 2340
Cdd:COG1196 554 --------EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2341 ALklkQEADSEMAKYkkLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2420
Cdd:COG1196 626 TL---VAARLEAALR--RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2421 QMEDLLKLKLKIEKENQELmKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEK 2500
Cdd:COG1196 701 AEEEEERELAEAEEERLEE-ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2501 K----QAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA----KKEMQQRLdQET-----EGFQK 2551
Cdd:COG1196 780 GpvnlLAIEEYEELEERYDFLSEQREDLEEARETLEEAieeiDRETRERF-LETfdavnENFQE 842
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
346-445 |
1.91e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 100.71 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 346 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 425
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1207141740 426 D-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1323-2048 |
2.12e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 114.08 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1323 EASQTQLQKLRSEAEGKQATFD----RLEEELQRATEVNKRMSQLHSERDVELEHYRQlVGNLRERWQAVFAQ----IEL 1394
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKaedaRKAEEARKAEDARKAEEARKAEDAKRVEIARK-AEDARKAEEARKAEdakkAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1395 RQRELDLlnRQMQAYRESYDwlIRWIADAKQRQDKLHAVPIggSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKfakgyid 1474
Cdd:PTZ00121 1181 ARKAEEV--RKAEELRKAED--ARKAEAARKAEEERKAEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEE------- 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1475 aIKDYELQLVTYKALVEPIASPLKKAKMESAsddiiqeyvtlrtRYSELMTLSsqyikfiiETQRRLQDEEKAAEKLKEE 1554
Cdd:PTZ00121 1248 -ERNNEEIRKFEEARMAHFARRQAAIKAEEA-------------RKADELKKA--------EEKKKADEAKKAEEKKKAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1555 ERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANElkTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQ----EI 1630
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE--AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkadAA 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1631 KAKSQQVEEALLSRTRIEEEihiirLQLETTMKQKNTAETELLQLRAKAVD---ADKLRNAAQE--EAEKLRKQvAEETQ 1705
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEED-----KKKADELKKAAAAKKKADEAKKKAEEkkkADEAKKKAEEakKADEAKKK-AEEAK 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1706 K----KRKAEE-----ELKRKSEAEKDAAKEKKKAledlEKFKLQAEEAERhlKQAELEKQRQIQVVEEVAKKTAATQLE 1776
Cdd:PTZ00121 1458 KaeeaKKKAEEakkadEAKKKAEEAKKADEAKKKA----EEAKKKADEAKK--AAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1777 SKQVAltarlEESLKNEQVMVIQLQEEAEHLKKqqAEADKAREQAEKELE---TWRQKANEALRLRLQAEEEANKKTAAQ 1853
Cdd:PTZ00121 1532 EAKKA-----DEAKKAEEKKKADELKKAEELKK--AEEKKKAEEAKKAEEdknMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1854 EEAEKQKEEAKREAKKRA----KAEE-----AALKQKEAAEMELGNQRKMAEETAKQKlaAEQELIRLRADFEHAEQQRT 1924
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAeelkKAEEekkkvEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKK 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1925 VLDDELQRLKNDVNSAVKQKKelEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVA 2004
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKK--AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141740 2005 EEAKKQRQIAEEeaarQRAEAEKILKEKLTAINEATRLKTEAEI 2048
Cdd:PTZ00121 1761 HLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
232-329 |
2.27e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 100.08 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 232 KTFTKWVNKHLVKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 307
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1207141740 308 NDDIADGnPKLTLGLIWTIILH 329
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
345-445 |
3.09e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 100.19 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 424
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1207141740 425 EDV---DVphPDEKSIITYVSSMY 445
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
332-445 |
4.21e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 100.53 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 332 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 412 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
344-450 |
6.68e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 99.28 E-value: 6.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 344 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY--RQTNLENLEQAFSIAERDLGVTR 420
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1207141740 421 -LLDPEDVDvpHPDEKSIITYVSSMYDVMPR 450
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
229-332 |
8.12e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 98.90 E-value: 8.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 229 VQKKTFTKWVNKHLVKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 304
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
990-1056 |
8.12e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 97.33 E-value: 8.12e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 990 QLKPRNpaQPIKGKLPVQAVCDFKQMEITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSICFIVP 1056
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
345-449 |
1.71e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.94 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1207141740 425 EDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1984-2868 |
3.49e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 109.68 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1984 ESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRK 2063
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2064 AEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 2143
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2144 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2223
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2224 KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQE-AEKAKDNAEKEAALLHKKAEEAERQ 2302
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2303 kkaaeaeaakqakaqedaEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDE 2382
Cdd:pfam02463 471 ------------------EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2383 tDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLA 2462
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2463 E-EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQR 2541
Cdd:pfam02463 612 TlEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2542 LDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEV 2621
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE---EEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2622 QRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQ--EKTILQQSFFAEKETLLKKEKAIEEEKK 2699
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEeeQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2700 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQsamdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNL 2779
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQK-------LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2780 REKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGvKKDVPLAFDGIREKVPASRLHEIGVLS 2859
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERL 1000
|
....*....
gi 1207141740 2860 KKEYDKLKK 2868
Cdd:pfam02463 1001 EEEKKKLIR 1009
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1815-2674 |
6.25e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 108.91 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1815 DKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1894
Cdd:pfam02463 168 KRKKKEALKKL---IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1895 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNdvnsavKQKKELEEELIKVRKEMEILLQQKSKAEKETmS 1974
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE------EELKLLAKEEEELKSELLKLERRKVDDEEKL-K 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1975 NTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 2054
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2055 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSG 2134
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2135 KQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGrlmKLAEE 2214
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV---IVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2215 AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAlLHK 2294
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK-DTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2295 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2374
Cdd:pfam02463 634 LTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2375 KVKVQLDETDKQKsvLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE 2454
Cdd:pfam02463 714 KLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2455 A-ENMKKLAEEAARLNIEAQEAA---RLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQK 2530
Cdd:pfam02463 792 KeEKLKAQEEELRALEEELKEEAellEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2531 LLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE-TEKHT 2609
Cdd:pfam02463 872 LLLKEEELEE-QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEaDEKEK 950
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2610 SEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2674
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEET 1015
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
348-448 |
6.28e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 96.38 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 348 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPEDV 427
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1207141740 428 DVPHPDEKSIITYVSSMYDVM 448
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1919-2782 |
8.55e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 108.52 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1919 AEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS-----KAEKETMSNTEKSKQL--LESEAAKMR 1991
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkEQAKKALEYYQLKEKLelEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1992 ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI-LKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 2070
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2071 RKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIAD 2150
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2151 ETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQV 2230
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2231 ILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEfEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEA 2310
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS-GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2311 AKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKL-------AEKTLKQKSSVEEELVKVKVQLDET 2383
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpilnLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2384 DKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEkenQELMKKDKDNTKKLLEEEAENMKKLAE 2463
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ---ELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2464 EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ-KLLEAKKEMQQRL 2542
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKeKELAEEREKTEKL 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2543 DQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2622
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2623 RLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLE 2702
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI------EERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2703 KQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDA-AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2781
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLmAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
.
gi 1207141740 2782 K 2782
Cdd:pfam02463 1021 E 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2257-2835 |
1.34e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 107.92 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2257 DSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAallhKKAEEAERQKKAAEAEAAKQAkaqedAEKLRK-E----AEKEA 2331
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEA----RKAEEAKKKAEDARKAEEARK-----AEDARKaEearkAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2332 SRRAEAEAAALKLKQEA-DSEMAKYKKLAEKTLKQKSSVE----EELVKVKV--------QLDETDKQKSVLDVELKRLK 2398
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEArKAEDAKKAEAARKAEEVRKAEElrkaEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2399 QEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKEN----QELMKKDK----DNTKKLLEEEAENMKKLAEEAARLNI 2470
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADElkkaEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2471 EAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQrLDQETEGFQ 2550
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2551 KSLEAERKRQlEITAEAEKLKVKvtqlSDAQSKAEEEAKKF--KKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2628
Cdd:PTZ00121 1392 KADEAKKKAE-EDKKKADELKKA----AAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2629 EadglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE--QLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFE 2706
Cdd:PTZ00121 1467 E----EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2707 DEVKKAEALKAEQERQRKlmeEERKKLQSAmdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLReklqql 2786
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKA---EEKKKAEEA-----KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK------ 1608
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1207141740 2787 qsSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGVKKD 2835
Cdd:PTZ00121 1609 --AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1511-2301 |
2.04e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.06 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1511 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEkqkqlaeTHAKAIAKAEQEANE 1589
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1590 LKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1669
Cdd:TIGR02168 286 LQKELYALANEISRL----EQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1670 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledlekfklqaeeAERHL 1749
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------------------------LEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1750 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1829
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1830 QKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKAEEAALKQK 1881
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKKAIAFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1882 E---AAEMELGNQRKMAEETAKQKLAAEQELIRLRADF--EHAEQQRTVLDDELQRLK--NDVNSAVKQKKELEEELIKV 1954
Cdd:TIGR02168 569 ElgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1955 RKEMEILLQQKS---KAEKETMSNTEKSKQLLESEaAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 2031
Cdd:TIGR02168 649 TLDGDLVRPGGVitgGSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2032 KLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEdQAAQHKQAIEEKIGQLKKssdtELDRQKKIVEETL 2111
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEA----QIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2112 KQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAAE 2191
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA--------------EIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2192 EEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEF-EK 2270
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEE 948
|
810 820 830
....*....|....*....|....*....|.
gi 1207141740 2271 AKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2301
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
228-333 |
3.80e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 95.15 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
228-333 |
5.41e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.77 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1737-2627 |
5.95e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1737 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKktaatQLES--KQVALTARLEEslkneqvmviqLQEEAEHLKKQQAEA 1814
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELER-----QLKSleRQAEKAERYKE-----------LKAELRELELALLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1815 DKarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELgnqrkm 1894
Cdd:TIGR02168 233 RL--EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1895 aEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtms 1974
Cdd:TIGR02168 305 -QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ--- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1975 ntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIALKEK 2053
Cdd:TIGR02168 381 --------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2054 EAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLkkssdteldrqkkiveETLKQRKVVEEEihiLKLNFEKASS 2133
Cdd:TIGR02168 453 QEELERLEEALEE-------LREELEEAEQALDAAEREL----------------AQLQARLDSLER---LQENLEGFSE 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2134 GKQELELELKKLKGIADETQKSKAKAEEEaekfrKLALEEEKKRKEAEAKVKQIQAAEEEAARQhkaAQEEVGRLMKLAE 2213
Cdd:TIGR02168 507 GVKALLKNQSGLSGILGVLSELISVDEGY-----EAAIEAALGGRLQAVVVENLNAAKKAIAFL---KQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2214 EAKKQKEIAEKEAE--KQVILVQEAAQKCSAAEQKAQ--------NVLVQQNKDSmAQDKLKEEFEKAKKLAQEAEK--- 2280
Cdd:TIGR02168 579 DSIKGTEIQGNDREilKNIEGFLGVAKDLVKFDPKLRkalsyllgGVLVVDDLDN-ALELAKKLRPGYRIVTLDGDLvrp 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2281 ----AKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedaeklRKEAEKeasrraeaeaaalKLKQEADSEMAKYK 2356
Cdd:TIGR02168 658 ggviTGGSAKTNSSILERRRE--------------------------IEELEE-------------KIEELEEKIAELEK 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2357 KLAEkTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQME------DLLKLKL 2430
Cdd:TIGR02168 699 ALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEeleerlEEAEEEL 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2431 KIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKL 2510
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2511 KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ---ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2587
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1207141740 2588 AKKFKKQ-ADEIKIRLQETEKHTSEKHTVVEKLE--VQRLQSK 2627
Cdd:TIGR02168 938 IDNLQERlSEEYSLTLEEAEALENKIEDDEEEARrrLKRLENK 980
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
345-443 |
7.66e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 93.07 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY-RQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1207141740 424 PEDVDVPHPDEKSIITYVSS 443
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1578-2456 |
9.64e-22 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 105.05 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1578 KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrtRIEEEIHIIRLQ 1657
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK-----EEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1658 LETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEK 1737
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE-KEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1738 FKLQAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKqqaEADKA 1817
Cdd:pfam02463 354 EEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK---EEKKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1818 REQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEE 1897
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1898 TAKQKLAAEQELIRLRADFEHAEQQR---TVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL-QQKSKAEKETM 1973
Cdd:pfam02463 508 GLKVLLALIKDGVGGRIISAHGRLGDlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgARKLRLLIPKL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1974 SNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALKEK 2053
Cdd:pfam02463 588 KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES-GLRKGVSLEEGLAEKSEVKA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2054 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIgqlKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKass 2133
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIK---KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL--- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2134 gkqelelelkKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEvgrlmKLAE 2213
Cdd:pfam02463 741 ----------LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE-----ELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2214 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA-KDNAEKEAALL 2292
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2293 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKssVEEE 2372
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE--ERNK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2373 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE 2452
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELG 1043
|
....
gi 1207141740 2453 EEAE 2456
Cdd:pfam02463 1044 GSAE 1047
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1511-2348 |
2.13e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 103.90 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1511 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1590
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1591 KTKMKDEVSK---RQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNT 1667
Cdd:pfam02463 246 LRDEQEEIESskqEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1668 AETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1747
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1748 HlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ------LQEEAEHLKKQQAEADKAREQA 1821
Cdd:pfam02463 406 E-AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelkllkDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1822 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR-AKAEEAALKQKEAAEMELGNQRKMAEETAK 1900
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1901 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND--VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEK 1978
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1979 SKQLLESEAAkMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEK-EAE 2056
Cdd:pfam02463 645 ESGLRKGVSL-EEGLAEKSEVKASLSELTKELLEIQELqEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2057 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ---LKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 2133
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKkeeKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2134 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2213
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2214 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKaqNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2293
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKE--NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2294 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEA 2348
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1536-2618 |
2.61e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 103.75 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1536 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK-QKQLAETHAKAIAKAEQeANELKTKMKdevskrqdvavdsekqKHN 1614
Cdd:NF041483 251 QARRQAAELSRAAEQRMQEAEEALREARAEAEKvVAEAKEAAAKQLASAES-ANEQRTRTA----------------KEE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1615 IQRELQELKTLSEQeIKAKSQQVeealLSRTRIEEEihiiRLQLETTMKQKN-TAETELLQLRAKAVDADKLRNAAQEEA 1693
Cdd:NF041483 314 IARLVGEATKEAEA-LKAEAEQA----LADARAEAE----KLVAEAAEKARTvAAEDTAAQLAKAARTAEEVLTKASEDA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1694 EKLRKQVAEETQK-KRKAEEELKRkseaekdaakekkkaledlekFKLQAEEAERHLKQAELE--KQRQIQVVE--EVAK 1768
Cdd:NF041483 385 KATTRAAAEEAERiRREAEAEADR---------------------LRGEAADQAEQLKGAAKDdtKEYRAKTVElqEEAR 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1769 KT--AATQLESKQVALTARLEESLKNEQVMviQLQEEA----EHLKKQQAEADKAREQAEKELETWRQKANE-ALRLRLQ 1841
Cdd:NF041483 444 RLrgEAEQLRAEAVAEGERIRGEARREAVQ--QIEEAArtaeELLTKAKADADELRSTATAESERVRTEAIErATTLRRQ 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1842 AEEEANkktaaqeeaekqkeeakreaKKRAKAEEaalkqkeaaemelgnQRKMAEETA-KQKLAAEQELIRLRADFEHA- 1919
Cdd:NF041483 522 AEETLE--------------------RTRAEAER---------------LRAEAEEQAeEVRAAAERAARELREETERAi 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1920 EQQRTVLDDELQRLKNDVNSAVKQKkelEEELIKVRKEMEILlqqkskaEKETMSNTEKskqlLESEAA-KMRELAEEAT 1998
Cdd:NF041483 567 AARQAEAAEELTRLHTEAEERLTAA---EEALADARAEAERI-------RREAAEETER----LRTEAAeRIRTLQAQAE 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1999 klrsvaEEAKKQRQIAEEEAARQRAEAEkilkekltaiNEATRLKTEAeialkekEAENDRLKRKAEEEGyQRKVLEDQA 2078
Cdd:NF041483 633 ------QEAERLRTEAAADASAARAEGE----------NVAVRLRSEA-------AAEAERLKSEAQESA-DRVRAEAAA 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2079 AQHKQAIEEkiGQLKKSSDTELDRQKKIVEETLkqrkvveeeihilklnfekassgkqelelelkklkgiadetqkskak 2158
Cdd:NF041483 689 AAERVGTEA--AEALAAAQEEAARRRREAEETL----------------------------------------------- 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2159 aeeeaekfrklaleeekkrkeaeakvkqiQAAEEEAARQHKAAQEEVGRLMklaeeAKKQKEIAEKEAEKQViLVQEAAQ 2238
Cdd:NF041483 720 -----------------------------GSARAEADQERERAREQSEELL-----ASARKRVEEAQAEAQR-LVEEADR 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2239 KC----SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAallhkkAEEAERqkkaaeaeaak 2312
Cdd:NF041483 765 RAtelvSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEA------QEEADR----------- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2313 qakAQEDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELvkvkvQLDETDKQKSVLDV 2392
Cdd:NF041483 820 ---VRSDAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL-----RSDASEYAQRVRTE 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2393 ELKRLKQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMK-KLAEEAAR 2467
Cdd:NF041483 882 ASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQ 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2468 LNIEAQ-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEAQKLL-EAKKEMQQRLDQE 2545
Cdd:NF041483 962 LIAEATgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEADRTLdEARKDANKRRSEA 1035
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141740 2546 TEGFQKSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEKHTSEKHTVVEK 2618
Cdd:NF041483 1036 AEQADTLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAEATVEGNSLVEK 1100
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1735-2668 |
3.59e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.98 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1735 LEKFKLQAEE----AERHLKQAELEKQRQIQvveEVAKKTAATQLESKQVALTARLE------------ESLKNEQVM-V 1797
Cdd:NF041483 78 LRNAQIQADQlradAERELRDARAQTQRILQ---EHAEHQARLQAELHTEAVQRRQQldqelaerrqtvESHVNENVAwA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1798 IQLQEEAEH-----LKKQQAEADK----AREQAEKELETWRQK-ANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1867
Cdd:NF041483 155 EQLRARTESqarrlLDESRAEAEQalaaARAEAERLAEEARQRlGSEAESARAEAEAILRRARKDAERLLNAASTQAQEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1868 KKRAK------AEEAALKQKEAAEMELGNQRKMAE-ETAKQKLAAEQELIRLRAD---------FEHAEQQRT-VLDDEL 1930
Cdd:NF041483 235 TDHAEqlrsstAAESDQARRQAAELSRAAEQRMQEaEEALREARAEAEKVVAEAKeaaakqlasAESANEQRTrTAKEEI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1931 QRLkndVNSAVKQ----KKELEEELIKVRKEMEILLQQ-----KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATklR 2001
Cdd:NF041483 315 ARL---VGEATKEaealKAEAEQALADARAEAEKLVAEaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKATT--R 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2002 SVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAI---------------NEATRLKTEAEIALKEKEAENDRLKRKAEE 2066
Cdd:NF041483 390 AAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAEAVAEGERIRGEARR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2067 EGYQR---------------KVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQkkiVEETLkQRKVVEEEihilKLNFEKA 2131
Cdd:NF041483 470 EAVQQieeaartaeelltkaKADADELRSTATAESERVRTEAIERATTLRRQ---AEETL-ERTRAEAE----RLRAEAE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2132 SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRL-MK 2210
Cdd:NF041483 542 EQAEEVRAAAERAARELREETERAIAARQAEAA--EELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrTE 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2211 LAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEF-EKAKKLAQEAEKAKDNAEKE 2288
Cdd:NF041483 620 AAERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAVRLRSEAAAEaERLKSEAqESADRVRAEAAAAAERVGTE 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2289 AA-LLHKKAEEAERQkkaaeaeaakqakaqedaeklRKEAEKEASRRaeaeaaalklKQEADSEMAKYKKLAEKTLKQ-K 2366
Cdd:NF041483 697 AAeALAAAQEEAARR---------------------RREAEETLGSA----------RAEADQERERAREQSEELLASaR 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2367 SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQ-KAQVEDELS-----------KVKIQMEDLLKLKLKIEK 2434
Cdd:NF041483 746 KRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGlQEQAEEEIAglrsaaehaaeRTRTEAQEEADRVRSDAY 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2435 ENQELMKKDKDNTKKLLEEEAENMKKLAE--------EAARLNIEAQE-AARLRQIAESDLAKQRELAEKMLEEkkqAIQ 2505
Cdd:NF041483 826 AERERASEDANRLRREAQEETEAAKALAErtvseaiaEAERLRSDASEyAQRVRTEASDTLASAEQDAARTRAD---ARE 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2506 EAAKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLE-----ITAEAEKLKVKVTQ-LS 2578
Cdd:NF041483 903 DANRIRSDaAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEqliaeATGEAERLRAEAAEtVG 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2579 DAQSKAE---EEAKKFKKQADEikirlqETEKHTSEKHTVVEKL--EVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2653
Cdd:NF041483 983 SAQQHAErirTEAERVKAEAAA------EAERLRTEAREEADRTldEARKDANKRRSEAAEQADTLITEAAAEADQLTAK 1056
|
1050
....*....|....*
gi 1207141740 2654 LQKQSKEMANVQQEQ 2668
Cdd:NF041483 1057 AQEEALRTTTEAEAQ 1071
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
349-447 |
4.08e-21 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 91.26 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 349 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 427
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141740 428 DVPHPDEKSIITYVSSMYDV 447
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1333-2046 |
1.09e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.17 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1333 RSEAEGK-QATFDRLEEELQRATEVNKRMSQLHSERDVeLEHYRQLVGNLRERwqavfaQIELRQRELDLLNRQMQAyre 1411
Cdd:COG1196 174 KEEAERKlEATEENLERLEDILGELERQLEPLERQAEK-AERYRELKEELKEL------EAELLLLKLRELEAELEE--- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1412 sydwlirwiadakqrqdklhavpiggskgLQEQLTQEKKLLEEIEKNKDKVEDcqkfakgyidaikdyelqlvtykalve 1491
Cdd:COG1196 244 -----------------------------LEAELEELEAELEELEAELAELEA--------------------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1492 piasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEErkkmAEMQAELEKQKQ 1571
Cdd:COG1196 268 ------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1572 LAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEI 1651
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1652 HIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKA 1731
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1732 LEDLEKFKLQAEEA-ERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKneqvmviQLQEEAEHLKKQ 1810
Cdd:COG1196 497 LEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE-------VAAAAIEYLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1811 QA--------EADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1882
Cdd:COG1196 570 KAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1883 AAEMELGNQRKMAEETAKQKLAAEQELIRLRAdfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1962
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL--EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1963 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI-------AEEEAARQRAEAEKILKEK--- 2032
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQRedl 807
|
730 740
....*....|....*....|.
gi 1207141740 2033 -------LTAINEATRLKTEA 2046
Cdd:COG1196 808 eearetlEEAIEEIDRETRER 828
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
345-442 |
6.24e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 87.92 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 424
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90
....*....|....*....
gi 1207141740 425 ED-VDVPHPDEKSIITYVS 442
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLC 98
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1318-2132 |
7.26e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 98.89 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1318 NEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQavfAQIELRQR 1397
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ---ELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1398 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1477
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1478 dyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDE-----------EK 1546
Cdd:pfam02463 332 --KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElelkseeekeaQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1547 AAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvavdSEKQKHNIQRELQELKTLS 1626
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-----ELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1627 EQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR-KQVAEETQ 1705
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAtADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1706 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTAR 1785
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1786 LEESLKNEQVMV---------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKktaaqEEA 1856
Cdd:pfam02463 645 ESGLRKGVSLEEglaeksevkASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLK-----LEA 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1857 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1936
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1937 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN-------------TEKSKQLLESEAAKMRELAEEATKLRSV 2003
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELalelkeeqkleklAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2004 AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaEEEGYQRKVLEDQAAQHKQ 2083
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE--ELLLEEADEKEKEENNKEE 957
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1207141740 2084 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 2132
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2262-2810 |
8.23e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.47 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2262 DKLKEEFEKAKK---LAQEAEKAK--------DNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKE 2330
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2331 ASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ 2410
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2411 VEDELSKVKIQMEDLLKLKLKIEKENQELMkKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQR 2490
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEAL-RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2491 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDqetegfqksLEAERKRQLEITAEAEKL 2570
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---------LLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2571 KVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEAdglhKAIADLEKEKEKLKKE 2650
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG----RATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2651 AADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEER 2730
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2731 KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEEL 2810
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1536-2423 |
1.24e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.97 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1536 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK---------QKQLAETHAKAIAKAEQEANELKTKMKDEVSK------ 1600
Cdd:NF041483 313 EIARLVGEATKEAEALKAEAEQALADARAEAEKlvaeaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKAttraaa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1601 ------RQDVAVDSEK---QKHNIQRELQELKTLSEQEIKAKSQQV-EEALLSRTRIEE-------EIHIIRLQLETTMK 1663
Cdd:NF041483 393 eeaeriRREAEAEADRlrgEAADQAEQLKGAAKDDTKEYRAKTVELqEEARRLRGEAEQlraeavaEGERIRGEARREAV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1664 QK-----NTAEtELLQlRAKAvDADKLRNAAQEEAEKLRKQVAEE-TQKKRKAEEELKRKSEAEKDAAKEKKKALedlEK 1737
Cdd:NF041483 473 QQieeaaRTAE-ELLT-KAKA-DADELRSTATAESERVRTEAIERaTTLRRQAEETLERTRAEAERLRAEAEEQA---EE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1738 FKLQAEEAERHLKQaELEK---QRQIQVVEEVAKK--TAATQLESKQVALT-ARLE-ESLKNEQVmviqlqEEAEHLKKQ 1810
Cdd:NF041483 547 VRAAAERAARELRE-ETERaiaARQAEAAEELTRLhtEAEERLTAAEEALAdARAEaERIRREAA------EETERLRTE 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1811 QAEADKA-REQAEKELETWRQKA------------NEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR------- 1870
Cdd:NF041483 620 AAERIRTlQAQAEQEAERLRTEAaadasaaraegeNVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvgteaae 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1871 --AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELI---RLRADFEHAEQQRTVldDELQRLKNDVNSAVKQ-- 1943
Cdd:NF041483 700 alAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQRLV--EEADRRATELVSAAEQta 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1944 ----------KKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLESEAAKMRELA-EEATKLRSVA-EEAKKQR 2011
Cdd:NF041483 778 qqvrdsvaglQEQAEEEIAGLRSAAE-------HAAERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAK 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2012 QIAEEEAARQRAEAEKILKEkltAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGyqRKVLEDQAAQHKQAIEEKIGQ 2091
Cdd:NF041483 851 ALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDA--NRIRSDAAAQADRLIGEATSE 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2092 LKKSSDTELDRQKKIVEETLKQRKvveeeihilKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLAl 2171
Cdd:NF041483 926 AERLTAEARAEAERLRDEARAEAE---------RVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEA- 995
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2172 eeekkrkeaeakvKQIQA-AEEEAARQHKAAQEEVGRLMKLAEE--AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQ 2248
Cdd:NF041483 996 -------------ERVKAeAAAEAERLRTEAREEADRTLDEARKdaNKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2249 NVLV--QQNKDSMAQDKLKEefekAKKLAQEA--------EKAKDNAE-------KEAALLHKKAEEAeRQKKAAEAEAA 2311
Cdd:NF041483 1063 RTTTeaEAQADTMVGAARKE----AERIVAEAtvegnslvEKARTDADellvgarRDATAIRERAEEL-RDRITGEIEEL 1137
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2312 KQAKAQEDAEKLRKEAEK-------EASRRAEAEAAALKLKQEADSEMAKYK----KLAEKTLKQKSSVEEELVKvkvql 2380
Cdd:NF041483 1138 HERARRESAEQMKSAGERcdalvkaAEEQLAEAEAKAKELVSDANSEASKVRiaavKKAEGLLKEAEQKKAELVR----- 1212
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*..
gi 1207141740 2381 dETDKQKSVLDVELKRL----KQEVSDAIKQKAQVEDELSKVKIQME 2423
Cdd:NF041483 1213 -EAEKIKAEAEAEAKRTveegKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
345-445 |
2.68e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 85.86 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1207141740 425 EDVDV--PHPDEKSIITYVSSMY 445
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
230-330 |
3.53e-19 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 85.71 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 230 QKKTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 305
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1207141740 306 IRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
345-441 |
4.13e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 85.67 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 424
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90
....*....|....*...
gi 1207141740 425 ED-VDVPHPDEKSIITYV 441
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYL 97
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
341-448 |
4.61e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 85.38 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 341 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 420
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1207141740 421 LLDPEDV-DVPHPDEKSIITYVSSMYDVM 448
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
348-444 |
5.65e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.06 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 348 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN----LENLEQAFSIAERDLGVTRLLD 423
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1207141740 424 PEDVDVPHPDEKSIITYVSSM 444
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1319-1964 |
1.01e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.12 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1319 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRE 1398
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1399 LDLLNRQMQAYRE----SYDWLIRWIADAKQRQDKLHAVPIggsKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYID 1474
Cdd:TIGR02168 395 IASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAEL---KELQAELEELEEELEELQEELERLEEALEELREELE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1475 ----AIKDYELQLVTYKALV--------------EPIASPLKKAKMESASDDIIQEYVTLRTRYS------------ELM 1524
Cdd:TIGR02168 472 eaeqALDAAERELAQLQARLdslerlqenlegfsEGVKALLKNQSGLSGILGVLSELISVDEGYEaaieaalggrlqAVV 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1525 TLSSQYIKFIIETQRRlQDEEKAA-----EKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAE--------------- 1584
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQ-NELGRVTflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdd 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1585 -QEANELKTKMK----------DEVSKRQDVAVDSEKQKHNIQ------RELQELKTLSEQEIKAKSQQVEEALLSRTRI 1647
Cdd:TIGR02168 631 lDNALELAKKLRpgyrivtldgDLVRPGGVITGGSAKTNSSILerrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1648 EEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE 1727
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1728 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT--------ARLEESLKNEQVMVIQ 1799
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelsediESLAAEIEELEELIEE 870
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1800 LQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTaaqeeaekQKEEAKREAKKRAKAEEAALK 1879
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR--------EKLAQLELRLEGLEVRIDNLQ 942
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1880 QK--EAAEMELGNQRKMAEETAKQKLAAEQELIRLR--------------ADFEHAEQQRtvldDELQRLKNDVNSAVKQ 1943
Cdd:TIGR02168 943 ERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEnkikelgpvnlaaiEEYEELKERY----DFLTAQKEDLTEAKET 1018
|
730 740
....*....|....*....|.
gi 1207141740 1944 kkeLEEELIKVRKEMEILLQQ 1964
Cdd:TIGR02168 1019 ---LEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1700-2574 |
1.09e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 94.75 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1700 VAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-QAELEKQRQIQVVEEvaKKTAATQLESK 1778
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAlLKEKREYEGYELLKE--KEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1779 QVALtARLEESLKneqvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRLRLQAEEEANKKTAAQEEAEK 1858
Cdd:TIGR02169 243 ERQL-ASLEEELE-------KLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1859 QKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1938
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1939 SAVKQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATklrSVAEEAKKQRQIAEEEA 2018
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEEL----ADLNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2019 ArQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ--------------AAQHKQA 2084
Cdd:TIGR02169 462 A-DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtvaqlgsvGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2085 IEEKIGQLKKS--SDTELDRQKKIveETLKQRKVveEEIHILKLNfEKASSGKQELELELKKLKGIA-------DETQKS 2155
Cdd:TIGR02169 541 IEVAAGNRLNNvvVEDDAVAKEAI--ELLKRRKA--GRATFLPLN-KMRDERRDLSILSEDGVIGFAvdlvefdPKYEPA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2156 KAKAEEEAEKFRKLALEEEKKRK-----------EAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEK 2224
Cdd:TIGR02169 616 FKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2225 EAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkk 2304
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE--- 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2305 aaeaeaakqakaqeDAEKLRKEAEKEASRraeaeaaalklkqEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETD 2384
Cdd:TIGR02169 773 --------------DLHKLEEALNDLEAR-------------LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2385 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnMKKLAEE 2464
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ-LRELERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2465 AARLNIEAQEA-ARLRQIAESDLAKQRELAEkmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-------LEAKK 2536
Cdd:TIGR02169 905 IEELEAQIEKKrKRLSELKAKLEALEEELSE--IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALepvnmlaIQEYE 982
|
890 900 910
....*....|....*....|....*....|....*...
gi 1207141740 2537 EMQQRLDqETEGFQKSLEAERKRQLEITAEAEKLKVKV 2574
Cdd:TIGR02169 983 EVLKRLD-ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
231-328 |
1.59e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.85 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 231 KKTFTKWVNKHL-VKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 306
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1207141740 307 RNDDI-ADGNPKLTLGLIWTIIL 328
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1976-2639 |
3.55e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1976 TEKSKQL--LESEAAKmrelAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLtainEATRLKTEAEIALKEK 2053
Cdd:COG1196 196 GELERQLepLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2054 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKigqlkkssdtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 2133
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2134 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2213
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2214 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2293
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2294 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEEL 2373
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2374 vkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVkIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2453
Cdd:COG1196 578 -----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV-LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2454 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLE 2533
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2534 AKKEMQQRLDQETEGFqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSK-------AEEEAkkfkkqaDEIKIRLQEte 2606
Cdd:COG1196 732 AEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEY-------EELEERYDF-- 799
|
650 660 670
....*....|....*....|....*....|...
gi 1207141740 2607 khtsekhtvvekLEVQRLQSKQEADGLHKAIAD 2639
Cdd:COG1196 800 ------------LSEQREDLEEARETLEEAIEE 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1865-2785 |
3.57e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.73 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1865 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFEHAE-----QQRTVLDDELQRLKNDVNS 1939
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELElallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1940 AVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 2019
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2020 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEgyqrkvleDQAAQHKQAIEEKIGQLKKssdtE 2099
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRS----K 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2100 LDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELElelkklkgiadetqkskakaeeeaekfRKLALEEEKKRKE 2179
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---------------------------KKLEEAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2180 AEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSM 2259
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2260 AQDKLKEEFEKAKKLAQEAEKA-----------KDNAEKEAALLHKKAEE-----------AERQKKAAEAEAAKQAKAQ 2317
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNELgrvtflpldsiKGTEIQGNDREILKNIEGF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2318 EDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKqkSSVEEELVKVK-VQLDETDKQKSVL---DVE 2393
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRI--VTLDGDLVRPGgVITGGSAKTNSSIlerRRE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2394 LKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ 2473
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2474 EAARLRQIAESDLAKQRElaekmleEKKQAIQEAAKLKAEAEKLQKQKDQ---AQVEAQKLLEAKKEMQQRLDQETEGFQ 2550
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEE-------ELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2551 KSLEAERKRQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQR 2623
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2624 LQSKQEADGLHKAIADlekekeklkkeaadlqkqskemANVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklek 2703
Cdd:TIGR02168 911 SELRRELEELREKLAQ----------------------LELRLEGLEVRIDNLQERLSEEYSLTLEE------------- 955
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2704 qFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2783
Cdd:TIGR02168 956 -AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
..
gi 1207141740 2784 QQ 2785
Cdd:TIGR02168 1035 KD 1036
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
349-447 |
3.87e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.92 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 349 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 427
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141740 428 DVPHPDEKSIITYVSSMYDV 447
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1507-2287 |
3.95e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.73 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1507 DDIIQEyvtLRTRYSELMTLSSQYIKFiietqRRLQDEEKAAE-----KLKEEERKKMAEMQAELEKQKQLAETHAKAIA 1581
Cdd:TIGR02168 192 EDILNE---LERQLKSLERQAEKAERY-----KELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1582 KAEQEANELKTKMKdEVSKRQDVavdsekqkhnIQRELQELKtlseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETT 1661
Cdd:TIGR02168 264 ELEEKLEELRLEVS-ELEEEIEE----------LQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1662 MKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKekkkaleDLEKFKLQ 1741
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL-------QIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1742 AEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1821
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1822 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKA 1873
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1874 EEAALKQKE---AAEMELGNQRKMAEETAKQKLAAEQELIRLRADF--EHAEQQRTVLDDELQRLK--NDVNSAVKQKKE 1946
Cdd:TIGR02168 561 AIAFLKQNElgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRKALSYLLGGVLvvDDLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1947 LEEE---------------------------LIKVRKEMEILLQQKSKAEketmSNTEKSKQLLESEAAKMRELAEEATK 1999
Cdd:TIGR02168 641 LRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELE----EKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2000 LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA 2079
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2080 QHKQAIEE----------------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 2143
Cdd:TIGR02168 797 ELKALREAldelraeltllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2144 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEA-ARQHKAAQEEVGRLMKLAEEAKKQKEIA 2222
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2223 EKEAEKQVILVQEAAQKCSAAEQKAQNvLVQQNKDSMAQ-DKLKEEFEKAKKLAQEAEKAKDNAEK 2287
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKE-LGPVNLAAIEEyEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1304-2119 |
5.09e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.35 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1304 KYENQLREVnKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRE 1383
Cdd:TIGR02168 217 ELKAELREL-ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1384 RWQAVFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLhavpiggskglQEQLTQEKKLLEEIEKNkdkVE 1463
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDEL-----------AEELAELEEKLEELKEE---LE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1464 DCQKFAKGYIDAIKDYELQLVTykalvepiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQyIKFIIETQRRLQD 1543
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEE------------LEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1544 EEKAAEKLKEEERkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQELK 1623
Cdd:TIGR02168 422 EIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1624 TLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETeLLQLRAKAV-----DADKLRNAAQEEAEKLRK 1698
Cdd:TIGR02168 496 RL-QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA-ALGGRLQAVvvenlNAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1699 QVAEETQKKrkaEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA--------------ERHLKQAELEKQRQIQVVE 1764
Cdd:TIGR02168 574 TFLPLDSIK---GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddlDNALELAKKLRPGYRIVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1765 E---VAKKTAATQLESKQVALT-------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1834
Cdd:TIGR02168 651 DgdlVRPGGVITGGSAKTNSSIlerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1835 A----LRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE---AALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1907
Cdd:TIGR02168 731 LrkdlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1908 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA 1987
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1988 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALkeKEAENDRLKRKAEEE 2067
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--EEAEALENKIEDDEE 968
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2068 GYQRKVledqaAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 2119
Cdd:TIGR02168 969 EARRRL-----KRLENKIKE-LGPVNLAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1872-2809 |
6.88e-17 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 89.08 E-value: 6.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1872 KAEEAALK-QKEAAEMELGNQRKMAEETAKQ-KLAAEQELirlradFEHAEQQRTVL---DDELQRLKNDVNSAVKQKKE 1946
Cdd:pfam01576 16 KVKERQQKaESELKELEKKHQQLCEEKNALQeQLQAETEL------CAEAEEMRARLaarKQELEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1947 LEEELIKVRKEMeillQQKSKAEKETMSNTEKSKQLLESEA----AKMRELAEEATKLRSVAEEAKKQRQIAEE---EAA 2019
Cdd:pfam01576 90 RSQQLQNEKKKM----QQHIQDLEEQLDEEEAARQKLQLEKvtteAKIKKLEEDILLLEDQNSKLSKERKLLEErisEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2020 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEA---ENDRLKRKAEEEGYQrkvLEDQAAQHKQAIEEKIGQLKKSS 2096
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTD---LQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2097 DTELDRQKKIVEETLK----QRKVVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQkskakaeeeaekfrklALE 2172
Cdd:pfam01576 243 EELQAALARLEEETAQknnaLKKIRELEAQISELQ-EDLESERAARNKAEKQRRDLGEELE----------------ALK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2173 eekkrkeaeakvkqiqaAEEEAARQHKAAQEEVgrlmklaeEAKKQKEIAEkeaekqvilvqeaAQKCSAAEQKAQNVLV 2252
Cdd:pfam01576 306 -----------------TELEDTLDTTAAQQEL--------RSKREQEVTE-------------LKKALEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2253 QQ--NKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK-------AEEAERQKKAAEAEAAKQAKAQEDAEKL 2323
Cdd:pfam01576 348 QEmrQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2324 RKEAEKEASRRAEAEAAALKLKQEADSEmakykklAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD 2403
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGK-------NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2404 AIKQ-------KAQVEDELSKVKIQMEDLLKLKLKIEKENQEL------MKKDKDNTKKLLEEEAENMKKLAEEAARLNI 2470
Cdd:pfam01576 501 LQEQleeeeeaKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkkrLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2471 EAQEAA----RLRQIAeSDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQV----EAQKLLEAKKEM---- 2538
Cdd:pfam01576 581 ELDDLLvdldHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALslarALEEALEAKEELertn 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2539 -QQRLD---------------QETEGFQKSLEA---ERKRQLE------ITAEAEKLKVKVT----------QLSDAQSK 2583
Cdd:pfam01576 660 kQLRAEmedlvsskddvgknvHELERSKRALEQqveEMKTQLEeledelQATEDAKLRLEVNmqalkaqferDLQARDEQ 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2584 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2663
Cdd:pfam01576 740 GEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2664 VQQEQLQQEKTILQQSFFAEKETL-----LKKEKAIEEEKKKLEKQFEDEVKKAEALK-AEQERQRKL------MEEERK 2731
Cdd:pfam01576 820 SRDEILAQSKESEKKLKNLEAELLqlqedLAASERARRQAQQERDELADEIASGASGKsALQDEKRRLeariaqLEEELE 899
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2732 KLQSAMDAAIKKQKEAEE-------EMNGKQKEMQDLEKKRIEQEKllaeENKNLREKLQQLQSSQKASYTKEIEIQTDK 2804
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLqveqlttELAAERSTSQKSESARQQLER----QNKELKAKLQEMEGTVKSKFKSSIAALEAK 975
|
....*
gi 1207141740 2805 VPEEE 2809
Cdd:pfam01576 976 IAQLE 980
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
347-445 |
3.83e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 77.34 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1207141740 427 -VDVPHPDEKSIITYVSSMY 445
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
227-326 |
8.42e-16 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 76.42 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 227 DRVQKKTFTKWVNKHLVKAQ-RHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 301
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1207141740 302 KLVNIRNDDIADGNPKLTLGLIWTI 326
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
347-446 |
1.02e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.77 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1207141740 427 VDV--PHPDEKSIITYVSSMYD 446
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
814-1004 |
1.10e-15 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 79.03 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 814 QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAF 893
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 894 TAALQTQWSWILQLCCCIETHLKENTAYFQFFSDVKEAEDRMKKMEDTMKKKYVCDrsiTVTRLEDLLQDAVEEKEQLNE 973
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1207141740 974 FKTHLEGLNRRAKTIIQLKPRNPAQPIKGKL 1004
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1801-2774 |
1.53e-15 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 84.49 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1801 QEEAEHLKKQQAEADKAREQAEK----------ELETWRQKANEALR------------LRLQAEEEANKKTAAQEEAEK 1858
Cdd:NF041483 11 RADDDHLSRFEAEMDRLKTEREKavqhaedlgyQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1859 QKEEAKREAKKRAK------AEEAALKQKE----------AAEMELGNQRKMAEETAKQKLA--------AEQELIRL-- 1912
Cdd:NF041483 91 DAERELRDARAQTQrilqehAEHQARLQAElhteavqrrqQLDQELAERRQTVESHVNENVAwaeqlrarTESQARRLld 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1913 --RADFEH------AEQQRtVLDDELQRLKNDVNSAvkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTE--KSKQL 1982
Cdd:NF041483 171 esRAEAEQalaaarAEAER-LAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDHAEqlRSSTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1983 LESEAAKMR----------ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE-------KILKEKLT-----AINEAT 2040
Cdd:NF041483 247 AESDQARRQaaelsraaeqRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2041 RLKTEAEIALKEKEAENDRLKRKAEEEGyQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEE 2120
Cdd:NF041483 327 ALKAEAEQALADARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2121 IHilKLNFEKASSGKQelelelkkLKGIA-DETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQA-AEEEAARQ- 2197
Cdd:NF041483 406 AD--RLRGEAADQAEQ--------LKGAAkDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGeARREAVQQi 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2198 HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLvqqnkdsmaqDKLKEEFEKAKKLAQE 2277
Cdd:NF041483 476 EEAARTAEELLTKAKADADELRSTATAESER---VRTEAIERATTLRRQAEETL----------ERTRAEAERLRAEAEE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2278 -AEKAKDNAEKEAALLHkkaEEAERqkkaaeAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAaalklkqEADSEMAKYK 2356
Cdd:NF041483 543 qAEEVRAAAERAARELR---EETER------AIAARQAEAAEELTRLHTEAEERLTAAEEALA-------DARAEAERIR 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2357 K-LAEKTLKQKSSVEEELVKVKVQLDEtdkqksvldvELKRLKQEVSdAIKQKAQVEDELSKVKIQMEdllklklkIEKE 2435
Cdd:NF041483 607 ReAAEETERLRTEAAERIRTLQAQAEQ----------EAERLRTEAA-ADASAARAEGENVAVRLRSE--------AAAE 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2436 NQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEkmlEEKKQAIQEAAKLKAEA 2514
Cdd:NF041483 668 AERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2515 eklQKQKDQAQVEAQKLLE------------AKKEMQQRLD----------QETEGFQKSLE--AERKRQlEITAEAEKL 2570
Cdd:NF041483 745 ---RKRVEEAQAEAQRLVEeadrratelvsaAEQTAQQVRDsvaglqeqaeEEIAGLRSAAEhaAERTRT-EAQEEADRV 820
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2571 KvkvtqlSDAQS---KAEEEAKKFKKQADEikirlqETE--KHTSEKhTVVEKL-EVQRLQSkQEADGLHKAIADLEKEK 2644
Cdd:NF041483 821 R------SDAYAereRASEDANRLRREAQE------ETEaaKALAER-TVSEAIaEAERLRS-DASEYAQRVRTEASDTL 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2645 EKLKKEAADLQKQSKEMANvqqeqlqqektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2724
Cdd:NF041483 887 ASAEQDAARTRADAREDAN------------RIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRAD 954
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2725 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQkemQDLEKKRIEQEKLLAE 2774
Cdd:NF041483 955 AAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAE 1001
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
345-442 |
3.25e-15 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 74.34 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1207141740 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1298-1964 |
3.50e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1298 AEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkrmsqlhserdvELEHYRQL 1377
Cdd:COG1196 251 LEAELEELEAELAEL------EAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1378 VGNLRERwqavfaQIELRQRELDLLNRQMQAYREsydwLIRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK 1457
Cdd:COG1196 311 RRELEER------LEELEEELAELEEELEELEEE----LEELEEELEEAEEELEE--------AEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1458 NKDKVEdcqkfakgyidaikdyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRyselmtlssqyikfIIET 1537
Cdd:COG1196 373 ELAEAE----------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--------------LEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1538 QRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDvavdsEKQKHNIQR 1617
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----AAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1618 ELQELKTLSEQEIKAKSQQVEEALLSRTrieeeihiIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1697
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA--------VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1698 KQVAEEtqkkRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1777
Cdd:COG1196 570 KAGRAT----FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1778 KQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1857
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1858 KQKEEAKREAKKRAKAEEAALKQKEAAEMELgnQRKMAEETAKQKLA-AEQELIRL-----RADFEHAEQQRTVldDELQ 1931
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEEL--PEPPDLEELERELErLEREIEALgpvnlLAIEEYEELEERY--DFLS 801
|
650 660 670
....*....|....*....|....*....|...
gi 1207141740 1932 RLKNDVNSAvkqKKELEEELIKVRKEMEILLQQ 1964
Cdd:COG1196 802 EQREDLEEA---RETLEEAIEEIDRETRERFLE 831
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2178-2738 |
3.53e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2178 KEAEAKVKQIQAAEEEAARQHKAAQEEVGRLmkLAEEAKKQKEIAEKEAEKQVilvqeaaqkcsaAEQKAQNVLVQQNKD 2257
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEA--QAEEYELLAELARLEQDIAR------------LEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2258 SMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEA 2337
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2338 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSK 2417
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2418 VKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKL------AEEAARLNIEAQEAARLRQIAESDLAKQRE 2491
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2492 LAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-----LEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAE 2566
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2567 AEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETekhtsekhtvvEKLEVQRLQSKQEADGLHKAIADLEKEKEK 2646
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE-----------LEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2647 LKKEAADLQKQSKEMANVQQEQLQQEKTILQQsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-------------- 2712
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELL----EEEELLEEEALEELPEPPDLEELERELERLereiealgpvnlla 786
|
570 580 590
....*....|....*....|....*....|...
gi 1207141740 2713 -EALKAEQER------QRKLMEEERKKLQSAMD 2738
Cdd:COG1196 787 iEEYEELEERydflseQREDLEEARETLEEAIE 819
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1566-2501 |
5.40e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 82.79 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1566 LEKQKQLAETHAKAIAKAEQEANELKT------KMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSE--QEIKAKSQQV 1637
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQykekacEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKeiEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1638 EEALLSRTRIEEEIHIIRLQLETTMKQ--KNTAE--TELLQLRAKAV-DADKLRNAAQEEAEKLRKQVAEETQKKRKAEE 1712
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKvfQGTDEqlNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1713 ELKRKSEAEKDAAKEKKKALEDLEKFKLQAE--------EAERHLKQA-ELEKQRQIQVVEEVAKKTA--ATQLESKQVA 1781
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFhTLVIERQEDEAKTAAQLCAdlQSKERLKQEQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1782 LT------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEAdkarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEE 1855
Cdd:TIGR00606 428 ADeirdekKGLGRTIELKKEILEKKQEELKFVIKELQQL----EGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1856 AEKQKEEAKREAKKRAKAEEAALKQKEA---AEMELGNQRKMA--EETAKQKLAAEQELIRLRADFEHAEQqrtvLDDEL 1930
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQLNHHTttrTQMEMLTKDKMDkdEQIRKIKSRHSDELTSLLGYFPNKKQ----LEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1931 QRLKNDvnsavkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLES--EAAKMRELAEEATKLRSVAEEAK 2008
Cdd:TIGR00606 580 HSKSKE-------INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2009 KQRQIAEEEAARQRAEAEKILKEKLTAINEATR-LKTEAEIALKEKEAENDRLKRKAEEEGyqrkvLEDQAAQHKQAIEE 2087
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDLQSKLRLAPDKLKS-----TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2088 KIGqLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2167
Cdd:TIGR00606 728 MLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVER 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2168 KLA-LEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQK 2246
Cdd:TIGR00606 807 KIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE---LKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2247 AQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEaerqkkaaeaeaakqakaqedaeklRKE 2326
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS-------------------------NKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2327 AEKEASRRAEaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2406
Cdd:TIGR00606 939 AQDKVNDIKE------KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2407 QKAQVEDELSKVKIQMEdllklklkIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAArlNIEAQEAARLRQIAESDl 2486
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENE--------LKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID--LIKRNHVLALGRQKGYE- 1081
|
970
....*....|....*
gi 1207141740 2487 aKQRELAEKMLEEKK 2501
Cdd:TIGR00606 1082 -KEIKHFKKELREPQ 1095
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
347-450 |
6.80e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 73.54 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1207141740 427 VDV--PHPDEKSIITYVSSMYDVMPR 450
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4228-4266 |
7.82e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.82 E-value: 7.82e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 4228 LLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEMNGIL 4266
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2263-2798 |
8.33e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 81.69 E-value: 8.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2263 KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaal 2342
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK--------------DLTFLLEESRDKAN---------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2343 KLKQEADSEMAKYKKLAEKtlkqKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQM 2422
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEK----KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2423 EDLLKLKLKIEKENQELMKKDKDNtkklLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQREL---AEKMLEE 2499
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQR----LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIlaeDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2500 KKQAIQEAAKLKAEAEKL-----QKQKDQAQVEAQklLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKV 2574
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllqAREKEIHDLEIQ--LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2575 TQLSDAQS-------KAEEEAKKFKKQADEIKIR---LQETEKH-TSEKHTVVEKLEVQRLQ-------SKQEADGLHKA 2636
Cdd:pfam05483 502 KELTQEASdmtlelkKHQEDIINCKKQEERMLKQienLEEKEMNlRDELESVREEFIQKGDEvkckldkSEENARSIEYE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2637 IADLEKEKEKLKKEAADLQKQSkEMANVQQEQLQQEKTILQQSFFAEKETLLK---KEKAIEEEKKKLEKQFEDEVKKAE 2713
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQI-ENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQ 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2714 ALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKN---LREKLQQLQSSQ 2790
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSA 740
|
....*...
gi 1207141740 2791 KASYTKEI 2798
Cdd:pfam05483 741 KAALEIEL 748
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
347-445 |
9.09e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 73.58 E-value: 9.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1207141740 427 -VDVPHPDEKSIITYVSSMY 445
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
350-445 |
1.09e-14 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 73.16 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 350 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDPED-VD 428
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1207141740 429 VPHPDEKSIITYVSSMY 445
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
230-330 |
1.10e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 72.72 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 230 QKKTFTKWVNKHLVK--AQRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 301
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1207141740 302 KLVNIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1536-2631 |
1.26e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 81.37 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1536 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKaEQEANELKTKMKDEVSKRQDVAVDSEKQKHNI 1615
Cdd:pfam01576 23 KAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR-KQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1616 QRELQELKT-LSEQEIKAKSQQVEEALLSRT--RIEEEIHIIRLQLETTMKQKNTAE-------TELLQLRAKAVDADKL 1685
Cdd:pfam01576 102 QQHIQDLEEqLDEEEAARQKLQLEKVTTEAKikKLEEDILLLEDQNSKLSKERKLLEeriseftSNLAEEEEKAKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1686 RNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKkkaledLEKFKLQAEEAERHLKQAELEKQR-QIQVVE 1764
Cdd:pfam01576 182 KNKHEAMISDLEERLKKE-EKGRQELEKAKRKLEGESTDLQEQ------IAELQAQIAELRAQLAKKEEELQAaLARLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1765 EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-------LQEEAEHLKKQ----------QAEADKAREQAEKELEt 1827
Cdd:pfam01576 255 ETAQKNNALKKIRELEAQISELQEDLESERAARNKaekqrrdLGEELEALKTEledtldttaaQQELRSKREQEVTELK- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1828 wRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE--AAEMELGNQRKMAEETAKQKLaa 1905
Cdd:pfam01576 334 -KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAelQAELRTLQQAKQDSEHKRKKL-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1906 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLles 1985
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNL--- 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1986 eAAKMRELAEEATKLRSVAEEAKKQRQIAEEE---AARQRAEAEKILKEKLTAINEATRLKTEAEialKEKEAENDRLKR 2062
Cdd:pfam01576 488 -STRLRQLEDERNSLQEQLEEEEEAKRNVERQlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ---RELEALTQQLEE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2063 KAEEegYQRkvLEDQAAQHKQAIEEKIgqlkkssdTELDRQKKIVEETLKQRKVVEEeihilKLNFEKASSGKqelelel 2142
Cdd:pfam01576 564 KAAA--YDK--LEKTKNRLQQELDDLL--------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISAR------- 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2143 kklkgIADETQKSKAKAEEEAEKFRKLAleeekkrkeaeAKVKQIQAAEEEAARQHKAAQEEVGRLM-------KLAEEA 2215
Cdd:pfam01576 620 -----YAEERDRAEAEAREKETRALSLA-----------RALEEALEAKEELERTNKQLRAEMEDLVsskddvgKNVHEL 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2216 KKQKEIAEKEAEKQVILVQEAAQKCSAAEQ------------KAQNVLVQQNKDSMAQDKLKEEFEKAKKLaqEAEKAKD 2283
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATEDaklrlevnmqalKAQFERDLQARDEQGEEKRRQLVKQVREL--EAELEDE 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2284 NAEKEAALLHKKAEEAErqkkaaeaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTL 2363
Cdd:pfam01576 762 RKQRAQAVAAKKKLELD---------LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESE 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2364 KQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkd 2443
Cdd:pfam01576 833 KKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQL------------------ 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2444 kdntKKLLEEEAENMKKLAEEAARLNIEAqEAARLRQIAESDLAKQRELAEKMLEEKKQAIQeaAKLkAEAEKLQKQKDQ 2523
Cdd:pfam01576 895 ----EEELEEEQSNTELLNDRLRKSTLQV-EQLTTELAAERSTSQKSESARQQLERQNKELK--AKL-QEMEGTVKSKFK 966
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2524 AQVEAqklLEAK-KEMQQRLDQETEGFQKSLEAERKRQleitaeaEKLKVKVTQLSDAQSKAEEeakkFKKQADEIKIRL 2602
Cdd:pfam01576 967 SSIAA---LEAKiAQLEEQLEQESRERQAANKLVRRTE-------KKLKEVLLQVEDERRHADQ----YKDQAEKGNSRM 1032
|
1130 1140
....*....|....*....|....*....
gi 1207141740 2603 QETEKHTSEKHTVVEKLEVQRLQSKQEAD 2631
Cdd:pfam01576 1033 KQLKRQLEEAEEEASRANAARRKLQRELD 1061
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2453-2813 |
2.28e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2453 EEAEnmKKLaeEAARLNIEaqeaaRL--------RQIAEsdLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQK 2521
Cdd:COG1196 175 EEAE--RKL--EATEENLE-----RLedilgeleRQLEP--LERQAEKAERYRElkeELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2522 DQAQVEAQKLLEAKKEMQQRLDQETegfqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR 2601
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAE------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2602 LQETEKhtsekhtVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFF 2681
Cdd:COG1196 318 LEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2682 AEKETLlkkekaieeekkklekqfedevkKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDL 2761
Cdd:COG1196 391 ALRAAA-----------------------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2762 EKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQM 2813
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3249-3287 |
6.88e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.12 E-value: 6.88e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 3249 LLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPELHEKL 3287
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
347-442 |
6.93e-14 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 70.49 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 347 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 425
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1207141740 426 DVDVPHPDEKSIITYVS 442
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1319-2087 |
8.05e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 78.68 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1319 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQR-ATEVNKRMSQLHSERDV--ELEHYRQLVGNLRERWQAVFAQIELR 1395
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQlCEEKNALQEQLQAETELcaEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1396 QRELDLLNRQMQAYRESydwLIRWIADAKQRQDKLHAvpigGSKGLQ-EQLTQE---KKLLEEIEKNKDKVEDCQKFAKG 1471
Cdd:pfam01576 84 LEEEEERSQQLQNEKKK---MQQHIQDLEEQLDEEEA----ARQKLQlEKVTTEakiKKLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1472 YIDAIKDYELQLvtykalvepiASPLKKAKMesasddiiqeyvtlrtryseLMTLSSQYIKFIIETQRRLQDEEK----- 1546
Cdd:pfam01576 157 LEERISEFTSNL----------AEEEEKAKS--------------------LSKLKNKHEAMISDLEERLKKEEKgrqel 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1547 -----AAEKLKEEERKKMAEMQAELEKQK-QLA---ETHAKAIAKAEQEAN-----------------ELKTKMKDEVSK 1600
Cdd:pfam01576 207 ekakrKLEGESTDLQEQIAELQAQIAELRaQLAkkeEELQAALARLEEETAqknnalkkireleaqisELQEDLESERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1601 RQdvavDSEKQKHNIQRELQELKTLSE---------QEIKAKSQQvEEALLSRTrIEEEIHIIRLQLEtTMKQKNTAETE 1671
Cdd:pfam01576 287 RN----KAEKQRRDLGEELEALKTELEdtldttaaqQELRSKREQ-EVTELKKA-LEEETRSHEAQLQ-EMRQKHTQALE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1672 -----LLQLRAKAVDADKLRNAAQEEAEKLRKQV-------AEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1739
Cdd:pfam01576 360 elteqLEQAKRNKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1740 LQAEEAERHLKQAElekQRQIQVVEEVAkkTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKARE 1819
Cdd:pfam01576 440 SELESVSSLLNEAE---GKNIKLSKDVS--SLESQLQDTQELLQEETRQKLNLST-RLRQLEDERNSLQEQLEEEEEAKR 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1820 QAEKELETWRQ------KANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK-EAAEMELGNQR 1892
Cdd:pfam01576 514 NVERQLSTLQAqlsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElDDLLVDLDHQR 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1893 KMAEETAKQ-----KLAAEQELIRLRA--DFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1965
Cdd:pfam01576 594 QLVSNLEKKqkkfdQMLAEEKAISARYaeERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1966 SKAEKeTMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAK------------------KQRQIAEEEAARQRA---- 2023
Cdd:pfam01576 674 DDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqferdlQARDEQGEEKRRQLVkqvr 752
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2024 EAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 2087
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEE 816
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1277-2061 |
1.59e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 77.85 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1277 LSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVP-VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE 1355
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1356 VNKRmsQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYREsydwlirwiadakQRQDKLHAVpi 1435
Cdd:pfam15921 199 ASGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKS-------------ESQNKIELL-- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1436 ggskglqeqltqekklleeIEKNKDKVEDCqkfakgyidaIKDYELQLVtykALVEPIASPLKKAKMESASDDIIQEYVT 1515
Cdd:pfam15921 262 -------------------LQQHQDRIEQL----------ISEHEVEIT---GLTEKASSARSQANSIQSQLEIIQEQAR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1516 LRT-----RYSELMTLSSQYIKFIIETQRRLQDEEKaaeklkeeerkkmaemqaELEKQKQLAETHakaIAKAEQEANEL 1590
Cdd:pfam15921 310 NQNsmymrQLSDLESTVSQLRSELREAKRMYEDKIE------------------ELEKQLVLANSE---LTEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1591 KTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIkAKSQQVEEalLSRTRIEEEIHIIRLQ-LETTMKQKNTAE 1669
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDT-GNSITIDH--LRRELDDRNMEVQRLEaLLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1670 TEllqlraKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlekfKLQAEEAER-- 1747
Cdd:pfam15921 446 ME------RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK---------------------KMTLESSERtv 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1748 -HLKQAELEKQRQIQvveevAKKTAATQLESKqVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELE 1826
Cdd:pfam15921 499 sDLTASLQEKERAIE-----ATNAEITKLRSR-VDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1827 TWRQKANEALRL-------RLQAEEEANKKtaAQEEAEKQKEEAKREAKKRA-KAEEAALKQKEAAEMELGNQRKMAEET 1898
Cdd:pfam15921 573 NMTQLVGQHGRTagamqveKAQLEKEINDR--RLELQEFKILKDKKDAKIRElEARVSDLELEKVKLVNAGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1899 AKQKL--------AAEQELIRLRADFE--------HAEQQRTVLD----------DELQRLKNDVNS-------AVKQKK 1945
Cdd:pfam15921 651 IKQERdqllnevkTSRNELNSLSEDYEvlkrnfrnKSEEMETTTNklkmqlksaqSELEQTRNTLKSmegsdghAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1946 ELEEELIKVRKEMEIlLQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatKLRSVAEEakKQRQIAEEEAARQRaea 2025
Cdd:pfam15921 731 GMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ------ELSTVATE--KNKMAGELEVLRSQ--- 798
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1207141740 2026 EKILKEKLT----AINEATRLKTEAEIALKEKEAENDRLK 2061
Cdd:pfam15921 799 ERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
223-329 |
1.71e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 69.62 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 223 ADERDrvqKKTFTKWVNKHLVKAQrhITDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALD 294
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVD 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141740 295 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 329
Cdd:cd21219 73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
345-445 |
2.55e-13 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 69.33 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 424
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1207141740 425 ED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1370-2068 |
2.84e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.93 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1370 ELEHYRQLVGNLRERWQAVFAQIELRQRELDLL----NRQMQAYRESYDWLIRWIADAKQRQDKLhavpiggsKGLQEQL 1445
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLtlctPCMPDTYHERKQVLEKELKHLREALQQT--------QQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1446 TQEKKLLEEIEKNkdkvedcQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDIIQ-------EYVTLRT 1518
Cdd:TIGR00618 246 TQKREAQEEQLKK-------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieqqaqrIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1519 RYSELMTLSSQYIKFI-----IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAEtHAKAIAKAEQEANELKTK 1593
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVkqqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1594 MKDEVSKRQDVAVDSEKQkHNIQRELQELKTLSEQEIKAksqQVEEALLSRTRIEEE--IHIIRLQLETTMKQKNTAETE 1671
Cdd:TIGR00618 398 LCKELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTaqCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1672 LLQLRAKAVDADKlRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQ 1751
Cdd:TIGR00618 474 QLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1752 AELEkqrQIQVVEEvaKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEhlKKQQAEADKAREQAEKELETWRQK 1831
Cdd:TIGR00618 553 SERK---QRASLKE--QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1832 ANEALRLRLQ--AEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1909
Cdd:TIGR00618 626 DLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1910 IR-----LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLE 1984
Cdd:TIGR00618 706 LRelethIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1985 SEAAKMRELAEEATKLRSVAEEAKKQ-------RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEN 2057
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
730
....*....|.
gi 1207141740 2058 DRLKRKAEEEG 2068
Cdd:TIGR00618 866 QEQAKIIQLSD 876
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2030-2828 |
3.05e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2030 KEKLTAINEA---TRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvLEDqaaqhkqAIEEKIGQLKKssdteLDRQKKI 2106
Cdd:TIGR02168 155 EERRAIFEEAagiSKYKERRKETERKLERTRENLDR-----------LED-------ILNELERQLKS-----LERQAEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2107 VEETLKQRKVVEE-EIHILKLNFEKASSGKQELELELKKLKGIADETQKskakaeeeaekfrklaleeekkrkeaeaKVK 2185
Cdd:TIGR02168 212 AERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTA----------------------------ELQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2186 QIQAAEEEAARQHKAAQEEVGRLMKLAEEAKkqKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmaqDKLK 2265
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALA--NEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-----DELA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2266 EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEK----LRKEAEKEASRRAEAEAAA 2341
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiasLNNEIERLEARLERLEDRR 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2342 LKLKQEADSEMAKYKKLAEKTLKQK-SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2420
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2421 QME--DLLKLKLKIEKENQELMKKDKDNTKKLLEEEA-----------ENMKKLA---EEAARLNIEAQEAARL--RQIA 2482
Cdd:TIGR02168 497 LQEnlEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaaieaalgGRLQAVVvenLNAAKKAIAFLKQNELgrVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2483 ESDLAKQRELAEKMLEEKK-------------------------------------QAIQEAAKL--------------- 2510
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggvlvvddldNALELAKKLrpgyrivtldgdlvr 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2511 -------------------KAEAEKLQKQKDQAQV---EAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAE 2568
Cdd:TIGR02168 657 pggvitggsaktnssilerRREIEELEEKIEELEEkiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2569 KLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEkekeklk 2648
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2649 keaADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEE 2728
Cdd:TIGR02168 810 ---AELTLLNEEAANLRERLESLERRI------AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2729 ERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEenknLREKLQQLQSsqkasytkEIEIQTDKVPEE 2808
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ----LELRLEGLEV--------RIDNLQERLSEE 948
|
890 900
....*....|....*....|
gi 1207141740 2809 ELVQMTMVETTKKVLNGSTE 2828
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEE 968
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3909-3947 |
3.65e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 3.65e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 3909 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEFHDKL 3947
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2922-2960 |
4.11e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 4.11e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 2922 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPELHTKL 2960
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
248-327 |
4.89e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.39 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 248 HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 319
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1207141740 320 LGLIWTII 327
Cdd:cd21223 105 LALLWRII 112
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
232-333 |
9.39e-13 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 67.65 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 232 KTFTKWVNKHLVKAqrHITDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21298 9 KTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1812-2599 |
1.08e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1812 AEADKAREQAEKELETWRQKANealRLRLQAEEEANKktaaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQ 1891
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIE---RLDLIIDEKRQQ--------------LERLRREREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1892 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRKEMEILLQQKSKAEK 1970
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1971 ETMSNTEKSKQLLESEA---AKMRELAEEATKL-RSVAEEAKKQRQIAEEEAARQ------RAEAEKILKEKLTAINEAT 2040
Cdd:TIGR02169 309 SIAEKERELEDAEERLAkleAEIDKLLAEIEELeREIEEERKRRDKLTEEYAELKeeledlRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2041 RLKTEAEIALKEKEAENDRLKRKAEEegyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKI------VEETLKQR 2114
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqewkLEQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2115 KVVEEEIHILKLNF---EKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-----------------LALEEE 2174
Cdd:TIGR02169 465 SKYEQELYDLKEEYdrvEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryaTAIEVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2175 KKRKEAEAKVKQIQAAEE--EAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLV 2252
Cdd:TIGR02169 545 AGNRLNNVVVEDDAVAKEaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-------DPKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2253 QQNKDSMaqdkLKEEFEKAKKLAQEAEKAKDNAEkeaalLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEAS 2332
Cdd:TIGR02169 618 YVFGDTL----VVEDIEAARRLMGKYRMVTLEGE-----LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2333 RRAEAEAAALKLKQEADSEMAKYKKLAEKT---LKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA 2409
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2410 QVEDELSKVKIQMEDllklklKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQ 2489
Cdd:TIGR02169 769 ELEEDLHKLEEALND------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2490 RELAEKMLEEKkqaiQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEK 2569
Cdd:TIGR02169 843 IDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830
....*....|....*....|....*....|
gi 1207141740 2570 LKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2599
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
345-445 |
1.41e-12 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 66.98 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 424
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1207141740 425 ED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3325-3363 |
2.00e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 2.00e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 3325 LLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEMNQNL 3363
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
719-908 |
2.07e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 69.40 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 719 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 795
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIeegHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 796 LQYAKLLTSSKTRLRSLD---QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNV 872
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207141740 873 QMTGDKLLKDGHP-ARKTIEAFTAALQTQWSWILQLC 908
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1865-2574 |
3.82e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1865 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVNSAVKQK 1944
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1945 KELEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLEsEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 2024
Cdd:PRK03918 248 ESLEGSK----RKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2025 AEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegYQR-KVLEDQAAQHKqaieekigqlKKSSDTELDRQ 2103
Cdd:PRK03918 323 INGI-EERIKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEaKAKKEELERLK----------KRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2104 KKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-LALEEEKKRKEAEA 2182
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKIT---ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2183 KVKQIQAAEEEAarqhKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQD 2262
Cdd:PRK03918 467 ELKEIEEKERKL----RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2263 KLKEEFEKAKKLAQEA---EKAKDNAEKEAALLHKKAEEaerqkkaaeaeaakqakaqedaeklrkeaekeasrraeaea 2339
Cdd:PRK03918 543 SLKKELEKLEELKKKLaelEKKLDELEEELAELLKELEE----------------------------------------- 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2340 AALKLKQEADSEMAKYKKLAEKTLKQKSSVEEelvkvkvqLDETDKqksvldvELKRLKQEVSDAIKQKAQVEDELSKVK 2419
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKE--------LEREEK-------ELKKLEEELDKAFEELAETEKRLEELR 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2420 IQMEdllklklkiekenqELMKKDKDNTKKLLEEEaenMKKLAEEAARLNIEAQEAARLRQIAESDLAKqrelaekmLEE 2499
Cdd:PRK03918 647 KELE--------------ELEKKYSEEEYEELREE---YLELSRELAGLRAELEELEKRREEIKKTLEK--------LKE 701
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2500 KKQAIQEAAKlkaEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAE---RKRQ-LEITAEAEKLKVKV 2574
Cdd:PRK03918 702 ELEEREKAKK---ELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEElteGKYSgVRVKAEENKVKLFV 777
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1560-2076 |
3.98e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1560 AEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQelktLSEQEIKAKSQQVEE 1639
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEAG----LDDADAEAVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1640 ALLSRTRIEEEIHIIRLQLETTmkqKNTAETellqLRAKAVDADKLRNAAQEEAEKLRKQV--AEETQKKRKAE-EELKR 1716
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAH---NEEAES----LREDADDLEERAEELREEAAELESELeeAREAVEDRREEiEELEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1717 KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEES-----LK 1791
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSphvetIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1792 NEQVMVIQLQEEAEHLKKQQAEADKAREQA------EKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakr 1865
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRETIE------------------ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1866 eakkrAKAEEAALKQKEAAEMELGNQRKmAEETAKQKLAAEQELIRLRAdfehAEQQRTVLDDELQRLkNDVNSAVKQKK 1945
Cdd:PRK02224 534 -----EKRERAEELRERAAELEAEAEEK-REAAAEAEEEAEEAREEVAE----LNSKLAELKERIESL-ERIRTLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1946 ELEEELIKVRKemeillQQKSKAEKEtmsntEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARqraea 2025
Cdd:PRK02224 603 DAEDEIERLRE------KREALAELN-----DERRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQ----- 664
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2026 ekiLKEKLTAINEA-TRLKTE---AEIALKEKEAENDRLKRKAEEEGYQRKVLED 2076
Cdd:PRK02224 665 ---VEEKLDELREErDDLQAEigaVENELEELEELRERREALENRVEALEALYDE 716
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1544-2301 |
4.01e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1544 EEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQ--------DVAVDSEKQKHNI 1615
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1616 QRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvdaDKLRNAAQEEAEK 1695
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE--------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL---EDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1696 LRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEKFKLQAEEAERHLKQAELEKQrqIQVVEEvAKKTAATQL 1775
Cdd:TIGR02169 380 FAETR-DELKDYREKLEKLKREINELKR------------ELDRLQEELQRLSEELADLNAA--IAGIEA-KINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1776 ESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAA 1852
Cdd:TIGR02169 444 EDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1853 QEEAEKQKEEAKREakkRAKAEEAA----------------------LKQKEAAEMELGNQRKMAEETAKQKLAAEQELI 1910
Cdd:TIGR02169 523 VHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavakeaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1911 RLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE-----LEEELIK---------VRKEMEILLQQKSKAEKE 1971
Cdd:TIGR02169 600 GFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKyrmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1972 TMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE----EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlK 2043
Cdd:TIGR02169 678 RLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkigEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---I 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2044 TEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHI 2123
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2124 LKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEKFRKLALEEEkkrkeaeakVKQIQAAEEEAARQHKAAQE 2203
Cdd:TIGR02169 827 EKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLNGKKEELEEE---------LEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2204 EVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL------------------VQQNKDSMAQD--- 2262
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledVQAELQRVEEEira 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1207141740 2263 ------KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2301
Cdd:TIGR02169 970 lepvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2219-2799 |
4.84e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2219 KEIAEKEAEKQVILVQEA--AQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKD---NAEKEAALLH 2293
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2294 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAeaaaLKLKQEadseMAKYKKLAEKTLKQKSSVEEEL 2373
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY----IKLSEF----YEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2374 VKVKVQLDETDKQKSVLDvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2453
Cdd:PRK03918 324 NGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2454 EAENMKKLAEEAARLNIEAQEaaRLRQIAESDLAKQ------RELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQKDQ 2523
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKE--LKKAIEELKKAKGkcpvcgRELTEehrkELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2524 AQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITA-EAEKLKVKVTQLSDAQSKAEEEAKK---FKKQADE 2597
Cdd:PRK03918 481 ELRELEKVLKKESELikLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2598 IKIRLQETEKHTSEKHTvveKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlq 2677
Cdd:PRK03918 561 LEKKLDELEEELAELLK---ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL-- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2678 qsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME-EERKKLQSAMDAAIKKQKEAEEEMNGKQK 2756
Cdd:PRK03918 636 ----AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAElEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1207141740 2757 EMQDLEKKRieqekllaEENKNLREKLQQLQSSQKASYTKEIE 2799
Cdd:PRK03918 712 ELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVG 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1875-2781 |
6.99e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.41 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1875 EAALKQKEAAEMELGNQRKMAEETAKQklaaeqeLIRLRADFEHAEQQRTVLDD----ELQRLKNDVNSAVKQKKELEEE 1950
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1951 LIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEatklrsvaEEAKKQRQIAEEEAarQRAEAEKILK 2030
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2031 EKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQ---AIEEKIGQLKKSSDTELDRQKKIV 2107
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeleDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2108 EETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLaleeekkrkeaEAKVKQI 2187
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-----------EWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2188 QAAEEEAARQHKAAQEEVGRLMKlaEEAKKQKEIAEKEAEKQVIlvqEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKE 2266
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEK--ELSKLQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlGSVGE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2267 EFEKAKKLAQEAEKA----KDNAEKEAALLHKKAEEAERQKKAaeaeaakqakaqedaeKLRKEAEKEASRRAEAEAAAL 2342
Cdd:TIGR02169 536 RYATAIEVAAGNRLNnvvvEDDAVAKEAIELLKRRKAGRATFL----------------PLNKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2343 KLKQEADSEMAKYKKlAEKTLKQKSSVEEELVKVKVQLDETdkQKSVLDVEL-----------KRLKQEVSDAIKQKAQV 2411
Cdd:TIGR02169 600 GFAVDLVEFDPKYEP-AFKYVFGDTLVVEDIEAARRLMGKY--RMVTLEGELfeksgamtggsRAPRGGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2412 E---DELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnmkklaeeaarlnieaqeaarlRQIAESDLAK 2488
Cdd:TIGR02169 677 QrlrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE----------------------IEQLEQEEEK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2489 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLD----QETEGFQKSLEAERKRQLEIT 2564
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2565 AEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvqrlqskQEADGLHKAIADLEKEK 2644
Cdd:TIGR02169 815 REIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-------EELEELEAALRDLESRL 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2645 EKLKKEAADLQKQSKEMANVQQEQ-LQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERqr 2723
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELeAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR-- 962
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2724 klMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2781
Cdd:TIGR02169 963 --VEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3576-3614 |
7.11e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 7.11e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 3576 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPEVHEKL 3614
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4152-4190 |
7.46e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.46e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 4152 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEFKDKL 4190
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1799-2783 |
8.47e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 72.13 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1799 QLQEEAEHLKKQQAEADKArEQAEKELETWRQKANE---ALRLRLQAEEE----ANKKTAAQEEAEKQKEEAKREAKKRA 1871
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEeknALQEQLQAETElcaeAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1872 KAEE------AALKQKEAAEMELGNQRKMAEETAKQKL-----AAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1940
Cdd:pfam01576 85 EEEEersqqlQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1941 VKQKKELEEE---LIKVRKEMEIL---LQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatklrsvaEEAKKQRQIA 2014
Cdd:pfam01576 165 TSNLAEEEEKaksLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQE------------QIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2015 EEEAARQRAEAEkiLKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRkvleDQAAQHKQAIEEKIGQLKK 2094
Cdd:pfam01576 233 ELRAQLAKKEEE--LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2095 SSDTELDRQKkiVEETLKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIA-DETQKSKAKAEEEAEKFRKLALEE 2173
Cdd:pfam01576 307 ELEDTLDTTA--AQQELRSKR--EQEVTELKKALEEETRSHEAQLQEMRQKHTQAlEELTEQLEQAKRNKANLEKAKQAL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2174 EKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQK-EIAEK----------------EAEKQVILVQEA 2236
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRaELAEKlsklqselesvssllnEAEGKNIKLSKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2237 AQKCSAAEQKAQNVLVQQNKDSMAQD----KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEA----ERQKKAAEA 2308
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMkkklEEDAGTLEA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2309 EAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEAD-------------SEMAKYKKLAEKTLKQKSSVEEELVK 2375
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdllvdldhqrqlvSNLEKKQKKFDQMLAEEKAISARYAE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2376 VKVQLDETDKQKSVLDVELKRlkqEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKkdkdnTKKLLEEEA 2455
Cdd:pfam01576 623 ERDRAEAEAREKETRALSLAR---ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER-----SKRALEQQV 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2456 ENMKKLAEEA---------ARL----NIEAQEAARLRQIAESD---------LAKQ-RELAEKMLEEKKQAIQEAA---- 2508
Cdd:pfam01576 695 EEMKTQLEELedelqatedAKLrlevNMQALKAQFERDLQARDeqgeekrrqLVKQvRELEAELEDERKQRAQAVAakkk 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2509 ------KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-------------ETEGFQKSLEAERKRQLEITAEAEK 2569
Cdd:pfam01576 775 leldlkELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEarasrdeilaqskESEKKLKNLEAELLQLQEDLAASER 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2570 LKVKVTQLSDA-QSKAEEEAKKFKKQADE---IKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKE 2645
Cdd:pfam01576 855 ARRQAQQERDElADEIASGASGKSALQDEkrrLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQ 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2646 KLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSF------FAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQ 2719
Cdd:pfam01576 935 KSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIaaleakIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE 1014
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 2720 ERQRKLMEEERKKLQSAMDAAIKKQKEAEEE---MNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2783
Cdd:pfam01576 1015 RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEasrANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2098-2812 |
1.01e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.92 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2098 TELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS-GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLA--LEEE 2174
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTqkREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2175 KKRKEAEAKVKQIQAAEEEAARQ---HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL--VQEAAQKCSAAEQKAQN 2249
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQeavLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHteLQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2250 VLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA---KDNAEKEAALLHK-KAEEAERQKKAAEAEAAKQAKAQEDAEKLRK 2325
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2326 EAEKEASRRAEAEAAALKLKQEADSEMAKYKKLA-EKTLKQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLKQEV 2401
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREqqlQTKEQIHLQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2402 SDAIKQKAQVEDELSKVKIQMEdLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQi 2481
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2482 AESDLAKQRElaekmleekkqaiqeaaKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrldqetegfqKSLEAERKRQL 2561
Cdd:TIGR00618 571 SFSILTQCDN-----------------RSKEDIPNLQNITVRLQDLTEKLSEAED--------------MLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2562 EITAEAEKLKVKVTQlsdaQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLE 2641
Cdd:TIGR00618 620 KLQPEQDLQDVRLHL----QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2642 KEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLlkkekaieEEKKKLEKQFEDEVKKAEALKAEQER 2721
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL--------NQSLKELMHQARTVLKARTEAHFNNN 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2722 QRKLMEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2800
Cdd:TIGR00618 768 EEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
730
....*....|..
gi 1207141740 2801 QTDKVPEEELVQ 2812
Cdd:TIGR00618 848 THQLLKYEECSK 859
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4498-4536 |
1.08e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.08e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 4498 LLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMVDRI 4536
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2203-2817 |
1.19e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.54 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2203 EEVGRLMKLAEEAKKQKEIAEKEAEKQV----ILVQEAAQKCSAAEQKAQnvlVQQNKDSMAQDKLKEEFEKAKKLAQEA 2278
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTlrsqLLTLCTPCMPDTYHERKQ---VLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2279 EKAKDNAEKEAALLHKKAEEAE-RQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkQEADSEMAKYKK 2357
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-QSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2358 LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQevsdaikqKAQVEDELSKVKIQMEDLLKLKLKIEKENQ 2437
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI--------SCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2438 ELMKKDKDNTKKLLEEEAENmkklAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQaIQEAAKLKAEAEKL 2517
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFR----DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2518 QKQKDQAQVEAQK--LLEAKKEMQQRLDQETEGFQKSLEAERKRQLEitaeAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2595
Cdd:TIGR00618 476 QTKEQIHLQETRKkaVVLARLLELQEEPCPLCGSCIHPNPARQDIDN----PGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2596 DEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTI 2675
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2676 LQQSFFAEKETLLKKEKAIEEEKKKLEKQFED--EVKKAEALKAEQeRQRKLMEEERKKLQSAMDAAIKKQK-----EAE 2748
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHalSIRVLPKELLAS-RQLALQKMQSEKEQLTYWKEMLAQCqtllrELE 710
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2749 EEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVE 2817
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
347-446 |
1.32e-11 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 63.90 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN---LENLEQAFSIAER-DLGVTRLL 422
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1207141740 423 DPEDVdVPHPDEKSIITYVSSMYD 446
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
225-324 |
1.44e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 64.37 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 225 ERDRvQKKTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 296
Cdd:cd21300 4 EGER-EARVFTLWLNSLDVEPA--VNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1207141740 297 KHRQVKLVNIRNDDIADGNPKLTLGLIW 324
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1301-2092 |
1.53e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.25 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1301 ILNKYENQLREVNKVPVNEKEIEASQTQLQKLRSEAEgkqatfDRLEEELQRATEVNKRMSQLHSERDVElehyrqlvgn 1380
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE------KRLEEIEQLLEELNKKIKDLGEEEQLR---------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1381 LRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiADAKQRQDKLhavpiggskglqeqltQEKKLLEEIEKNKD 1460
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELED------------AEERLAKLEA----------------EIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1461 KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASddiiqeyvtLRTRYSELmtlsSQYIKFIIETQRR 1540
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------YREKLEKL----KREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1541 LQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEvskrqdvavdsEKQKHNIQRELQ 1620
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-----------EQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1621 ELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQ---LETTMKQKNTAETELLQLRAKAVDAdkLRNAAqeeAEKLR 1697
Cdd:TIGR02169 480 RV----EKELSKLQRELAEAEAQARASEERVRGGRAVeevLKASIQGVHGTVAQLGSVGERYATA--IEVAA---GNRLN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1698 KQVAEETQKKRKAEEELKRK-----------------SEAEKDAAKEKKKALEDLEKFKLQ-----------------AE 1743
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRkagratflplnkmrderRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvedIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1744 EAERHLKQAelekqRQIQVVEEVAKKT--------AATQLESKQVALTARLEESLKNEQVMVIQ---LQEEAEHLKKQQA 1812
Cdd:TIGR02169 631 AARRLMGKY-----RMVTLEGELFEKSgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1813 EADKAREQAEKELETWRQKANealrlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAE-EAALKQKEAAEMELgnq 1891
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIE-----QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKElEARIEELEEDLHKL--- 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1892 rKMAEETAKQKLaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSaVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1971
Cdd:TIGR02169 778 -EEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1972 TMSNTEKSKQLLESEAAK----MRELAEEATKLRSVAEEAKKQR---QIAEEEAARQRAEAEKILKEkltaineatrLKT 2044
Cdd:TIGR02169 855 EIENLNGKKEELEEELEEleaaLRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSE----------LKA 924
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1207141740 2045 EAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKIGQL 2092
Cdd:TIGR02169 925 KLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAE-LQRVEEEIRAL 970
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1619-1932 |
2.01e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.54 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1619 LQELKTLSEQEIKAKSQQVEEallSRTRIEEEIHIIRLQLETTMKQKNTAETELLQlRAKAVDADKLRNAAQEEAEKLRK 1698
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ---ERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1699 QvaeetQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK-----LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1773
Cdd:pfam17380 354 R-----QEERKRELERIRQEEIAMEISRMRELERLQMERQQknervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1774 QLESKQVALTaRLEESLKNEQVMV----IQLQEEAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANK- 1848
Cdd:pfam17380 429 QEEARQREVR-RLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKILEKELEERKq 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1849 -------KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgnQRKMAEETAKqklaAEQELIRLRADFEHAEQ 1921
Cdd:pfam17380 507 amieeerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE-----RRRIQEQMRK----ATEERSRLEAMEREREM 577
|
330
....*....|.
gi 1207141740 1922 QRTVLDDELQR 1932
Cdd:pfam17380 578 MRQIVESEKAR 588
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3652-3688 |
2.32e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.32e-11
10 20 30
....*....|....*....|....*....|....*..
gi 1207141740 3652 LLDAQVATGGIIDPVNSHRLPNDVAIERGYFSKQLAK 3688
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1560-2017 |
5.09e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1560 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAvDSEKQKHNIQRELQELKtlSEQEIKAKSQQVEE 1639
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELR--EELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1640 ALLSRTRIEEEIHIIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKse 1719
Cdd:COG4717 130 LYQELEALEAELAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1720 aEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQiQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVM--- 1796
Cdd:COG4717 201 -LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1797 ------VIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKkTAAQEEAEKQKEEAKREAKKR 1870
Cdd:COG4717 279 lflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-EELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1871 AKAEEAALKQKEAAEMELGNQRKMA-EETAKQKLAAEQELIRLRADFEHAEQQ----------------RTVLDDELQRL 1933
Cdd:COG4717 358 ELEEELQLEELEQEIAALLAEAGVEdEEELRAALEQAEEYQELKEELEELEEQleellgeleellealdEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1934 KNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI 2013
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1207141740 2014 AEEE 2017
Cdd:COG4717 509 YREE 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1415-2088 |
5.20e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 69.37 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1415 WLIRWIADAKQRQDKLH---AVPIGGSKGLQE-QLTQEK---KLLEEIEKNKDKV--------------EDCQKFAKGYI 1473
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIkennatrhlcnllkETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1474 DAIKDYELQLVTYKAL---VEPIASPLKKAKMEsASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRR-----LQDEE 1545
Cdd:pfam05483 173 KYEYEREETRQVYMDLnnnIEKMILAFEELRVQ-AENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQvslllIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1546 KAAEKLKEEERKKMAEMQA-ELEKQKQLAETHAKAIAKAE----QEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQ 1620
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKAnQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1621 ELKTLSEQEIKAKSQQ---VEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1697
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1698 KQVAE------ETQKKRKAEEELKRKSEAEKdaakekkkaledlekFKLQAEEAERHLKQAEL-----EKQRQIQVVEEV 1766
Cdd:pfam05483 412 KILAEdeklldEKKQFEKIAEELKGKEQELI---------------FLLQAREKEIHDLEIQLtaiktSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1767 akKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA 1846
Cdd:pfam05483 477 --KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1847 NKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVL 1926
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1927 DDELQRLKNDVNSAvkqKKELEEELIKVRKEMEIllqqKSKAEKETMSNTEKSKQlleseaakmreLAEEATKLRSVAEE 2006
Cdd:pfam05483 635 EIKVNKLELELASA---KQKFEEIIDNYQKEIED----KKISEEKLLEEVEKAKA-----------IADEAVKLQKEIDK 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2007 aKKQRQIAEEEA--ARQRAEAEKILKEKLTAI-------NEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ 2077
Cdd:pfam05483 697 -RCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
730
....*....|.
gi 1207141740 2078 AAQHKQAIEEK 2088
Cdd:pfam05483 776 AKENTAILKDK 786
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1586-1906 |
8.86e-11 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 68.50 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1586 EANELKTKMKDEV-----SKRQDVAVDSEKQKH----NIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRL 1656
Cdd:NF033838 51 SGNESQKEHAKEVeshleKILSEIQKSLDKRKHtqnvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1657 QLETTMKQKNTAET----ELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakeKKKAL 1732
Cdd:NF033838 131 KKDTLEPGKKVAEAtkkvEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE----------EAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1733 EDLEKFKlqAEEAERHLKQAELEKQRQIQV----VEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1808
Cdd:NF033838 201 RDEEKIK--QAKAKVESKKAEATRLEKIKTdrekAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1809 KQQ-------------------------AEADKAREQAEKELETWRQK------ANEALRLRLQ-AEEEAN-KKTAAQEE 1855
Cdd:NF033838 279 KENdakssdssvgeetlpspslkpekkvAEAEKKVEEAKKKAKDQKEEdrrnypTNTYKTLELEiAESDVKvKEAELELV 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 1856 AEKQKEEAKREAKKRAKAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAE 1906
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVES-KKAEATRLEkIKTDRKKAEEEAKRKAAEE 409
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
347-445 |
9.16e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 61.60 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1207141740 427 VdVPHPDEKSIITYVSSMY 445
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2190-2547 |
9.27e-11 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 68.00 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2190 AEEEAARQHKAAQEEVGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL----VQQNKDSMAQDKL 2264
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEArireLEEDIKTLTQRVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2265 KEEfekakklaQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKL 2344
Cdd:pfam07888 147 ERE--------TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2345 KQEADSEMAKYKKLaEKTLKQKSSVEEELvkvkvqldETDKQKSVLdvelkrLKQEVSDAIKQKAQVEDELSKVKI---Q 2421
Cdd:pfam07888 219 TQKLTTAHRKEAEN-EALLEELRSLQERL--------NASERKVEG------LGEELSSMAAQRDRTQAELHQARLqaaQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2422 MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKK 2501
Cdd:pfam07888 284 LTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESR 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1207141740 2502 QAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETE 2547
Cdd:pfam07888 364 RELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3985-4023 |
1.26e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.88 E-value: 1.26e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 3985 LLEAQVATGGLMDPEYYFRLPIDIAMQRGYMNKETSERI 4023
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1168-1946 |
1.50e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.17 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1168 SVEQGEQDESVCKSyitQIKDLRLRLEGCESRTVNRLRQMVDKEplKACTQRATEQKKVQTELEGIKKDLDKVVEKSEAV 1247
Cdd:TIGR02169 302 EIASLERSIAEKER---ELEDAEERLAKLEAEIDKLLAEIEELE--REIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1248 LATSQQSSSAPV-LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ----GAEDILNKYENQLREVN-KVPVNEKE 1321
Cdd:TIGR02169 377 DKEFAETRDELKdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEEKEDKAlEIKKQEWK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1322 IEASQTQLQKLRSEAEGKQATFDRLEEELqraTEVNKRMSQLHSERDV---ELEHYRQLVGNLRERWQAVFAQIelrqre 1398
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKEL---SKLQRELAEAEAQARAseeRVRGGRAVEEVLKASIQGVHGTV------ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1399 ldllnRQMQAYRESYDWLIRWIADAKqrqdkLHAVPIGGSKGLQE--QLTQEKKL--LEEIEKNKDKVEDCQKfAKGYID 1474
Cdd:TIGR02169 528 -----AQLGSVGERYATAIEVAAGNR-----LNNVVVEDDAVAKEaiELLKRRKAgrATFLPLNKMRDERRDL-SILSED 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1475 AIKDYELQLVTYKALVEPI-----ASPLKKAKMESASDDIIQ-EYVTLRTRYSE---LMTLSSQYIKFIIETQRRLQDEE 1545
Cdd:TIGR02169 597 GVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRSEPAEL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1546 kaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTL 1625
Cdd:TIGR02169 677 --------------QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1626 sEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdadklrnaaQEEAEKLRKQVAEETQ 1705
Cdd:TIGR02169 743 -EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---------QAELSKLEEEVSRIEA 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1706 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhlKQAELEKQrqiqvveevaKKTAATQLESKQVALtAR 1785
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK--EIENLNGK----------KEELEEELEELEAAL-RD 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1786 LEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANK---KTAAQEEAEKQKEE 1862
Cdd:TIGR02169 880 LESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSE-LKAKLEALEEELSeieDPKGEDEEIPEEEL 951
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1863 AKREAKKRAKAEEAALKQKEAAEMelgnqrkmaeetakqklAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVK 1942
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEPVNM-----------------LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
....
gi 1207141740 1943 QKKE 1946
Cdd:TIGR02169 1015 KKRE 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2517-2785 |
1.70e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.46 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2517 LQKQKDQAQVEAQKLLEakKEMQQRLDQETEgfQKSLEAERKRQLEitaEAEKLKvKVTQLSDAQSKAEEEAKKFKKQAD 2596
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE--KMEQERLRQEKE--EKAREVERRRKLE---EAEKAR-QAEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2597 EIKIRLQETEKHTS-----------EKHTVVEKLEVQRLQS----KQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEM 2661
Cdd:pfam17380 350 LERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKnervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2662 ANVQQEQLQQektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQ-------RKLMEEERKKLQ 2734
Cdd:pfam17380 430 EEARQREVRR----LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraeeqrRKILEKELEERK 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 2735 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2785
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1531-2245 |
1.73e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1531 IKFIIETQRRLQDEE-------------------------KAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQ 1585
Cdd:TIGR02169 193 IDEKRQQLERLRRERekaeryqallkekreyegyellkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1586 EANELKTKMKDEVSKRQ--------DVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQ 1657
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAE--------IDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1658 LETTMKQKNTAETELLQLRAKavdADKLRNAAQEEAEKLRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEK 1737
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEE---LEDLRAELEEVDKEFAETR-DELKDYREKLEKLKREINELKR------------EL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1738 FKLQAEEAERHLKQAELEKqrQIQVVEEvAKKTAATQLESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1817
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNA--AIAGIEA-KINELEEEKEDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1818 REQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREakkRAKAEEAA----------------- 1877
Cdd:TIGR02169 485 LSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavak 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1878 -----LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE- 1946
Cdd:TIGR02169 562 eaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKy 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1947 ----LEEELIK---------VRKEMEILLQQKSKAEKETMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE---- 2005
Cdd:TIGR02169 640 rmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkig 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2006 EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAI 2085
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2086 EEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHILKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEK 2165
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTLEKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2166 FRKLALeeekkrkeaEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQ 2245
Cdd:TIGR02169 861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1672-2102 |
2.29e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.67 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1672 LLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELK------RKSEAEKDAAKEKKKALEDLEKFKLQAEE- 1744
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlNLVQTALRQQEKIERYQEDLEELTERLEEq 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1745 ----AERHLKQAELEKQRQiQVVEEVakKTAATQLESKQVALTARLEESLKNEQVmvIQLQEEAEHLkkqQAEADKAREQ 1820
Cdd:COG3096 367 eevvEEAAEQLAEAEARLE-AAEEEV--DSLKSQLADYQQALDVQQTRAIQYQQA--VQALEKARAL---CGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1821 AEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEETAK 1900
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLS----------------VADAARRQFEKAYELVCKIAGEVE----RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1901 qklaaeqELIRLRADFEHAEQQRTVLDDELQRLkndvnsavkqkkeleEELIKVRKEMEILLQQKSKAEKETMSNTEKSK 1980
Cdd:COG3096 499 -------ELLRRYRSQQALAQRLQQLRAQLAEL---------------EQRLRQQQNAERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1981 QLLESEAAKMRELAEEAtklRSVAEEAKKQRQiAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 2060
Cdd:COG3096 557 ELLAELEAQLEELEEQA---AEAVEQRSELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAM 632
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1207141740 2061 KRKAEEEgYQRKVLEDQAAQHKQAIEEKIGQLKK---SSDTELDR 2102
Cdd:COG3096 633 QQLLERE-REATVERDELAARKQALESQIERLSQpggAEDPRLLA 676
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
223-330 |
3.44e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 60.68 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 223 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLKH 298
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMED 89
|
90 100 110
....*....|....*....|....*....|..
gi 1207141740 299 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21222 90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2245-2628 |
3.46e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.69 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2245 QKAQNVLVQQNK-DSMAQDKLKEEFEKakkLAQEAEKAKDNAEKEAAllhkKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2323
Cdd:pfam17380 281 QKAVSERQQQEKfEKMEQERLRQEKEE---KAREVERRRKLEEAEKA----RQAEMDRQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2324 RKEAEKEASRRAEaeaaalklKQEADSEMAKYKKLAektlkqkssveeelvkvKVQLDETDKQKsvldvelkRLKQEVSD 2403
Cdd:pfam17380 354 RQEERKRELERIR--------QEEIAMEISRMRELE-----------------RLQMERQQKNE--------RVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2404 AIKQKAQVEDELSKVKIQMEDllklklkiekenQELMKKDKDNTKKlleeeaENMKKLAEEAARlnieaqEAARLRQiae 2483
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVE------------MEQIRAEQEEARQ------REVRRLEEERAR------EMERVRL--- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2484 SDLAKQRElaekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEakKEMQQRLdqetegfQKSLEAERKRQLeI 2563
Cdd:pfam17380 454 EEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE--KELEERK-------QAMIEEERKRKL-L 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2564 TAEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2628
Cdd:pfam17380 519 EKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1689-1908 |
5.03e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.21 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1689 AQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledLEKFKLQA-EEAERHLKQAELEKQRQIQVVEEVA 1767
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQ-----------------LEKERLAAqEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1768 KKTAATQLESKQVAltARLEESLKneqvmviqlQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRlRLQAEEEA 1846
Cdd:PRK09510 140 KAAAAAKAKAEAEA--KRAAAAAK---------KAAAEAKKKAEAEAAkKAAAEAKKKAEAEAAAKAAAEA-KKKAEAEA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 1847 NKKTaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1908
Cdd:PRK09510 208 KKKA-------------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2357-2788 |
6.03e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2357 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkieken 2436
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2437 qelmkkdkdntkklLEEEAENMKKL-AEEAARLNIEAQEAARLRQIAEsdlaKQRELAEKMLEEKKQAIQEAAKLKAEAE 2515
Cdd:COG4717 141 --------------LAELPERLEELeERLEELRELEEELEELEAELAE----LQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2516 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQ-SKAEEEAKKFKKQ 2594
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLlSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2595 ADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2674
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2675 ILQQSFFAEKETLLKKEKAIEEEK-KKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ-KEAEEEMN 2752
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELE 442
|
410 420 430
....*....|....*....|....*....|....*...
gi 1207141740 2753 GKQKEMQDL--EKKRIEQEKLLAEENKNLREKLQQLQS 2788
Cdd:COG4717 443 ELEEELEELreELAELEAELEQLEEDGELAELLQELEE 480
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1688-2121 |
6.32e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1688 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1767
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1768 KKTAATQLESKQVALTARLEESLKneqvmviQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEAN 1847
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELK-------EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-IEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1848 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK--------QKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHA 1919
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAkkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1920 EQQRTVLDDELQRLKNDVNSAVKQKKELEE------------ELIKVRKEMEILLQQKSKAEKEtMSNTEKsKQLLESEA 1987
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTEehrkelleeytaELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1988 AKMRELAEEatkLRSVAEEAKKqrqIAEEEAARQRAEAEK-------------ILKEKLTAINEATRLKTEAEIALKEKE 2054
Cdd:PRK03918 496 IKLKELAEQ---LKELEEKLKK---YNLEELEKKAEEYEKlkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELE 569
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2055 AENDRLKRKAEEEGYqrKVLEDqaaqhkqaIEEKIGQLKKSSD--TELDRQKKIVEETLKQRKVVEEEI 2121
Cdd:PRK03918 570 EELAELLKELEELGF--ESVEE--------LEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEEL 628
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1736-2510 |
6.84e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.02 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1736 EKFKLQAEEAERHLKQAELekqrqIQVVEEVAKKTAATQLESKQVaLTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAD 1815
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQA-----IAGIMKIRPEFTKLQQEFNTL-ESAELRLSHLHFGYKSDETLIASRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1816 KAREQAEKELEtWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA---KKRAKAEEAALKQKEAAEME----- 1887
Cdd:pfam12128 288 LNQLLRTLDDQ-WKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLDAdieTAAADQEQLPSWQSELENLEerlka 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1888 -LGNQRKMAEETAKQKLAAEQELIR--------LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKK---ELEEELIKVR 1955
Cdd:pfam12128 366 lTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELREQLEAGKlefNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1956 KEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 2035
Cdd:pfam12128 446 LGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2036 INEATRLKTEAEIALKEkeaendrlkrkaeeegyqrkVLEDQAAQHKQAIEEKIgqlkkssDTELDRQKKIVEETLKQRK 2115
Cdd:pfam12128 522 LDELELQLFPQAGTLLH--------------------FLRKEAPDWEQSIGKVI-------SPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2116 VVEEEIHILKLNFEKAS-----SGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAA 2190
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG--------------ELEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2191 EEEAARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcSAAEQKAQNVLVQQNKD----SMAQDKL 2264
Cdd:pfam12128 641 ETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQL-KQLDKKHQAWLEEQKEQkreaRTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2265 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER------------QKKAAEAEAAKQAKAQEDAEKLRKEA-EKEA 2331
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYkrdlaslgvdpdVIAKLKREIRTLERKIERIAVRRQEVlRYFD 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2332 SRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQK--- 2408
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKeda 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2409 --AQVEDELSKVKIQMED-LLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNieaqeAARLRQIAESD 2485
Cdd:pfam12128 880 nsEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQN-----DKGIRLLDYRK 954
|
810 820
....*....|....*....|....*.
gi 1207141740 2486 LAKQRE-LAEKMLEEKKQAIQEAAKL 2510
Cdd:pfam12128 955 LVPYLEqWFDVRVPQSIMVLREQVSI 980
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1736-2084 |
7.06e-10 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 65.42 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1736 EKFKLQAEEAERHLK------QAELEKQRQIQVVE----------------EVAKKTAATQLESK-QVALTARLEESLKN 1792
Cdd:NF033838 54 ESQKEHAKEVESHLEkilseiQKSLDKRKHTQNVAlnkklsdikteylyelNVLKEKSEAELTSKtKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1793 eqvmVIQLQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRA 1871
Cdd:NF033838 134 ----TLEPGKKVAEATKKVEEAEkKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1872 KAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAEQE--LIRLRADFEHAEQQRTVLDDELQRL------KNDVNS--- 1939
Cdd:NF033838 210 KAKVES-KKAEATRLEkIKTDREKAEEEAKRRADAKLKeaVEKNVATSEQDKPKRRAKRGVLGEPatpdkkENDAKSsds 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1940 ----------AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSkqlLESEAAKMRELAEEAtKLRSVAEEAKK 2009
Cdd:NF033838 289 svgeetlpspSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKT---LELEIAESDVKVKEA-ELELVKEEAKE 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2010 QRQIAEEEAARQRAEAEKIlkekltainEATRL-KTEAEIALKEKEAendrlKRKAEEEgyqRKVLEDQAAQHKQA 2084
Cdd:NF033838 365 PRNEEKIKQAKAKVESKKA---------EATRLeKIKTDRKKAEEEA-----KRKAAEE---DKVKEKPAEQPQPA 423
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1291-2016 |
8.21e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1291 VIRSTQGAEDILNKYENqLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQatfDRLEEELQRATEVNKRMSQLHSERDvE 1370
Cdd:PRK03918 150 VVRQILGLDDYENAYKN-LGEV------IKEIKRRIERLEKFIKRTENIE---ELIKEKEKELEEVLREINEISSELP-E 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1371 LEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYdwlirwiadakqrqdklhavpiggsKGLQEQLTQEKK 1450
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-------------------------RELEERIEELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1451 LLEEIEKNKDKVEDCQKFAKGYIDAIKDYElqlvtykalvepiasplkkaKMESASDDIIQEYVTLRTRYSELmtlssqy 1530
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYE--------------------EYLDELREIEKRLSRLEEEINGI------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1531 ikfiietQRRLQDEEKaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKdevskrqdvavdsek 1610
Cdd:PRK03918 327 -------EERIKELEE------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE--------------- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1611 qkhNIQRELQELKTLSEQEIKAKSQQVEEAllsRTRIEEEIHII---RLQLETTMKQKNTAETELLQLRAKAV------- 1680
Cdd:PRK03918 373 ---ELERLKKRLTGLTPEKLEKELEELEKA---KEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPvcgrelt 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1681 --DADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1758
Cdd:PRK03918 447 eeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-----LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1759 qiqvveevAKKTAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL 1838
Cdd:PRK03918 522 --------KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1839 RLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEH 1918
Cdd:PRK03918 593 RLKELEPFYNEYL--------------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1919 AEQQRtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlqqksKAEKETMSNTEKSKQLLESEAAKMRELAEEAT 1998
Cdd:PRK03918 659 EEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKELEKLEKALERVEELREKVK 731
|
730 740
....*....|....*....|
gi 1207141740 1999 KLRSVAEEA--KKQRQIAEE 2016
Cdd:PRK03918 732 KYKALLKERalSKVGEIASE 751
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2440-2602 |
8.95e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 64.10 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2440 MKKDKDNTKKLLEEEAENMKK--LAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKL 2517
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKqrAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2518 QKQKDQAQveAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT--AEAEKLKVKVTQlsdAQSKAEEEAKKFKKQA 2595
Cdd:TIGR02794 142 RKAKEEAA--KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEakAKAEEAKAKAEA---AKAKAAAEAAAKAEAE 216
|
....*..
gi 1207141740 2596 DEIKIRL 2602
Cdd:TIGR02794 217 AAAAAAA 223
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1799-2126 |
1.03e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.14 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1799 QLQEEAEHLKKQ---QAEADKAREQAEK----ELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREaKKRA 1871
Cdd:pfam17380 288 QQQEKFEKMEQErlrQEKEEKAREVERRrkleEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQEERKRE-LERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1872 KAEEAALKQKEAAEME-LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK--KELE 1948
Cdd:pfam17380 366 RQEEIAMEISRMRELErLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRleEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1949 EELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEeaaRQRAEAEKI 2028
Cdd:pfam17380 446 REMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE---RKRKLLEKE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2029 LKEKLTAINEATRLKTEAEIALKEKEAENDR----LKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 2104
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEERRriqeQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
330 340
....*....|....*....|..
gi 1207141740 2105 KIVEETLKQRKVVEEEIHILKL 2126
Cdd:pfam17380 602 PIYRPRISEYQPPDVESHMIRF 623
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
231-327 |
1.08e-09 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 58.74 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 231 KKTFTKWVNKHLVKaQRHIT----------DLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 295
Cdd:cd21217 3 KEAFVEHINSLLAD-DPDLKhllpidpdgdDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 1207141740 296 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 327
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1319-2001 |
1.16e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1319 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE-----VNKRMSQLHSER---DVELEHYRQLVGNLRERWQAVFA 1390
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrVKEKIGELEAEIaslERSIAEKERELEDAEERLAKLEA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1391 QIELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAK 1470
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1471 GYID--------------AIKDYELQLVTYKALVEPIASPLKKA--KMESASDDII---QEYVTLRTRYS----ELMTLS 1527
Cdd:TIGR02169 410 RLQEelqrlseeladlnaAIAGIEAKINELEEEKEDKALEIKKQewKLEQLAADLSkyeQELYDLKEEYDrvekELSKLQ 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1528 SQYIKfiIETQRRLQDEE----KAAEKLKEEERKKMAEMQAELEKQKqlaETHAKAI----------------AKAEQEA 1587
Cdd:TIGR02169 490 RELAE--AEAQARASEERvrggRAVEEVLKASIQGVHGTVAQLGSVG---ERYATAIevaagnrlnnvvveddAVAKEAI 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1588 NELK------------TKMKDE-----VSKRQDVA------VDSEKQKHN----------IQRELQELKTLS-------- 1626
Cdd:TIGR02169 565 ELLKrrkagratflplNKMRDErrdlsILSEDGVIgfavdlVEFDPKYEPafkyvfgdtlVVEDIEAARRLMgkyrmvtl 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1627 EQEIKAKS------------------QQVEEALLSRTRIEEeihiIRLQLETTMKQKNTAETELLQLRAKAVDADKL--- 1685
Cdd:TIGR02169 645 EGELFEKSgamtggsraprggilfsrSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKige 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1686 ----RNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL-EKQRQI 1760
Cdd:TIGR02169 721 iekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAEL 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1761 QVVEEVAkktaatqleSKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELetwrqkanEALRLRL 1840
Cdd:TIGR02169 801 SKLEEEV---------SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI--------ENLNGKK 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1841 QAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEaaemelgNQRKMAEETAKQKLAaeqeliRLRADFEHAE 1920
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI-------EELEAQIEKKRKRLS------ELKAKLEALE 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1921 QQRTVLDDELQRLKNDVNSA------VKQKKELEEELIKVrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELA 1994
Cdd:TIGR02169 931 EELSEIEDPKGEDEEIPEEElsledvQAELQRVEEEIRAL-EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009
|
....*..
gi 1207141740 1995 EEATKLR 2001
Cdd:TIGR02169 1010 EEYEKKK 1016
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2998-3036 |
1.19e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 56.18 E-value: 1.19e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 2998 LLDCQYATGGIIDPVNSHHVPVQLACTQGQLDEDLSKIL 3036
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1478-2125 |
1.64e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1478 DYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKE---E 1554
Cdd:pfam05483 38 DPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1555 ERKKMAEMQAELEKqkqlaethakaiakaeqeaneLKTKMKDEVSKRQDVAVDSEKQKHnIQRELQELKTLSEQEIKAKS 1634
Cdd:pfam05483 118 QRKAIQELQFENEK---------------------VSLKLEEEIQENKDLIKENNATRH-LCNLLKETCARSAEKTKKYE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1635 QQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETEL-LQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE 1713
Cdd:pfam05483 176 YEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1714 LKRKSEAEKDAAKEKKKALedlEKFKLQAEeaerHLKQAELEKQRQIQVVEEVakKTAATQLESKQVAltarLEESLKNE 1793
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLE---EKTKLQDE----NLKELIEKKDHLTKELEDI--KMSLQRSMSTQKA----LEEDLQIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1794 QVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL---RLQAEEEANKKTAAQEEAEKQKEEAKREAKKR 1870
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1871 AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRL----RADFEHAEQQRTVLD-------DELQRLKNDVNS 1939
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKtseehylKEVEDLKTELEK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1940 AVKQKKELEEELIKVRKEMEILLQQKS------KAEKETMSNTEKSKQ--------LLESEAAKMRELAEEATKLRSVAE 2005
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASdmtlelKKHQEDIINCKKQEErmlkqienLEEKEMNLRDELESVREEFIQKGD 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2006 EAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKV-------LE 2075
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGSAENKQLNAyeikvnkLE 642
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2076 DQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 2125
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2346-2567 |
1.70e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2346 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2425
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2426 LKLKLKIEKENQElmkkDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2505
Cdd:COG4942 117 GRQPPLALLLSPE----DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2506 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegfqksLEAERKRQLEITAEA 2567
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR--------LEAEAAAAAERTPAA 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2262-2781 |
1.94e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2262 DKLKEEFEKAKKLAQEAEKAKD-------NAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRR 2334
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDkflteikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2335 AEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEE---ELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ- 2410
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQn 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2411 ------VEDELSKVKIQMEDLLKLKlkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQI--- 2481
Cdd:TIGR04523 280 nkkikeLEKQLNQLKSEISDLNNQK------EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltn 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2482 AESD-LAKQRELAEKmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQ 2560
Cdd:TIGR04523 354 SESEnSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQINDLE---SKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2561 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADL 2640
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2641 EKEKEklkkeaaDLQKQSKEMaNVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklekqfeDEVKKAEALKAE-Q 2719
Cdd:TIGR04523 509 EEKVK-------DLTKKISSL-KEKIEKLESEKKEKESKISDLEDELNKD----------------DFELKKENLEKEiD 564
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2720 ERQRKLmeeerKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2781
Cdd:TIGR04523 565 EKNKEI-----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4574-4612 |
2.25e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.41 E-value: 2.25e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 4574 FLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTAQKL 4612
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
345-442 |
2.28e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 58.16 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90
....*....|....*....
gi 1207141740 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLS 106
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
232-326 |
2.77e-09 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 57.35 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 232 KTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 303
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1207141740 304 VNIRNDDIADGNPKLTLGLIWTI 326
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1736-2403 |
2.94e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.59 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1736 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtaRLEESLKNEQVMVIQ----------LQE--- 1802
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSL--KLEEEIQENKDLIKEnnatrhlcnlLKEtca 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1803 -EAEHLKKQQAEADKARE-------------QAEKELETWRQKANEALRLRLQA--------EEEANKKTAAQEEAEKQK 1860
Cdd:pfam05483 166 rSAEKTKKYEYEREETRQvymdlnnniekmiLAFEELRVQAENARLEMHFKLKEdhekiqhlEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1861 EEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ----RTVLDDELQRLKND 1936
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1937 VNSAVKQKKELEEELIKVRKEMEIL----------LQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLrsvaee 2006
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAHSFVvtefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKF------ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2007 aKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIAL----KEKEAENDRLK---RKAEEEGYQRKVLEDQA 2078
Cdd:pfam05483 400 -KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFllqaREKEIHDLEIQltaIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2079 AQHKQAIE---------------EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELK 2143
Cdd:pfam05483 479 ELEKEKLKnieltahcdklllenKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2144 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2223
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2224 KEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAllHKKAEEAERQk 2303
Cdd:pfam05483 636 IKVNKLELELASAKQK---FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ--HKIAEMVALM- 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2304 kaaeaeaakqakaqedaEKLRKEAEkeasrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDET 2383
Cdd:pfam05483 710 -----------------EKHKHQYD--------------KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSL 758
|
730 740
....*....|....*....|
gi 1207141740 2384 DKQKSVLDVELKRLKQEVSD 2403
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1165-1915 |
4.55e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1165 LLRSVEQGEQDESVCKSYITQIKDLRLRLEgcesRTVNRLRQMVDKEPLKACTQRATEQKKVQTELEGIKKDLDKVvEKS 1244
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL-ERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1245 EAVLATSQQSSSAPV--LRSEIDITQKKMEhvyGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNK-VPVNEKE 1321
Cdd:TIGR02169 310 IAEKERELEDAEERLakLEAEIDKLLAEIE---ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKeFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1322 IEASQTQLQKLRSEAEGKQATFDRLEEELQRATE-----------VNKRMSQLHSERDV-----------------ELEH 1373
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEeladlnaaiagIEAKINELEEEKEDkaleikkqewkleqlaaDLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1374 YRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLHAvPIGGSKGLQEQLTQ-EKKLL 1452
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-------VRGGRAVEEVLKA-SIQGVHGTVAQLGSvGERYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1453 EEIE------------KNKDKVEDCQKFAK------------------------GYIDAIKDYELQLVTYKALVEPI--- 1493
Cdd:TIGR02169 539 TAIEvaagnrlnnvvvEDDAVAKEAIELLKrrkagratflplnkmrderrdlsiLSEDGVIGFAVDLVEFDPKYEPAfky 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1494 --ASPLKKAKMESASDDIIQ-EYVTLRTRYSE---LMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELE 1567
Cdd:TIGR02169 619 vfGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRSEPAEL--------------QRLRERLE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1568 KQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRI 1647
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKEL 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1648 EEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdadklrnaaQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE 1727
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSRIPEI---------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1728 KKKALEDLEKFKLQAEEAERhlKQAELEKQrqiqvveevaKKTAATQLESKQVALtARLEESLKNeqvmviqLQEEAEHL 1807
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEK--EIENLNGK----------KEELEEELEELEAAL-RDLESRLGD-------LKKERDEL 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1808 KKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAA 1884
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSE-LKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
|
810 820 830
....*....|....*....|....*....|....*..
gi 1207141740 1885 EMELGNQRKMAEET------AKQKLAAEQELIRLRAD 1915
Cdd:TIGR02169 974 NMLAIQEYEEVLKRldelkeKRAKLEEERKAILERIE 1010
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1112-1909 |
4.83e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 63.07 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1112 KTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKAT---QHYDNLLRSVEQGEQDESVCKSYI-TQIK 1187
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEeklAQVLKENKEEEKEKKLQEEELKLLaKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1188 DLRLRLEGCESRTVNRLRQMV-DKEPLKACTQRATEQKKVQTELEGIKKDLDKVVEKSE-AVLATSQQSSSAPVLRSEID 1265
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKeSEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEeEEEELEKLQEKLEQLEEELL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1266 ITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREvnkvpvNEKEIEASQTQLQKLRSEAEGKQATFDR 1345
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK------EEKKEELEILEEEEESIELKQGKLTEEK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1346 LEEELQRATEVNKRMS------QLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAY-----RESYD 1414
Cdd:pfam02463 451 EELEKQELKLLKDELElkksedLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggriiSAHGR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1415 WLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEE----------IEKNKDKVEDCQKFAKGYIDAIKDYEL--- 1481
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALtelplgarklRLLIPKLKLPLKSIAVLEIDPILNLAQldk 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1482 ------QLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEE 1555
Cdd:pfam02463 611 atleadEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1556 RkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvAVDSEKQKHNIQRELQELKTLSEQEIKAKSQ 1635
Cdd:pfam02463 691 K---EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI--NEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1636 QVEEALLSRTRIEEEIHIIRLQLEttmKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELK 1715
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVE---EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1716 RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQV 1795
Cdd:pfam02463 843 KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1796 MV------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL------RLQAEEEANKKTAAQEEAEKQKEEA 1863
Cdd:pfam02463 923 IKeeaeilLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEElgkvnlMAIEEFEEKEERYNKDELEKERLEE 1002
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1207141740 1864 KREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1909
Cdd:pfam02463 1003 EKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1563-2104 |
5.61e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 62.93 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1563 QAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAL 1641
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1642 LsRTRIEEEIHIIRL-QLETTMKQKNTAETELLQLRAKavdaDKLRNAAQEEAEKLRKQVaeetqkkrkaeEELKRksea 1720
Cdd:pfam12128 433 L-EFNEEEYRLKSRLgELKLRLNQATATPELLLQLENF----DERIERAREEQEAANAEV-----------ERLQS---- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1721 ekdaakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQiqvveevakKTAATQLESKQVALTARLEESLKNEqvmviqL 1800
Cdd:pfam12128 493 -------------ELRQARKRRDQASEALRQASRRLEER---------QSALDELELQLFPQAGTLLHFLRKE------A 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1801 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEAL---RLRLQAEEeankktaaQEEAEKQKEEAKREAKKRAKAEEAA 1877
Cdd:pfam12128 545 PDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvKLDLKRID--------VPEWAASEEELRERLDKAEEALQSA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1878 LKQKEAAEMELGNQRKMAEEtakqklaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRK 1956
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEK-------ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1957 EMEIL---LQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklRSVAEEAKKQRQIAEEEAARQRAEA-EKILKEK 2032
Cdd:pfam12128 690 QLKQLdkkHQAWLEEQKEQKREARTEKQ------AYWQVVEGA----LDAQLALLKAAIAARRSGAKAELKAlETWYKRD 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2033 LTA--INEATRLKTEAEIALKEKEAENDRLKRKA---------EEEGYQRKVLEDQAAQHKQAIEEKIGQL-KKSSDTEL 2100
Cdd:pfam12128 760 LASlgVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKL 839
|
....
gi 1207141740 2101 DRQK 2104
Cdd:pfam12128 840 RRAK 843
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1658-1902 |
6.08e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.40 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1658 LETTMKQKNTAETELLQLRAKAVDADKlrnaAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlEK 1737
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAK----KEQERQKKLEQQAEEAEKQRAAEQARQKE------------------LE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1738 FKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNeqvmviqlQEEAEHLKKQQAEADKA 1817
Cdd:TIGR02794 96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--------QAEEEAKAKAAAEAKKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1818 REQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAalkQKEAAEMELGNQRKMAEE 1897
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA---ERKADEAELGDIFGLASG 243
|
....*
gi 1207141740 1898 TAKQK 1902
Cdd:TIGR02794 244 SNAEK 248
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4496-4533 |
7.12e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 7.12e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1207141740 4496 QRLLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMV 4533
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2370-2597 |
8.43e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2370 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekeNQELmkkdkdntKK 2449
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----------QAEI--------AE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2450 LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES----DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQ 2525
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2526 VEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2597
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1210-2064 |
9.00e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1210 KEPLKACTQRATEQKKVQT---ELEGIKKDLDKVVEKSEAVLATSQQSSS--APVLRSEIDITQKKMEHVYGlssvyldk 1284
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASleeELEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKEKIGELEA-------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1285 lkTIDLVIRSTQGAEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ-RATEVNKRMSQL 1363
Cdd:TIGR02169 302 --EIASLERSIAEKERELEDAEERLAKL------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAeLKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1364 HSErDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQE 1443
Cdd:TIGR02169 374 EEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1444 QLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPI--ASPLKKAKMESASDDIIQEYVTLRtrys 1521
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeeRVRGGRAVEEVLKASIQGVHGTVA---- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1522 ELMTLSSQYIKFI-IETQRRLQ-----DEEKAAEKLkeeerkkmaemqaELEKQKQLAETHAKAIAKAEQEANELKTKMK 1595
Cdd:TIGR02169 529 QLGSVGERYATAIeVAAGNRLNnvvveDDAVAKEAI-------------ELLKRRKAGRATFLPLNKMRDERRDLSILSE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1596 DEVSKRQDVAVDSEKQKHNIQRE-------LQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKnta 1668
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFKYvfgdtlvVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSE--- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1669 ETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaaKEKKKALEDLEKFKLQAEEAERH 1748
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEED 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1749 LKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMviQLQEEAEHLKKQQAEADKAREQAEKELet 1827
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKL-- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1828 wrqkaNEALRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALkqkEAAEMELGNQRKMAEETAKQKLAAEQ 1907
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQEL-----------QEQRIDLKEQIKSIEKEI---ENLNGKKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1908 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELikvrkemEILLQQKSKAEKETMSNTEKSKQLLESE- 1986
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEEELSLEd 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 1987 -AAKMRELAEEATKLRSVAEEAKKQrqiAEEEAARQraeaeKILKEKLtaineaTRLKTEAEiALKEKEAENDRLKRKA 2064
Cdd:TIGR02169 956 vQAELQRVEEEIRALEPVNMLAIQE---YEEVLKRL-----DELKEKR------AKLEEERK-AILERIEEYEKKKREV 1019
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2346-2624 |
1.24e-08 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 61.27 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2346 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQldetdkqksvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2425
Cdd:pfam03528 14 EKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE-------------DLKRQNAVLQEAQVELDALQNQLALARAEMENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2426 LKLKLKIEKENQELMkkdkDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQ 2505
Cdd:pfam03528 81 KAVATVSENTKQEAI----DEVKSQWQEEVASLQAIMKETVR-EYEVQFHRRLEQ-ERAQWNQYRESAEREIADLRRRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2506 EAAklkaEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ------ETEGFQKSLEAERKRQLEITAEAEK-----LKVKV 2574
Cdd:pfam03528 155 EGQ----EEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAEKscrtdLEMYV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2575 TQLSDAQSKAEEEAKKFKKQADEIKIRL-QETEKHTSEKHTVVEK----LEVQRL 2624
Cdd:pfam03528 231 AVLNTQKSVLQEDAEKLRKELHEVCHLLeQERQQHNQLKHTWQKAndqfLESQRL 285
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1857-2066 |
1.30e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1857 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKmaeetakqklAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1936
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----------ALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1937 VNSAVKQKKELEEELIKV---------RKEMEILLQQKSKAEKETMSNTEKS-KQLLESEAAKMRELAEEATKLRSVAEE 2006
Cdd:COG4942 92 IAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2007 AKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE 2066
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
230-329 |
1.34e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 55.97 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 230 QKKTFTKWVNKhlVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILH 329
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
345-442 |
1.96e-08 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 55.56 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 345 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1207141740 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1926-2679 |
2.10e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.14 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1926 LDDELQRLKNDVNSAVKQKKELEEELIKV--RKEMEILLQQKSKAEKETMSNT--------EKSKQLLESEAAK-MRELA 1994
Cdd:TIGR00618 83 LGTKIYRVHRTLRCTRSHRKTEQPEQLYLeqKKGRGRILAAKKSETEEVIHDLlkldyktfTRVVLLPQGEFAQfLKAKS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1995 EEATKLRSVAEEAKKQRQIAeeeaarqrAEAEKILKEkltaineatrLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVL 2074
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLA--------LMEFAKKKS----------LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2075 EDQAAQhkqaIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL-NFEKASSGKQELELELKKLKGIADETQ 2153
Cdd:TIGR00618 225 EKELKH----LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELrAQEAVLEETQERINRARKAAPLAAHIK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2154 ----------------KSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAA---QEEVGRLMKLAEE 2214
Cdd:TIGR00618 301 avtqieqqaqrihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQH 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2215 AKKQKEIAEKEAEKQVILVQE-----AAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEA 2289
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKEldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2290 ALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSV 2369
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2370 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK---------IQMEDLLKLKLKIEKENQELM 2440
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrlqdlTEKLSEAEDMLACEQHALLRK 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2441 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEA--------QEAARLRQIAESDLAKQRELAEKMLEEKKQAI-------- 2504
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQltltqervREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemla 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2505 QEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgFQKSLEAERKRQLEITAEAEKLK----VKVTQLSDA 2580
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFNNneevTAALQTGAE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2581 QSKAEEEAKKFKKQADEIKIRLQETE-KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKeaadLQKQSK 2659
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEaEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH----QLLKYE 855
|
810 820
....*....|....*....|
gi 1207141740 2660 EMANVQQEQLQQEKTILQQS 2679
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLS 875
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1885-2628 |
2.15e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.90 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1885 EMELGNQRKMAEETAKQKLAaeqeliRLRADFEHAEQqrtvlddELQRLKNDVNSA-VKQKKELEEELIKVRKEMeillq 1963
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEHIE------RVLEEYSHQVK-------DLQRRLNESNELhEKQKFYLRQSVIDLQTKL----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1964 QKSKAEKETMSNTEKSkqllesEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK 2043
Cdd:pfam15921 120 QEMQMERDAMADIRRR------ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2044 TEAEIALKEKEAENDRL-----KRKAEEEGYQRKVLEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRk 2115
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISYLKGRIfpvEDQLEALKSESQNKIELLLQQHQDRIEQL- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2116 VVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQKskakaeEEAEKFRKLAleeekkrkEAEAKVKQIQAAEEEAA 2195
Cdd:pfam15921 273 ISEHEVEITGLT-EKASSARSQANSIQSQLEIIQEQARN------QNSMYMRQLS--------DLESTVSQLRSELREAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2196 RQHKAAQEEVGRLMKLAE----EAKKQKEIAEKEA-------EKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2264
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANseltEARTERDQFSQESgnlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2265 KEEFEKAKKLAQEAE--------KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKL--RKEAEKEASRR 2334
Cdd:pfam15921 418 RRELDDRNMEVQRLEallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtaKKMTLESSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2335 AEAEAAALKLKQEA----DSEMAKYK-----KLAE-KTLKQKS----SVEEELVKVKVQLDETDKQKSVLDVELKRLKQE 2400
Cdd:pfam15921 498 VSDLTASLQEKERAieatNAEITKLRsrvdlKLQElQHLKNEGdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2401 V------SDAIK-QKAQVEDELSKVKIQMEDLlklklkiekenqELMKKDKDNTKKLLEEEAENMkklaeEAARLNIEAQ 2473
Cdd:pfam15921 578 VgqhgrtAGAMQvEKAQLEKEINDRRLELQEF------------KILKDKKDAKIRELEARVSDL-----ELEKVKLVNA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2474 EAARLRqiAESDLAKQRElaeKMLEEKKQAIQEAAKLKAEAEKLQK----QKDQAQVEAQKLLEAKKEMQQRLDQeTEGF 2549
Cdd:pfam15921 641 GSERLR--AVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQ-TRNT 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2550 QKSLEAERKR--------QLEITA---EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEK 2618
Cdd:pfam15921 715 LKSMEGSDGHamkvamgmQKQITAkrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS---QELSTVATEKNKMAGE 791
|
810
....*....|
gi 1207141740 2619 LEVQRLQSKQ 2628
Cdd:pfam15921 792 LEVLRSQERR 801
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2285-2788 |
2.56e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2285 AEKEAALLHKKAEEAErqkkaaeaeaakQAKAQEDAEKLRKEAEKEASRRAeaeaaalklKQEADSEMAKYkklaEKTLK 2364
Cdd:PRK02224 197 EEKEEKDLHERLNGLE------------SELAELDEEIERYEEQREQARET---------RDEADEVLEEH----EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2365 QKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD-----------------AIKQKAQVEDELSKVKIQMEDLLK 2427
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaeaglddaDAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2428 LKLKIEKENQELMKKDKDNTKKlLEEEAenmKKLAEEAARLNIEAQEAARLRQIAESDLAK-----------------QR 2490
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADD-LEERA---EELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdapvDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2491 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2570
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2571 KVKVTQLSDAQSKAeEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvQRLQSKQEADGLHKAIADLEKEKEKLKKE 2650
Cdd:PRK02224 488 EEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKR-ERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2651 AADLQKQSKEMANVQQEQLQQEKTILqqsffAEKETLLKKEKAIEEEKKKLEKQFED----EVKKAEALKAEQERQRKL- 2725
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelNDERRERLAEKRERKRELe 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2726 --MEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKK------RIEQEKLLAEENKNLREKLQQLQS 2788
Cdd:PRK02224 641 aeFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavenELEELEELRERREALENRVEALEA 712
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1875-2562 |
2.60e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.62 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1875 EAALKQKEAAEMELGNQRKmaEETAKQKLAAEQELIRLRADFEHAEQQRTvLDDELQRLKNDVNSavkQKKELEEELIKV 1954
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHF--GYKSDETLIASRQEERQETSAELNQLLRT-LDDQWKEKRDELNG---ELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1955 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEE----ATKLRSVAEEAKKQRQIAEEEAARQRAEaekiLK 2030
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERlkalTGKHQDVTAKYNRRRSKIKEQNNRDIAG----IK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2031 EKLTAINEA-TRLKTEAEIALKEKEA----ENDRLKRKAEEEGYQrkvledqaaqhkqaIEEKIGQLKKSSDteldrQKK 2105
Cdd:pfam12128 397 DKLAKIREArDRQLAVAEDDLQALESelreQLEAGKLEFNEEEYR--------------LKSRLGELKLRLN-----QAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2106 IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQkskakaeeeaekfRKLALeeekkrkeAEAKVK 2185
Cdd:pfam12128 458 ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS-------------EALRQ--------ASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2186 QIQAAEEEAARQHKAAQeevGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL---------VQQN 2255
Cdd:pfam12128 517 ERQSALDELELQLFPQA---GTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvkldlkrIDVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2256 KDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEkeasrra 2335
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR--------------EETFARTALKNAR------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2336 eaeaaaLKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDEL 2415
Cdd:pfam12128 653 ------LDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2416 SKVKI-QMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES---------- 2484
Cdd:pfam12128 727 LDAQLaLLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwl 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2485 ----DLAKQRELAEKMLEEKKQ---AIQEAAKLK-AEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL-----DQETEGFQK 2551
Cdd:pfam12128 807 qrrpRLATQLSNIERAISELQQqlaRLIADTKLRrAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkeDANSEQAQG 886
|
730
....*....|.
gi 1207141740 2552 SLeAERKRQLE 2562
Cdd:pfam12128 887 SI-GERLAQLE 896
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1868-2604 |
3.01e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.51 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1868 KKRAKAEEAALKQKEAaemELGNQRKM--AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR-----LKNDVNSA 1940
Cdd:pfam05483 91 KKWKVSIEAELKQKEN---KLQENRKIieAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1941 VKQKKELEEELIKVRkemEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 2020
Cdd:pfam05483 168 AEKTKKYEYEREETR---QVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2021 ---QRAEAEKILKEkLTAINEATRLKTEAeiaLKEK-EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIeekigqlkkSS 2096
Cdd:pfam05483 245 lliQITEKENKMKD-LTFLLEESRDKANQ---LEEKtKLQDENLKELIEKKDHLTKELEDIKMSLQRSM---------ST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2097 DTELDRQKKIVEETLKQRkVVEEEIHILKLNfeKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKK 2176
Cdd:pfam05483 312 QKALEEDLQIATKTICQL-TEEKEAQMEELN--KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2177 RKEAEAKVKQIQAAEEEAARQHKAAqeeVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQNK 2256
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKI---LAEDEKLLDEKKQFEKIAEELKGKE----QELIFLLQAREKEIHDLEIQLTA 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2257 DSMAQDKLKEEFEKAKKlaqEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAE 2336
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKT---ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2337 AEAAALKLKQEADSemakykklAEKTLKQKSSveeelvKVKVQLDETDKQKsvldvelKRLKQEVSDAIKQKAQVEDELS 2416
Cdd:pfam05483 539 LEEKEMNLRDELES--------VREEFIQKGD------EVKCKLDKSEENA-------RSIEYEVLKKEKQMKILENKCN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2417 KVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAE-NMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEk 2495
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE- 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2496 mLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLDQETE---GFQKSLEAERKR-QLEITAEAEKLK 2571
Cdd:pfam05483 677 -VEKAKAIADEAVKLQKEIDKRCQHK---IAEMVALMEKHKHQYDKIIEERDselGLYKNKEQEQSSaKAALEIELSNIK 752
|
730 740 750
....*....|....*....|....*....|...
gi 1207141740 2572 VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE 2604
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2706-2890 |
3.23e-08 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 60.23 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2706 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ--------KEAEEEMNGKQKEMQDLEKKRIEQ--EKLLAEE 2775
Cdd:PRK00409 533 EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAHELIEA 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2776 NKNLREKLQQLQSSQKASYTKEIEIQT-DKVPEEELVQMTMVETTKKvlngstevdgvKKDVPLAFDGIREKVPASRLHE 2854
Cdd:PRK00409 613 RKRLNKANEKKEKKKKKQKEKQEELKVgDEVKYLSLGQKGEVLSIPD-----------DKEAIVQAGIMKMKVPLSDLEK 681
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207141740 2855 IGVLSKKEydklKKGKTTVQELSKNDKVKMCLKGKD 2890
Cdd:PRK00409 682 IQKPKKKK----KKKPKTVKPKPRTVSLELDLRGMR 713
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
340-442 |
3.97e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 54.33 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 340 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGV 418
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....
gi 1207141740 419 TRLLDPEDVDVPHPDEKSIITYVS 442
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLS 103
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2185-2329 |
4.10e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2185 KQIQAAEEE---AARQHKAAQEEvgrlMKLAEEAKKQKEIAEKEAEKQviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ 2261
Cdd:TIGR02794 81 EKQRAAEQArqkELEQRAAAEKA----AKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEE 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2262 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2329
Cdd:TIGR02794 155 EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAA 222
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2449-2799 |
4.25e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2449 KLLEEEAENMKKLAEEAARLnieaqeaarlrqiaeSDLAKQRELAEKMLEEKKQAIQE----AAKLKAEAEKLQKQKDQA 2524
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGI---------------SKYKERRKETERKLERTRENLDRlediLNELERQLKSLERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2525 QvEAQKLLEAKKEMQ--------QRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2596
Cdd:TIGR02168 213 E-RYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2597 EIKIRLQETEKhtsekhtvveklEVQRLQSKQEADglhkaiadlekekeklkkeaadlqKQSKEMANVQQEQLQQEKTIL 2676
Cdd:TIGR02168 292 ALANEISRLEQ------------QKQILRERLANL------------------------ERQLEELEAQLEELESKLDEL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2677 QQSFfAEKETLLKKEKAIEEekkklekQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQK 2756
Cdd:TIGR02168 336 AEEL-AELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1207141740 2757 EMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIE 2799
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1614-2135 |
4.38e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 59.66 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1614 NIQRELQELKTLSEQEIKAKSQQVEEaLLSRTRIEEEIhiiRLQLETTMKQKNTA--ETELLQLRAKAVD---ADKLRNA 1688
Cdd:pfam05701 46 KVQEEIPEYKKQSEAAEAAKAQVLEE-LESTKRLIEEL---KLNLERAQTEEAQAkqDSELAKLRVEEMEqgiADEASVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1689 AQE--EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKAledlekfklQAEEAERHLKQAElekqrqiQVVEEV 1766
Cdd:pfam05701 122 AKAqlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIK---------RAEEAVSASKEIE-------KTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1767 AKKTAATQlESKQVALTARLEeslKNEQVMVIQLQEEAEHLKKQqaeadKAREQAEKELETWRQK------------ANE 1834
Cdd:pfam05701 186 TIELIATK-ESLESAHAAHLE---AEEHRIGAALAREQDKLNWE-----KELKQAEEELQRLNQQllsakdlkskleTAS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1835 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKaeeAALKQKEAAEMElGNQRKMAEETAKQKLAAEQelirLRA 1914
Cdd:pfam05701 257 ALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAA---LASAKKELEEVK-ANIEKAKDEVNCLRVAAAS----LRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1915 DFehaEQQRTVLdDELQRLKNDVNSAVKQkkeLEEELIKVRKEMEiLLQQKSKAEKETMSNTEKskqlleseaaKMRELA 1994
Cdd:pfam05701 329 EL---EKEKAEL-ASLRQREGMASIAVSS---LEAELNRTKSEIA-LVQAKEKEAREKMVELPK----------QLQQAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1995 EEATKLRSVAEEAKKQRQIAEEEAARQRAEA-------EKILKEKLtAINEATRLKTEAEIALKEKEAEndrlKRKAEEE 2067
Cdd:pfam05701 391 QEAEEAKSLAQAAREELRKAKEEAEQAKAAAstvesrlEAVLKEIE-AAKASEKLALAAIKALQESESS----AESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2068 GYQRKV---LEDQAAQHKQA----------IEEKIGQLKKSSDTELDRQKKI--VEETLKQRKvveEEIHILKLNFEKAS 2132
Cdd:pfam05701 466 DSPRGVtlsLEEYYELSKRAheaeelankrVAEAVSQIEEAKESELRSLEKLeeVNREMEERK---EALKIALEKAEKAK 542
|
...
gi 1207141740 2133 SGK 2135
Cdd:pfam05701 543 EGK 545
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2448-2771 |
4.44e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.39 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2448 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQrELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2527
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ-ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2528 AQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA--DEIKIRLQET 2605
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNE-EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEekEREIARLRAQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2606 EKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffAEKE 2685
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREE--------EEFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2686 TLLkkekaieeekkklekqfEDEVKKAEALKAEQERQRKLMEEERKKLQSAMD---AAIKKQKEAEEEMNGKQKEMQDLE 2762
Cdd:pfam13868 265 RML-----------------RKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEereEQRAAEREEELEEGERLREEEAER 327
|
....*....
gi 1207141740 2763 KKRIEQEKL 2771
Cdd:pfam13868 328 RERIEEERQ 336
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1511-2113 |
6.15e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1511 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1590
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-------------LEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1591 KTKMKDevskrqdvavdsekqkhNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTmkqkntaET 1670
Cdd:COG4913 329 EAQIRG-----------------NGGDRLEQL----EREIERLERELEERERRRARLEALLAALGLPLPAS-------AE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1671 ELLQLRAKAVDadkLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA----- 1745
Cdd:COG4913 381 EFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1746 -------------------------------------ERHLKQA-------ELEKQRQIQVVEEVAKKTAATQLESKQVA 1781
Cdd:COG4913 458 aelpfvgelievrpeeerwrgaiervlggfaltllvpPEHYAAAlrwvnrlHLRGRLVYERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1782 ---------LTARLEESLkNEQVMVIQLqEEAEHLKKqqaeADKA----------REQAEKELETWRQKA------NEAL 1836
Cdd:COG4913 538 gkldfkphpFRAWLEAEL-GRRFDYVCV-DSPEELRR----HPRAitragqvkgnGTRHEKDDRRRIRSRyvlgfdNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1837 RLRLQAEEEAnkktaaqeeaEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR---KMAEETAKQKLAAEQELIRLR 1913
Cdd:COG4913 612 LAALEAELAE----------LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1914 ADFEHAEQqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMREL 1993
Cdd:COG4913 682 ASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1994 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE-KLTAINEATRLKTEAEiALKEKEAENDRLkrkaEEEGyqrk 2072
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRL----EEDG---- 828
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1207141740 2073 vLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 2113
Cdd:COG4913 829 -LPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
225-332 |
7.84e-08 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 54.24 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 225 ERDRVQKKTFTKWVNKHLVKAqrHITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 295
Cdd:cd21331 18 EGETREERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141740 296 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2184-2765 |
8.01e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2184 VKQIQAAEEEAARQHKAAQEEVGRLMKLAE---EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQnVLVQQNKDSMA 2260
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2261 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAA 2340
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK--------------ELEEKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2341 ALKLKQEADS-EMAKYKKLAEKTLKQKSSvEEELVKVKVQLDETDKQKSVLDVELKRLKQEvsdaikqKAQVEDELSKVK 2419
Cdd:PRK03918 354 LEELEERHELyEEAKAKKEELERLKKRLT-GLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2420 IQMEDLLKLKLKIEKENQELmkkDKDNTKKLLEEEAENMKKLAEEAARL-NIEAQEAARLRQI-----AESDLAKQRELA 2493
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGREL---TEEHRKELLEEYTAELKRIEKELKEIeEKERKLRKELRELekvlkKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2494 EKMLE-EKKQAIQEAAKLKAEAEKLQKQKdqaqveaQKLLEAKKEmqqrldqetegfQKSLEAERKRQLEITAEAEKLKV 2572
Cdd:PRK03918 503 EQLKElEEKLKKYNLEELEKKAEEYEKLK-------EKLIKLKGE------------IKSLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2573 KVTQLSDAQSKAEEEAKKFK-KQADEIKIRLQETEKHTSEKHTVVE-KLEVQRLQSKQE--ADGLHKAIADLEKEKEKLK 2648
Cdd:PRK03918 564 KLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDaEKELEREEKELKklEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2649 KEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKkklekqfedevKKAEALKAEQERqrklMEE 2728
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK-----------KTLEKLKEELEE----REK 708
|
570 580 590
....*....|....*....|....*....|....*..
gi 1207141740 2729 ERKKLQSamdaaIKKQKEAEEEMNGKQKEMQDLEKKR 2765
Cdd:PRK03918 709 AKKELEK-----LEKALERVEELREKVKKYKALLKER 740
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1263-2119 |
8.07e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1263 EIDITQKKMEHVYGLSSVYLDKLKTIDLVIRST--------QGAEDILNKYENQLREVNKvpvNEKEIEASQTQLQKLRS 1334
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYENELDPLKN---RLKEIEHNLSKIMKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1335 EAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFaqielrQRELDLLNRQMQAYRESYD 1414
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDC------QRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1415 WLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKklLEEIEKNKDKVEDCQKFAKGYIDAIKDyelqlvtykalvepia 1494
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIKNFHTLVIERQED---------------- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1495 splkKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQR-RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLA 1573
Cdd:TIGR00606 406 ----EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKeILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1574 ETHAKaIAKAEQEANeLKTKMKDEVSkRQDVAVDSEKQKHNIQRELQELKTLSEQEikaksQQVEEALLSRTRIEEEIHI 1653
Cdd:TIGR00606 482 KAERE-LSKAEKNSL-TETLKKEVKS-LQNEKADLDRKLRKLDQEMEQLNHHTTTR-----TQMEMLTKDKMDKDEQIRK 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1654 IRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE------ 1727
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcg 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1728 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMVIQLQEEAEH 1806
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTeAELQEFISDLQSKLRLAPDKLKS 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1807 LKKQQAEADKAREQAEKELETwrqKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1886
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPG---RQSI-IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1887 ELGNQRKMAEETAK-----QKLAAEQELIRLRADFEHAEQQRTVLDDELQRlkndvnsaVKQKKELEEELIKVRKEMEIL 1961
Cdd:TIGR00606 790 DVTIMERFQMELKDverkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDT--------VVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1962 LQQKS---KAEKETMS-NTEKSKQLLESEAAKMRELAEEATKLRSVAEE------AKKQRQIAEEEAARQRAEAEKILKE 2031
Cdd:TIGR00606 862 LKSKTnelKSEKLQIGtNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLEKDQQEKEELISSKETSNKKAQD 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2032 KLTAINEATRLKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTElDRQKKIVEET 2110
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ-KIQERWLQDN 1020
|
....*....
gi 1207141740 2111 LKQRKVVEE 2119
Cdd:TIGR00606 1021 LTLRKRENE 1029
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2184-2388 |
9.42e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.55 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2184 VKQIQAAEEEAArqhKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDsmAQDK 2263
Cdd:TIGR02794 52 ANRIQQQKKPAA---KKEQERQKKLEQQAEEAEKQRA-AEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA--EEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2264 LKEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAL 2342
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAErKAKEEAAKQAEEEAKAKAAAEAKKKAEE--AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141740 2343 KLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKS 2388
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1743-2301 |
9.87e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1743 EEAERHLKQAElEKQRQIQVVEEVAKK-TAATQLESKQVALTARLEesLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1821
Cdd:COG4913 238 ERAHEALEDAR-EQIELLEPIRELAERyAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1822 EKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKq 1901
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDR-----------------LEQLEREIERLERELEERERRRARLEALLAALGLPLP- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1902 klAAEQELIRLRADfehAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSkaeketmsntekskq 1981
Cdd:COG4913 377 --ASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS--------------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1982 LLESEAAKMRELAEEATK-----LRSVAEEAkkqrQIAEEEAARQRAeAEKIL--------------KEKLTAINE---A 2039
Cdd:COG4913 437 NIPARLLALRDALAEALGldeaeLPFVGELI----EVRPEEERWRGA-IERVLggfaltllvppehyAAALRWVNRlhlR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2040 TRLKTEaeialKEKEAENDRLKRKAEEEGYQRKVL-------------------------EDQAAQHKQAIEEKiGQLKK 2094
Cdd:COG4913 512 GRLVYE-----RVRTGLPDPERPRLDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdsPEELRRHPRAITRA-GQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2095 SSDT-ELDRQKKIVEE------TLKQRKVVEEEIHILKLNFEKASSgkqelelELKKLKGIADETQKskakaeeeaekfR 2167
Cdd:COG4913 586 NGTRhEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEE-------RLEALEAELDALQE------------R 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2168 KLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKA 2247
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQA 725
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2248 QNVL--VQQNKDSMAQDKLKEEFEKAKKLAQEA------EKAKDNAEKEAALLHKKAEEAER 2301
Cdd:COG4913 726 EEELdeLQDRLEAAEDLARLELRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1615-2122 |
1.06e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1615 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE-----TELLQLRAKAVDADKLRNAA 1689
Cdd:COG4913 244 LEDAREQIELL--EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEleelrAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1690 QEEAEKLRKQVAE-ETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK 1768
Cdd:COG4913 322 REELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1769 K--TAATQLESKQVALTARLEEslkneqvmviqLQEEAEHLKKQQ----AEADKAREQAEKEL----------------- 1825
Cdd:COG4913 402 AleEALAEAEAALRDLRRELRE-----------LEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgelievr 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1826 ---ETWRQKANEAL---RLRL----QAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK---------EA 1883
Cdd:COG4913 471 peeERWRGAIERVLggfALTLlvppEHYAAALRwvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrAW 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1884 AEMELGNQRKMAeetakqKLAAEQELIRL-RA----------------DFEHAEQQRTVLddelqrlkndVNSAVKQKKE 1946
Cdd:COG4913 551 LEAELGRRFDYV------CVDSPEELRRHpRAitragqvkgngtrhekDDRRRIRSRYVL----------GFDNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1947 LEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEE-AKKQRQIAE--------EE 2017
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAE-LDALQERREALQ----RLAEYSWDEIDVASAEREiAELEAELERldassddlAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2018 AARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkVLEDQAAQHKQAIEEKIGQLKKSsd 2097
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA------AEDLARLELRALLEERFAAALGD-- 761
|
570 580
....*....|....*....|....*
gi 1207141740 2098 telDRQKKIVEETLKQRKVVEEEIH 2122
Cdd:COG4913 762 ---AVERELRENLEERIDALRARLN 783
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2348-2589 |
1.37e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2348 ADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlk 2427
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2428 lklkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLN-IEAQEAARLRQIAEsdlakQRELAEKMLEEKKQAIQE 2506
Cdd:COG3883 92 --------ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkIADADADLLEELKA-----DKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2507 AAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEE 2586
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
...
gi 1207141740 2587 EAK 2589
Cdd:COG3883 239 AAA 241
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1632-2232 |
1.42e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 58.22 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1632 AKSQQVEeaLLSRT-----RIEEEIHIIRlqlETTMKQKNTAETELLQLRAKAVdADKlrnAAQEEAEKLRKQVAEETQK 1706
Cdd:pfam07111 60 ALSQQAE--LISRQlqelrRLEEEVRLLR---ETSLQQKMRLEAQAMELDALAV-AEK---AGQAEAEGLRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1707 KRKAEEELKR-----KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAA--TQLESKQ 1779
Cdd:pfam07111 131 RKNLEEGSQReleeiQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELlrKQLSKTQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1780 VALTAR--LEESLKN---EQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETWR-QKANEALRLRlqaEEEAN 1847
Cdd:pfam07111 211 EELEAQvtLVESLRKyvgEQVPPEVHSQTWELERQelldtmQHLQEDRADLQATVELLQVRvQSLTHMLALQ---EEELT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1848 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK-QKEAAEMELGNQRKmaeeTAKQKLAAEQELIRLRAdfehaeQQRTVL 1926
Cdd:pfam07111 288 RKIQPSDSLEPEFPKKCRSLLNRWREKVFALMvQLKAQDLEHRDSVK----QLRGQVAELQEQVTSQS------QEQAIL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1927 DDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE---TMSNTEKSKQLLESEAAKMRELAEEATKLRSV 2003
Cdd:pfam07111 358 QRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQlkfVVNAMSSTQIWLETTMTRVEQAVARIPSLSNR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2004 AEEAKKQRQIAEEEAARQRAEAEkILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvlEDQAAQHkq 2083
Cdd:pfam07111 438 LSYAVRKVHTIKGLMARKVALAQ-LRQESCPPPPPAPPVDADLSLELEQLREERNRLDA------------ELQLSAH-- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2084 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEea 2163
Cdd:pfam07111 503 LIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQ-- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2164 ekfRKLALEEEKKRKEAEAKVKQIQAAEEEAAR--------QHKAAQEE--VGRLMKLAEEAKKQ------KEIAEKEAE 2227
Cdd:pfam07111 581 ---EKVAEVETRLREQLSDTKRRLNEARREQAKavvslrqiQHRATQEKerNQELRRLQDEARKEegqrlaRRVQELERD 657
|
....*
gi 1207141740 2228 KQVIL 2232
Cdd:pfam07111 658 KNLML 662
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2472-2607 |
1.45e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.16 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2472 AQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQK 2551
Cdd:TIGR02794 49 AQQANRIQQ-QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2552 SlEAERKRQLEitAEAEKlkvkvTQLSDAQSKAEEEAKKfkKQADEIKIRLQETEK 2607
Cdd:TIGR02794 128 Q-AAEAKAKAE--AEAER-----KAKEEAAKQAEEEAKA--KAAAEAKKKAEEAKK 173
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4226-4262 |
1.62e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.17 E-value: 1.62e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1207141740 4226 IRLLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEM 4262
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1920-2116 |
1.77e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 57.91 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1920 EQQRTVLDDELQRLKNDVNSAVKQKKELEEElikvRKEMEILLQQkskAEKETMSNTEKSKQLLESEAAKMRELAEEATK 1999
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQK----AEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2000 LRSVAEEAKKQ--RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE---NDRLK-RKAEEEGYQRKV 2073
Cdd:PRK00409 578 AIKEAKKEADEiiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkvGDEVKyLSLGQKGEVLSI 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141740 2074 LEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRKV 2116
Cdd:PRK00409 658 PDDKEAIVQAGImkmKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTV 703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1788-2027 |
2.01e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1788 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakREA 1867
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-----------AEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1868 KKRAKAEEAALKQKEA--AEMELGNQRKMAEETAKQKLAAE--QELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQ 1943
Cdd:COG4942 89 EKEIAELRAELEAQKEelAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1944 KKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRA 2023
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1207141740 2024 EAEK 2027
Cdd:COG4942 249 AALK 252
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
349-442 |
2.19e-07 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 53.07 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 349 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-------------------------- 401
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141740 402 -----LENLEQAFSIAE---RDLG-VTRLLDPEDVDVPHPDEKSIITYVS 442
Cdd:cd21224 82 lsselLANEKRNFKLVQqavAELGgVPALLRASDMSNTIPDEKVVILFLS 131
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1224-1758 |
2.32e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1224 KKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVyLDKLKTIDLVIRSTQGAEDILn 1303
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQSQLEII- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1304 kyENQLREVNKVPVNE-KEIEASQTQLqklRSE-AEGKQATFDRLEEELQRATEVNKRMSQLHSERDveleHYRQLVGNL 1381
Cdd:pfam15921 305 --QEQARNQNSMYMRQlSDLESTVSQL---RSElREAKRMYEDKIEELEKQLVLANSELTEARTERD----QFSQESGNL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1382 RERWQAVFAQIELRQRELDLLNRQMQAYRE-------SYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQE------ 1448
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqg 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1449 -KKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAkmESASDDIIQEYVTLRTRYsELMTLS 1527
Cdd:pfam15921 456 kNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNAEITKLRSRV-DLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1528 SQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVD 1607
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1608 SEKQKHNIQR--------ELQELKTLSE--------QEIKA-KSQQVEEALLSRTRIE---EEIHIIRL-------QLET 1660
Cdd:pfam15921 613 KDKKDAKIRElearvsdlELEKVKLVNAgserlravKDIKQeRDQLLNEVKTSRNELNslsEDYEVLKRnfrnkseEMET 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1661 TMK----QKNTAETELLQLR-------------------------AKAVDADKLRNAAQ-----------------EEAE 1694
Cdd:pfam15921 693 TTNklkmQLKSAQSELEQTRntlksmegsdghamkvamgmqkqitAKRGQIDALQSKIQfleeamtnankekhflkEEKN 772
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 1695 KLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1758
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1868-2068 |
2.68e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.71 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1868 KKRAKAEEAALKQKEAAEMElgnqrkmAEETAKQK-LAAEQELIRLRADFEhaeqqrtvlddelqrlkndvnsavKQKKE 1946
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-------AEAIKKEAlLEAKEEIHKLRNEFE------------------------KELRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1947 LEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA-KKQRQIAEEEAARQRAEA 2025
Cdd:PRK12704 80 RRNEL----QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207141740 2026 EKILKEKLTAineatrlKTEAEIALKEKEAENdrlkrKAEEEG 2068
Cdd:PRK12704 156 KEILLEKVEE-------EARHEAAVLIKEIEE-----EAKEEA 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1884-2088 |
3.23e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1884 AEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM----- 1958
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1959 ------------EILLQQKSKAEkeTMSNTEKSKQLLESEAAKMRELAEEATKLrsvaEEAKKQRQIAEEEAARQRAEAE 2026
Cdd:COG3883 94 alyrsggsvsylDVLLGSESFSD--FLDRLSALSKIADADADLLEELKADKAEL----EAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2027 KILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEK 2088
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2441-2654 |
3.26e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2441 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAE--SDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2518
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2519 KQKDQAQVEAqkllEAKKemqqrldQETEGFQKSLEAERKRQleitAEAEklkvkvtqlsdAQSKAEEEAKKFKKQADEI 2598
Cdd:PRK09510 156 AAAAAKKAAA----EAKK-------KAEAEAAKKAAAEAKKK----AEAE-----------AAAKAAAEAKKKAEAEAKK 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2599 KIRLQETEKHTSEKHTVVEKLEVqrlQSKQEADGLHKAIADLEKEKEKLKKEAADL 2654
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1329-2058 |
3.30e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.16 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1329 LQKLRSEAEGKQATFDRLEEELQRATEVNK-------RMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELR------ 1395
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFgyksdetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaada 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1396 -----QRELDLLNRQMQAYR----ESY----DWLIRWIADAKQRQDKLHAVPigGSKGLQEQLTQEKKLLEEiEKNKDKV 1462
Cdd:pfam12128 316 avakdRSELEALEDQHGAFLdadiETAaadqEQLPSWQSELENLEERLKALT--GKHQDVTAKYNRRRSKIK-EQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1463 EDCQKfakgYIDAIKD-YELQLVTYKALVEPIASPLKKaKMESASDDIIQEYVTLRTRYSELMTL--SSQYIKFIIETQR 1539
Cdd:pfam12128 393 AGIKD----KLAKIREaRDRQLAVAEDDLQALESELRE-QLEAGKLEFNEEEYRLKSRLGELKLRlnQATATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1540 RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMkDEVSKRQDvavdseKQKHNIQREL 1619
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAL-DELELQLF------PQAGTLLHFL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1620 QELKTLSEQEIkakSQQVEEALLSRTRIEEEIhiirlqLETTMKQKNTAETelLQLRAKAVDADK---LRNAAQEEAEKL 1696
Cdd:pfam12128 541 RKEAPDWEQSI---GKVISPELLHRTDLDPEV------WDGSVGGELNLYG--VKLDLKRIDVPEwaaSEEELRERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1697 RKQVAEETQKKRKAEEELKRKSEAekdaakekkkaledLEKFKLQAEEAERHLKQAElEKQRQIQVVEEVAKKTAATQLE 1776
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGE--------------LEKASREETFARTALKNAR-LDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1777 SKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeea 1856
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG---------- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1857 ekqkeeakreakkrAKAEEAALKQKEAAEMElgnqRKMAEETAKQKLAAE-QELIRLRADFEHAEQQRTVLDDELQrlkn 1935
Cdd:pfam12128 745 --------------AKAELKALETWYKRDLA----SLGVDPDVIAKLKREiRTLERKIERIAVRRQEVLRYFDWYQ---- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1936 dvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET-MSNTEKSKQLLESEAAKMReLAEEATKLRSVaeeakkQRQIA 2014
Cdd:pfam12128 803 --ETWLQRRPRLATQLSNIERAISELQQQLARLIADTkLRRAKLEMERKASEKQQVR-LSENLRGLRCE------MSKLA 873
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141740 2015 EEEAARQRAEAEKILKEKLTAINEaTRLKTEAEIALKEKEAEND 2058
Cdd:pfam12128 874 TLKEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHF 916
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2437-2599 |
3.51e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 56.76 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2437 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAE 2515
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAiKEAKKEAD 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2516 KLQK------QKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS------------------------LEAERKRQLEITA 2565
Cdd:PRK00409 588 EIIKelrqlqKGGYASVKAHELIEARKRLNKANEKKEKKKKKQkekqeelkvgdevkylslgqkgevLSIPDDKEAIVQA 667
|
170 180 190
....*....|....*....|....*....|....
gi 1207141740 2566 EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2599
Cdd:PRK00409 668 GIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1321-1849 |
3.57e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.67 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1321 EIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELE-HYRQLVGNLRERWQAVFAQIELRQREL 1399
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1400 DLLNRQMQAYRESYDWL-------------IRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQ 1466
Cdd:pfam05557 83 KYLEALNKKLNEKESQLadarevisclkneLSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1467 KFAKGYIDAIKD--YELQLVTYKALVepiaspLKKAKMESAS-DDIIQEYVTLRTRYSELMTLSSQyiKFIIETQ----- 1538
Cdd:pfam05557 163 SSLAEAEQRIKEleFEIQSQEQDSEI------VKNSKSELARiPELEKELERLREHNKHLNENIEN--KLLLKEEvedlk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1539 RRLQDEEKaAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSE-KQKHNIQ 1616
Cdd:pfam05557 235 RKLEREEK-YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1617 RELQE-----LKTLSEQEIKAKSQQVEEALLSRTRI--EEEIHIIRLQL-----ETTMKQKNTAETELLQLRAKAVDADK 1684
Cdd:pfam05557 314 RELEQelaqyLKKIEDLNKKLKRHKALVRRLQRRVLllTKERDGYRAILesydkELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1685 LRNA--------AQEEAE--KLRKQVAEETQKKRKAEEELKRKSeaekDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL 1754
Cdd:pfam05557 394 AHNEemeaqlsvAEEELGgyKQQAQTLERELQALRQQESLADPS----YSKEEVDSLRRKLETLELERQRLREQKNELEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1755 EKQRQIQVVEEVAKKTAATQLESKQvalTARLEESLKNeqvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN- 1833
Cdd:pfam05557 470 ELERRCLQGDYDPKKTKVLHLSMNP---AAEAYQQRKN---QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFk 543
|
570
....*....|....*.
gi 1207141740 1834 EALRLRLQAeEEANKK 1849
Cdd:pfam05557 544 EVLDLRKEL-ESAELK 558
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1799-2055 |
3.65e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.99 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1799 QLQEEAEHLkkqQAEADKAREQAEkELETWRQKANEALRL------RLQAEEEANKKTaaqeeaekqkeeakreakkrAK 1872
Cdd:PRK10929 117 QLLEKSRQA---QQEQDRAREISD-SLSQLPQQQTEARRQlneierRLQTLGTPNTPL--------------------AQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1873 AEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFehAEQQRTVLDDELQRLKNDVNSAVKQK-------- 1944
Cdd:PRK10929 173 AQLTALQAESAALKALVDELELAQLSANNR----QELARLRSEL--AKKRSQQLDAYLQALRNQLNSQRQREaeralest 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1945 ---------------------KELEEELIKVRKEMEILLQQKSKAEKETM------------------SNT--------- 1976
Cdd:PRK10929 247 ellaeqsgdlpksivaqfkinRELSQALNQQAQRMDLIASQQRQAASQTLqvrqalntlreqsqwlgvSNAlgealraqv 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1977 ----EKSK-QLLESEAAKMR-------ELAEEATKLRSVAEE-----AKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 2039
Cdd:PRK10929 327 arlpEMPKpQQLDTEMAQLRvqrlryeDLLNKQPQLRQIRQAdgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILEL 406
|
330 340
....*....|....*....|
gi 1207141740 2040 TRLK---TEAEIALKE-KEA 2055
Cdd:PRK10929 407 TKLKvanSQLEDALKEvNEA 426
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2233-2804 |
4.28e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2233 VQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEkAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAK 2312
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE-ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2313 QAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkqeADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDV 2392
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2393 ELKRL--------------KQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLlEEEAENM 2458
Cdd:pfam15921 399 QNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL-ESTKEML 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2459 KKLAEE--AARLNIEAQEaarlRQIaeSDLAKQRELAEKMLEEKKQAI-----------QEAAKLKAEAEKLQKQkdQAQ 2525
Cdd:pfam15921 478 RKVVEEltAKKMTLESSE----RTV--SDLTASLQEKERAIEATNAEItklrsrvdlklQELQHLKNEGDHLRNV--QTE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2526 VEAQKLLEAKKemqqrlDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQET 2605
Cdd:pfam15921 550 CEALKLQMAEK------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2606 EKHTSEKHtvVEKLEV-----QRLQS----KQEADGLHKAI----ADLEKEKEKLKKEAADLQKQSKEM---ANVQQEQL 2669
Cdd:pfam15921 624 EARVSDLE--LEKVKLvnagsERLRAvkdiKQERDQLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMettTNKLKMQL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2670 QQEKTILQQSffaeKETLLKKekaieeekkklekqfedEVKKAEALKAEQERQRKLMEEerkklQSAMDAAIKKQKEAEE 2749
Cdd:pfam15921 702 KSAQSELEQT----RNTLKSM-----------------EGSDGHAMKVAMGMQKQITAK-----RGQIDALQSKIQFLEE 755
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2750 EMNGKQKEMQDL--EKKRIEQE-KLLAEENKNLREKLQQLQSSQKASYTK--EIEIQTDK 2804
Cdd:pfam15921 756 AMTNANKEKHFLkeEKNKLSQElSTVATEKNKMAGELEVLRSQERRLKEKvaNMEVALDK 815
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1736-2056 |
4.33e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1736 EKFKLQAEEAERhlKQAELEKQRqiqvveevakktaatqLESKQvaltARLEEslkneqvmviqlqEEAEHLKKQQAEAD 1815
Cdd:PRK05035 434 AKAEIRAIEQEK--KKAEEAKAR----------------FEARQ----ARLER-------------EKAAREARHKKAAE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1816 KAREQAEKELetwrQKANEALRLRlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRK-- 1893
Cdd:PRK05035 479 ARAAKDKDAV----AAALARVKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA----DPKKaa 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1894 --MAEETAKQKLAAEQElirlradfEHAEQQRTVlDDELQRLKNDVNSAVKQKKELEEElikvrkemeillqQKSKAEKE 1971
Cdd:PRK05035 550 vaAAIARAKAKKAAQQA--------ANAEAEEEV-DPKKAAVAAAIARAKAKKAAQQAA-------------SAEPEEQV 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1972 TMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKqrqiAEEEAARQRAEAEKILKEKLTAINEAT----RLKTEAE 2047
Cdd:PRK05035 608 AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRK----AAVAAAIARAKARKAAQQQANAEPEEAedpkKAAVAAA 683
|
330
....*....|
gi 1207141740 2048 IA-LKEKEAE 2056
Cdd:PRK05035 684 IArAKAKKAA 693
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1424-1759 |
4.65e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1424 KQRQDKLHavpiggsKGLQEQLTQEKK-LLEEIEKNKdKVEDCQKFAKGYID---AI-KDYELQLVTYKALVEPIASPLK 1498
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDrqaAIyAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1499 KAKMESASDDIIQEYVTlRTRYSELMTLSSQyikfiiETQRRLQDEEKAAEKLKEEERkkmaEMQAELEKQKQLAEThak 1578
Cdd:pfam17380 359 KRELERIRQEEIAMEIS-RMRELERLQMERQ------QKNERVRQELEAARKVKILEE----ERQRKIQQQKVEMEQ--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1579 aIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHniQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEihiirlql 1658
Cdd:pfam17380 425 -IRAEQEEARQREVRRLEEERAREMERVRLEEQER--QQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQ-------- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1659 ettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF 1738
Cdd:pfam17380 493 -----RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340
....*....|....*....|...
gi 1207141740 1739 KLQAEEAERHLKQ--AELEKQRQ 1759
Cdd:pfam17380 567 RLEAMEREREMMRqiVESEKARA 589
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1892-2031 |
4.80e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1892 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR---------KEMEILL 1962
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 1963 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 2031
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1741-1950 |
4.91e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.24 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1741 QAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLEskqvalTARLEESLKneqvmviqlQEEAEHLKKQQAEADKAREQ 1820
Cdd:TIGR02794 76 QAEEAE---KQRAAEQARQKELEQRAAAEKAAKQAE------QAAKQAEEK---------QKQAEEAKAKQAAEAKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1821 AEKEletwRQKANEALRlrlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAK 1900
Cdd:TIGR02794 138 AEAE----RKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1901 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1950
Cdd:TIGR02794 211 AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1602-1824 |
5.22e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1602 QDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvd 1681
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1682 aDKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-----QAELEK 1756
Cdd:COG4942 93 -AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAelaalRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 1757 QRQIQVV---EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKE 1824
Cdd:COG4942 172 ERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1565-2047 |
5.79e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1565 ELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIqRELQELKTLSEQ---------EIKAKSQ 1635
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEyiklsefyeEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1636 QVEEALlsrTRIEEEIHIIRLQL----------ETTMKQKNTAETELLQLRAKAVDADKLRnAAQEEAEKLRKQVAEETQ 1705
Cdd:PRK03918 311 EIEKRL---SRLEEEINGIEERIkeleekeerlEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1706 KKRKAE-EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQA---------ELEKQRQIQVVEEVAKKTAATql 1775
Cdd:PRK03918 387 EKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEYTAELKRI-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1776 eSKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANK-KTAAQE 1854
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1855 EAEKQKEEAKREAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR 1932
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELlkELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1933 LKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQ 2012
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
490 500 510
....*....|....*....|....*....|....*...
gi 1207141740 2013 IAEEEAARQRAEAEKILK--EKLTAINEATR-LKTEAE 2047
Cdd:PRK03918 701 EELEEREKAKKELEKLEKalERVEELREKVKkYKALLK 738
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2185-2327 |
6.00e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2185 KQIQAAEEEAARQHKAAQEEVgrlmklAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKL 2264
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQA------EEAAAKAAAAAKAKAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKK 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2265 KEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEA 2327
Cdd:PRK09510 186 KAEAEAAAKAAAEAKkKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1900-2607 |
6.18e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1900 KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKeTMSNTEKS 1979
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK-NIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1980 KQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE---EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 2056
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKdniEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2057 NDRLKRKAEEegyqrkvLEDQAAQHKQAIE----EKIGQLKKSSDTELDRQKKIVEETlkQRKVVEEEIHILKLNfekas 2132
Cdd:TIGR04523 276 LEQNNKKIKE-------LEKQLNQLKSEISdlnnQKEQDWNKELKSELKNQEKKLEEI--QNQISQNNKIISQLN----- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2133 sgkqelelelkklkgiadetqkskakaeeeaekfrklaleeekkrkeaeakvKQIQAAEEEaarqhkaaqeevgRLMKLA 2212
Cdd:TIGR04523 342 ----------------------------------------------------EQISQLKKE-------------LTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2213 EEAKKQKEIAEKEAEKQVILVQEAAQKcsaaeQKAQNVLVQQNkdsmaqdKLKEEFEKAKKLAQEAEKAKDNAEKEAALL 2292
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYK-----QEIKNLESQIN-------DLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2293 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLaEKTLKQKssvEEE 2372
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE----------SLETQLKVLSRSINKI-KQNLEQK---QKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2373 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDllklklkiekENQELMKKDKDNTKKLLE 2452
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD----------LEDELNKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2453 EEAENMKKLAEEaarlnieaqeaarLRQIAESDLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2529
Cdd:TIGR04523 561 KEIDEKNKEIEE-------------LKQTQKSLKKKQEEKQELIDQkekEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2530 KLLEAKK---EMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2606
Cdd:TIGR04523 628 KLSSIIKnikSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLP 707
|
.
gi 1207141740 2607 K 2607
Cdd:TIGR04523 708 K 708
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1914-2653 |
6.34e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.88 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1914 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKsKAEKETMSNTEKSKQLLESEAAKMREL 1993
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQR-KAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1994 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIAlkEKEAENDRLKrkaeeegYQRKV 2073
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAENARLE-------MHFKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2074 LEDQaaqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAssgkQELELELKKLKGIADETQ 2153
Cdd:pfam05483 218 KEDH---------EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES----RDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2154 KskakaeeeaekfrklalEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEV----GRLMKLAEEAKKQKEIAEKEAEKQ 2229
Cdd:pfam05483 285 K-----------------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiatKTICQLTEEKEAQMEELNKAKAAH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2230 VILVQE-AAQKCSAAEQ-KAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAE 2307
Cdd:pfam05483 348 SFVVTEfEATTCSLEELlRTEQQRLEKNEDQLKI--ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2308 AeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQK 2387
Cdd:pfam05483 426 Q-----------FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2388 SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ----------MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEN 2457
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQeermlkqienLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2458 MKKLAEEAarlnIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKE 2537
Cdd:pfam05483 575 ARSIEYEV----LKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKALKKKGSAE--NKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2538 MQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK-----------KFKKQADEIkIRLQETE 2606
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmeKHKHQYDKI-IEERDSE 726
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2607 -----KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2653
Cdd:pfam05483 727 lglykNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4329-4357 |
6.90e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 6.90e-07
10 20
....*....|....*....|....*....
gi 1207141740 4329 IVDPETGKEMSVYEAYRKGLIDHQTYIEL 4357
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1685-2126 |
7.41e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1685 LRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVE 1764
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1765 EVAKKTAATQLESKQVALTARLEEsLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA--------EKELETWRQKANEAL 1836
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1837 RLRLQAEEEANKKTAAQEEAEKQKEEAkrEAKKRAKAEEAALKQKE------AAEMELGNQRKMAEETAKQKLAAEQELI 1910
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1911 RLRAD-FEHAEQQRTVLDDELQRLkndvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAK 1989
Cdd:COG4717 284 GLLALlFLLLAREKASLGKEAEEL----QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1990 MRELAEEAtkLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEND--RLKRKAEEE 2067
Cdd:COG4717 360 EEELQLEE--LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2068 GYQRKVLEDQAAQHKQAIEEKIGQLKK-SSDTELDRQKKIVEETLKQRKVVEEEIHILKL 2126
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2185-2370 |
1.07e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2185 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmAQDKL 2264
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---AEAKK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2265 KEEFEKAKKLAQEA-EKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALK 2343
Cdd:PRK09510 170 KAEAEAAKKAAAEAkKKAEAEAAAKAAAEAKKKAEAEA------------------KKKAAAEAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*..
gi 1207141740 2344 LKQEADSEMAKYKKLAEKTLKQKSSVE 2370
Cdd:PRK09510 232 AEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1297-1842 |
1.19e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1297 GAEDILNKYENQLREVnKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQL---HSERDVELEH 1373
Cdd:PRK02224 177 GVERVLSDQRGSLDQL-KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVleeHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1374 YRQLVGNLRErwqavfaQIELRQRELDLLNRQMQAYRESYDWLIRWIADA--------------KQRQDKLHAVPIGGSK 1439
Cdd:PRK02224 256 LEAEIEDLRE-------TIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadaeavEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1440 GLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEpiasplkkaKMESASDDIIQEYVTLRTR 1519
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE---------DRREEIEELEEEIEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1520 YSELMTL---SSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQK-----QLAE--THAKAIAKAEQEANE 1589
Cdd:PRK02224 400 FGDAPVDlgnAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEgsPHVETIEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1590 LKTKMKDEVSKRQDVavdseKQKHNIQRELQELKTLSEqEIKAKSQQVEEAL-LSRTRIEEEihiiRLQLETTMKQKNTA 1668
Cdd:PRK02224 480 LEAELEDLEEEVEEV-----EERLERAEDLVEAEDRIE-RLEERREDLEELIaERRETIEEK----RERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1669 ETELLQLRAKAvdadklrNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaAKEKKKALEDLEKFKLQAEE-AER 1747
Cdd:PRK02224 550 EAEAEEKREAA-------AEAEEEAEEAREEVAELNSKLAELKERIES--------LERIRTLLAAIADAEDEIERlREK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1748 HLKQAELEKQRQIQVVEevaKKTAATQLESKQVAltARLEESLKNEQVMVIQLQEEAEHLKKQQAEADK------AREQA 1821
Cdd:PRK02224 615 REALAELNDERRERLAE---KRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeigAVENE 689
|
570 580
....*....|....*....|...
gi 1207141740 1822 EKELETWRQ--KANEALRLRLQA 1842
Cdd:PRK02224 690 LEELEELRErrEALENRVEALEA 712
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1919-2089 |
1.20e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1919 AEQQRTVLDdeLQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLESEAAKMRELAEEAT 1998
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1999 KLrsvAEEAKKQRQIA-----EEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKV 2073
Cdd:COG1579 80 EQ---LGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1207141740 2074 LEDQAAQHKQAIEEKI 2089
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1584-1928 |
1.33e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1584 EQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSeqeikAKSQQVEEALLSRTRIEEEIHIIRLQlETTMK 1663
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERRQKRLQ-EALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1664 QKNTAETellQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE--LKRKSEAEKDAAKEKKKALEDLEKFKLQ 1741
Cdd:pfam02029 86 QKEFDPT---IADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1742 AEEAERHLKQAEL-EKQRQIQVVEEVAKKTAATQLESKQVALTarlEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQ 1820
Cdd:pfam02029 163 SEEAEEVPTENFAkEEVKDEKIKKEKKVKYESKVFLDQKRGHP---EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1821 AEKELETwrQKANEALRLRLQA--EEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEET 1898
Cdd:pfam02029 240 AEVFLEA--EQKLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE----RKLREEE 313
|
330 340 350
....*....|....*....|....*....|
gi 1207141740 1899 AKQKLaaEQELIRLRAdfEHAEQQRTVLDD 1928
Cdd:pfam02029 314 EKRRM--KEEIERRRA--EAAEKRQKLPED 339
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2555-2777 |
1.45e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2555 AERKRQLEitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLH 2634
Cdd:COG4942 19 ADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2635 KAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQ--QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2712
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2713 EALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENK 2777
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
227-326 |
1.47e-06 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 50.35 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 227 DRVQKKTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLKHRQVK 302
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1207141740 303 LVNIRNDDIADGNPKLTLGLIWTI 326
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1942-2089 |
1.57e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.11 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1942 KQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSV---------AEEAKKQRQ 2012
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEAnaerevqrqLEIAERERE 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 2013 IAEEEAARQRAEAEKILKEKLTAinEATRLKTEAEialKEKEAENDRLKRKAEEEGYQRKVlEDQAAQHKQAIEEKI 2089
Cdd:COG2268 292 IELQEKEAEREEAELEADVRKPA--EAEKQAAEAE---AEAEAEAIRAKGLAEAEGKRALA-EAWNKLGDAAILLML 362
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2578-2793 |
1.58e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2578 SDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQ 2657
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2658 SKEmanvQQEQLQQEKTILQQSFFAEKETLL------KKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERK 2731
Cdd:COG4942 99 LEA----QKEELAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2732 KLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKAS 2793
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1901-2096 |
1.64e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1901 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSK 1980
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1981 Q-----------LLESEAAKmrELAEEATKLRSVAEEAKK---QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 2046
Cdd:COG3883 96 YrsggsvsyldvLLGSESFS--DFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2047 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSS 2096
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
816-908 |
1.68e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 816 HAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTA 895
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1207141740 896 ALQTQWSWILQLC 908
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1925-2125 |
1.76e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1925 VLDDelQRLKNDVNSAVKQKKEL---EEELIKVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAA--KMRELA 1994
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDLeraHEALEDAREQIELLepireLAERYAAARERLAELEYLRAALRLWFAqrRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1995 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA----INEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 2070
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2071 ----RKVLEDQAAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 2125
Cdd:COG4913 375 lpasAEEFAALRAEAAALLEA-LEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2454-2596 |
2.10e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.72 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2454 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQkDQAQVEA- 2528
Cdd:COG2268 187 DALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAEleqeREIETARIAEAEAELAKKKAEERREA-ETARAEAe 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2529 QKLLEAKKEMQQRLDQETEgfqkslEAERKRQLEItAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2596
Cdd:COG2268 266 AAYEIAEANAEREVQRQLE------IAEREREIEL-QEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1940-2809 |
2.86e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.90 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1940 AVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlRSVAEEAKKQRQIAEEEAA 2019
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITS-KEAQLESSREIVKSYENEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2020 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE-------------EGYQRKVLEDQaaQHKQAIE 2086
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyHNHQRTVREKE--RELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2087 EKIGQLKKSSdTELDRQKK--IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKA-KAEEEA 2163
Cdd:TIGR00606 326 RELEKLNKER-RLLNQEKTelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTlVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2164 EKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAK-KQKEIAEKEAEKQVILVQEAAQKCSA 2242
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKfVIKELQQLEGSSDRILELDQELRKAE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2243 AEqkaqnvLVQQNKDSMAQDKLKEEF----EKA---KKLAQEAEK-AKDNAEKEA-----ALLHKKAEEAERQKKAAEAE 2309
Cdd:TIGR00606 485 RE------LSKAEKNSLTETLKKEVKslqnEKAdldRKLRKLDQEmEQLNHHTTTrtqmeMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2310 AAKQAKAQEDAEKlRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSv 2389
Cdd:TIGR00606 559 SDELTSLLGYFPN-KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD- 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2390 LDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD------NTKKLLEEEAENMKKLAE 2463
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAElqefisDLQSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2464 EAARLNIEAQEAARLRQIAESDLA-KQRELAEkmLEEKKQAI-QEAAKLKAEAEKLQKQKD--QAQVEAQKLLEAKKEMQ 2539
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDlKEKEIPE--LRNKLQKVnRDIQRLKNDIEEQETLLGtiMPEEESAKVCLTDVTIM 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2540 QRLDQETEGFQKSLEaerkrQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKL 2619
Cdd:TIGR00606 795 ERFQMELKDVERKIA-----QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2620 EVQRLQ-----------------SKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN-------VQQEQLQQEKTI 2675
Cdd:TIGR00606 870 KSEKLQigtnlqrrqqfeeqlveLSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISsketsnkKAQDKVNDIKEK 949
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2676 LQQSFFAEKETllkkEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ----------- 2744
Cdd:TIGR00606 950 VKNIHGYMKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqdnltlrk 1025
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2745 -----KEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEE 2809
Cdd:TIGR00606 1026 renelKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2190-2734 |
3.11e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2190 AEEEAARQHKAAQEEVGRLMKLAEEAkkQKEIAEKEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQ-------- 2261
Cdd:pfam05483 206 AENARLEMHFKLKEDHEKIQHLEEEY--KKEINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQleektklq 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2262 -DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE---KEASRRAEA 2337
Cdd:pfam05483 281 dENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2338 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVK----VQLDE-------------TDKQKSVLDVELKRLKQE 2400
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkeVELEElkkilaedeklldEKKQFEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2401 VSDAIKQKaqvEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQ 2480
Cdd:pfam05483 441 LIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVED-LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2481 IAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2560
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2561 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD--EIKIRLQETEKHTSEK------HTVVEKLEVQRLQSKQEADG 2632
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayEIKVNKLELELASAKQkfeeiiDNYQKEIEDKKISEEKLLEE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2633 LHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2712
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
570 580
....*....|....*....|..
gi 1207141740 2713 EALKAEQERQRKLMEEERKKLQ 2734
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEKLK 773
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1836-2254 |
3.31e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1836 LRLRLQAE-EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE------ETAKQKLAAEQE 1908
Cdd:COG4717 47 LLERLEKEaDELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEaeleelREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1909 LIRLRADFEHAEQQRTVLDDELQRLKN---DVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT--------- 1976
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaeeleelqq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1977 --EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAArQRAEAEKILKEKLTAINEATRLKTEAEIAL---- 2050
Cdd:COG4717 207 rlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2051 ------------KEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDT-----ELDRQKKIVEETLkQ 2113
Cdd:COG4717 286 lallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELEEEL-Q 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2114 RKVVEEEIHILkLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEE 2193
Cdd:COG4717 365 LEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 2194 AARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQ 2254
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELE----ELKAELRELAEEWAALKLALE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2443-2639 |
3.57e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2443 DKDNTKKLLEEEAENMKKL--AEEAARlnIEAQEAARLRQI---------AESDLAKQREL--------AEKMLEEKKQA 2503
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLerAHEALE--DAREQIELLEPIrelaeryaaARERLAELEYLraalrlwfAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2504 I----QEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKvkvTQLSD 2579
Cdd:COG4913 297 LeelrAELARLEAELERLEARLDALR---EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2580 AQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAD 2639
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2473-2750 |
3.70e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.41 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2473 QEAARLRQIAE----SDLAKQR-ELAEKMLEEKKQAiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrlDQETE 2547
Cdd:PRK05035 433 QAKAEIRAIEQekkkAEEAKARfEARQARLEREKAA--REARHKKAAEARAAKDKDAVAAALARVKAKK------AAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2548 GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA----DEIKIRLQETEKHTSEKHTVVEKLEVQR 2623
Cdd:PRK05035 505 PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiarAKAKKAAQQAANAEAEEEVDPKKAAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2624 LQSKQEAdglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQ---QEQLQQEKTILQQSFFAEKETLlkkekaieeekkk 2700
Cdd:PRK05035 585 AIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARakaKKAEQQANAEPEEPVDPRKAAV------------- 648
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2701 lekqfEDEVKKAEALKAEQER--QRKLMEEERKKLQSAMDAAIKKQKEAEEE 2750
Cdd:PRK05035 649 -----AAAIARAKARKAAQQQanAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1577-1817 |
4.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1577 AKAIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEallsrtrIEEEIHIIRL 1656
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1657 QLETTMKQKNTAETELLQLR---AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALE 1733
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1734 DLEKfKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQEEAEHLKKQQAE 1813
Cdd:COG4942 164 ALRA-ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAA 238
|
....
gi 1207141740 1814 ADKA 1817
Cdd:COG4942 239 AAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2319-2792 |
4.20e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2319 DAEKLRKEAEKEASRRAEAEAAALKLK---------QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqlDETDKQKSV 2389
Cdd:pfam12128 235 GIMKIRPEFTKLQQEFNTLESAELRLShlhfgyksdETLIASRQEERQETSAELNQLLRTLDDQWKEKR--DELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2390 LDVELKRLKQEVSDAIKQKAQVEDE-LSKVKIQMEDLLKLKLKIEKENQELmkkdkdntkKLLEEEAENMKKlAEEAARL 2468
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---------KALTGKHQDVTA-KYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2469 NIEAQEAARLRQIaESDLAKQRELAEKMLEEKKQAIQeaaKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET- 2546
Cdd:pfam12128 383 KIKEQNNRDIAGI-KDKLAKIREARDRQLAVAEDDLQ---ALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2547 --------EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEK-HTVVE 2617
Cdd:pfam12128 459 tpelllqlENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQaGTLLH 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2618 KLevqRLQSKQEADGLHKAIAdlekekeKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQ----SFFAEKETLlkkeka 2693
Cdd:pfam12128 539 FL---RKEAPDWEQSIGKVIS-------PELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEEL------ 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2694 ieeekKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLA 2773
Cdd:pfam12128 603 -----RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK---NKALA 674
|
490
....*....|....*....
gi 1207141740 2774 EENKNLREKLQQLQSSQKA 2792
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQ 693
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2384-2599 |
4.52e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2384 DKQKSVLDVELKRLKQEvsdaikqkAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE--AENMKKL 2461
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE--------QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2462 AEEAARLNIEAQeaarlrQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQr 2541
Cdd:PRK09510 141 AAAAAKAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA- 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2542 ldqetegfqkslEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2599
Cdd:PRK09510 214 ------------EAKKK------AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1632-1881 |
4.75e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1632 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1711
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1712 EELK-RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE----LEKQRQIQVVEEVAKKTAATQLESKQVALTARL 1786
Cdd:COG4942 97 AELEaQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkyLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1787 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKRE 1866
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA-----------------AAA 239
|
250
....*....|....*
gi 1207141740 1867 AKKRAKAEEAALKQK 1881
Cdd:COG4942 240 AERTPAAGFAALKGK 254
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1686-1901 |
4.80e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1686 RNAAQEEAEKLRKQVAE----ETQKKRKAEEELKRkseAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQaELEKQRQIQ 1761
Cdd:pfam15709 328 REQEKASRDRLRAERAEmrrlEVERKRREQEEQRR---LQQEQLERAEKMREELELEQQRRFEEIRLRKQ-RLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1762 VVEEvakKTAATQLESKQVALTARLEESLKNEQvmviQLQEeaehlKKQQAEADKAREQAEKELETWRQKANEALRLRLQ 1841
Cdd:pfam15709 404 EEEE---RKQRLQLQAAQERARQQQEEFRRKLQ----ELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1842 AEEEankktaaqeEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQ 1901
Cdd:pfam15709 472 AEEE---------RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1799-2088 |
5.03e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1799 QLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLR-----LQ---AEEEANKKTAAQEEAEKQKEEAKREAKKR 1870
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREELAEEVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1871 AKAEEAAL----------------KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLK 1934
Cdd:PRK02224 297 DLLAEAGLddadaeavearreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1935 NDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnteksKQLLESEAAKMRE-LAEEATKLRSVAEEAKKQRQI 2013
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF--------LEELREERDELRErEAELEATLRTARERVEEAEAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2014 AEE-----------------EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEnDRLKRKAEeegyQRKVLED 2076
Cdd:PRK02224 449 LEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE----RREDLEE 523
|
330
....*....|..
gi 1207141740 2077 QAAQHKQAIEEK 2088
Cdd:PRK02224 524 LIAERRETIEEK 535
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1588-2135 |
5.05e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1588 NELKTKmKDEVSKRQDVAVDSEKQKHNIQRELQELKTlSEQEIKAKSQQVEEALlsrTRIEEEIHIIRLQLETTMKQKNT 1667
Cdd:TIGR04523 47 NELKNK-EKELKNLDKNLNKDEEKINNSNNKIKILEQ-QIKDLNDKLKKNKDKI---NKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1668 AETELLQLRAKAvdadklrnaaqEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1747
Cdd:TIGR04523 122 LEVELNKLEKQK-----------KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1748 HLKQAELEKQRQIQVVEEvakktaatqLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAeKELET 1827
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKK---------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL-NQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1828 WRQKANEALRLRLQAEEEANKKTAAQEEAEkqkeeakreakKRAKAEEAALKQKEAAEMelgnQRKMAEETAKQklaaEQ 1907
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQL-----------NQLKSEISDLNNQKEQDW----NKELKSELKNQ----EK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1908 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKaEKETMSNTEKSKQLLESea 1987
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-YKQEIKNLESQINDLES-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1988 aKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEkltaINEATRLKTEAEIALKEKEAENDRLKRKAEEE 2067
Cdd:TIGR04523 399 -KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2068 GYQRKVLEDQAAQHKQAIEEKIGQLKKssdteLDRQKKIVEETLkqrKVVEEEIHILKLNFEKASSGK 2135
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKK-----LNEEKKELEEKV---KDLTKKISSLKEKIEKLESEK 533
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1499-2075 |
5.09e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.82 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1499 KAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELE----KQKQLAE 1574
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1575 THAKAIAK--AEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEqEIKAKSQQVEEALLS-----RTRI 1647
Cdd:pfam05557 88 LNKKLNEKesQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNlekqqSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1648 EEEIHIIRLQLETTMKQKNTAETELLQLR-AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAeEELKRKSEAEKDAAK 1726
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIENKLLLKEEV-EDLKRKLEREEKYRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1727 EKKKALEDLEKFKLQAEEAERhlkqaeLEKQRQIQVVEEVAKKTAATQLESKQVALTAR---LEESLKNEQVMVIQLQEE 1803
Cdd:pfam05557 246 EAATLELEKEKLEQELQSWVK------LAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEnssLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1804 AEHLKKQQAEADKAREQAEKELETWRQKANEALRLR--LQAEEEANKKTAAQEEAEKQKEEAKREAKK---RAKAEEAAL 1878
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgYRAILESYDKELTMSNYSPQLLERIEEAEDmtqKMQAHNEEM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1879 K-QKEAAEMELGNQRKMAEetakqklAAEQELIRLRADFEHAEQQRTvlddelqrlKNDVNSAVKQKKELEEELIKVRKE 1957
Cdd:pfam05557 400 EaQLSVAEEELGGYKQQAQ-------TLERELQALRQQESLADPSYS---------KEEVDSLRRKLETLELERQRLREQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1958 MEILLQQKSKAEKETMSNTEKSK--QLLESEAAKMRE-LAEEATKLRsvaeeakkqrqiAEEEAARQRAEAEKILKEKLT 2034
Cdd:pfam05557 464 KNELEMELERRCLQGDYDPKKTKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVL 531
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1207141740 2035 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLE 2075
Cdd:pfam05557 532 RLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2370-2799 |
5.11e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2370 EEELVKVKVQLDETDKQKSvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKK 2449
Cdd:PRK02224 212 ESELAELDEEIERYEEQRE----QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2450 LLEEEAENMKKLAE-EAARLNIEAQEAARlrqiaeSDLAKQRELAEKMLEEKKQAIQEAAKlkaEAEKLQKQKDQAQVEA 2528
Cdd:PRK02224 288 LEELEEERDDLLAEaGLDDADAEAVEARR------EELEDRDEELRDRLEECRVAAQAHNE---EAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2529 QKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKH 2608
Cdd:PRK02224 359 EELREEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2609 TSEKHTVVEklEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAdLQKQSKEMANVQQEQLQQEKTILQQSFFAEketll 2688
Cdd:PRK02224 435 LRTARERVE--EAEALLEAGKCPECGQPVEGSPHVETIEEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVE----- 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2689 kkekaieeekkkLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQ 2768
Cdd:PRK02224 507 ------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
410 420 430
....*....|....*....|....*....|....*
gi 1207141740 2769 EKLLAE--ENKNLREKLQQLQSSQK--ASYTKEIE 2799
Cdd:PRK02224 575 AELNSKlaELKERIESLERIRTLLAaiADAEDEIE 609
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2452-2588 |
5.24e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 52.70 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2452 EEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA------------KLKAEAEKLQK 2519
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtsspkedkqvaeNQKREIEKAQI 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 2520 QKDQAQVEAQKLLEAKKE--MQQRLDQETEGFQKSLEAERKRqLEITAEAEKLKVKVtqlsDAQSKAEEEA 2588
Cdd:pfam05262 289 EIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQV----EAQPTSLNED 354
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1865-2300 |
5.42e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1865 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1944
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1945 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 2024
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2025 AEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 2104
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2105 KIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKV 2184
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2185 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2264
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1207141740 2265 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAE 2300
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAAL 517
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1751-1971 |
5.62e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1751 QAELEKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvmviQLQEEaehlKKQQAEADKAREQAEKELETWRQ 1830
Cdd:PRK09510 74 AKRAEEQRKKKE------QQQAEELQQKQAAEQERLKQLEKERL----AAQEQ----KKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1831 KANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEli 1910
Cdd:PRK09510 140 KAAAAAKAKAEAEAKR-----------------AAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK-- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 1911 rlradfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1971
Cdd:PRK09510 201 ------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
334-442 |
5.69e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 48.26 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 334 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIA 412
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|
gi 1207141740 413 ERDLGVTRLLDPEDVDVPHPDEKSIITYVS 442
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLS 107
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1298-1958 |
6.19e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.13 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1298 AEDILNKYENQLREVNKVPVNEKEI-EASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQ 1376
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1377 L------------VGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYD----------WLIRWIADAKQRQDKLHAVP 1434
Cdd:TIGR00606 504 KslqnekadldrkLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiksrhsdeltSLLGYFPNKKQLEDWLHSKS 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1435 iGGSKGLQEQLTQEKKLLEEIEKNKD--------KVEDCQKFAKGYIDAIKDYELQlVTYKALVEPIASPLKKAKMESAS 1506
Cdd:TIGR00606 584 -KEINQTRDRLAKLNKELASLEQNKNhinnelesKEEQLSSYEDKLFDVCGSQDEE-SDLERLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1507 DDIIQEYVTLRTRYSE----LMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAK 1582
Cdd:TIGR00606 662 TAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1583 AEQEANELKTKMkdevskrQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTM 1662
Cdd:TIGR00606 742 KEKEIPELRNKL-------QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1663 KQKNTAETELLQLRAKAVDAD-KLRNAAQ--EEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1739
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQhELDTVVSkiELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1740 LQAEEAERHLKQaeleKQRQIQVVEEVAKKtaatqLESKQVALTARLEESLKNEQVMVIQLQEEAEHL--------KKQQ 1811
Cdd:TIGR00606 895 TEVQSLIREIKD----AKEQDSPLETFLEK-----DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdieNKIQ 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1812 AEADKAREQAEKELETWRQKANEALRLRLQAEEEankktaaqeeaekqkEEAKREAKKRAKAEEAALkQKEAAEMELGNQ 1891
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLEECEKHQEKINED---------------MRLMRQDIDTQKIQERWL-QDNLTLRKRENE 1029
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 1892 RKMAEETAKQKLAAEQELIRLRADFEHAEqqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1958
Cdd:TIGR00606 1030 LKEVEEELKQHLKEMGQMQVLQMKQEHQK-----LEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2437-2804 |
6.92e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2437 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES--DLAKQRELAEKMLEEKKQAIQ------EAA 2508
Cdd:COG4717 56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQllplyqELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2509 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2588
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2589 KKFKKQADEIKIRLQETEKhTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA--------------DL 2654
Cdd:COG4717 216 EEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallfllLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2655 QKQSKEMANVQQEQLQQEKTILQQsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-----EALKAEQERQRKLMEEE 2729
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEE---EELEELLAALGLPPDLSPEELLELLDRIEELqellrEAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2730 RKKLQSAMDA-----------AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENknLREKLQQLQSSQKASYTKEI 2798
Cdd:COG4717 372 IAALLAEAGVedeeelraaleQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELE 449
|
....*.
gi 1207141740 2799 EIQTDK 2804
Cdd:COG4717 450 ELREEL 455
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
225-333 |
7.27e-06 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 48.06 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 225 ERDRVQKKTFTKWVNKhlVKAQRHITDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 295
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141740 296 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1587-2047 |
7.63e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1587 ANELKTKMKDEVSKRQDVA-----VDSEKQKHN-IQRELQELK---TLSEQEIKAKS---QQVEEALLSRTRIE---EEI 1651
Cdd:PRK04863 278 ANERRVHLEEALELRRELYtsrrqLAAEQYRLVeMARELAELNeaeSDLEQDYQAASdhlNLVQTALRQQEKIEryqADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1652 HIIRLQLETTMKQKNTAETELLQLRAKAvdadklrNAAQEEAEKLRKQVAEETQkkrkAEEELKRKSeaekdaakekkka 1731
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARA-------EAAEEEVDELKSQLADYQQ----ALDVQQTRA------------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1732 ledlekfkLQAEEAerhlKQAeLEKQRQIQVVEEVAKKTAATQLEskqvALTARLEEslkneqvmviqLQEEAEHLKKQQ 1811
Cdd:PRK04863 414 --------IQYQQA----VQA-LERAKQLCGLPDLTADNAEDWLE----EFQAKEQE-----------ATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1812 AEADKAREQAEKELETWRQKANEALRLrlQAEEEAnkktaaqeeaekqkeeakREAKKRAKAEEAALKQKEAAEMELGnq 1891
Cdd:PRK04863 466 SVAQAAHSQFEQAYQLVRKIAGEVSRS--EAWDVA------------------RELLRRLREQRHLAEQLQQLRMRLS-- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1892 rkmaeeTAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEillQQKSKAEKE 1971
Cdd:PRK04863 524 ------ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALR---QQLEQLQAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1972 TMSNTEKSKQLLESEAA--KMRELAEEATK--------LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR 2041
Cdd:PRK04863 595 IQRLAARAPAWLAAQDAlaRLREQSGEEFEdsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPR 674
|
....*.
gi 1207141740 2042 LKTEAE 2047
Cdd:PRK04863 675 LNALAE 680
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1782-2120 |
7.68e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1782 LTARLEESLKnEQVMVIQLQEEAehlkKQQAEADKAREQAEKEleTWRQKANEaLRLRLQAEEEANKKTaaqeeaekqke 1861
Cdd:pfam07888 32 LQNRLEECLQ-ERAELLQAQEAA----NRQREKEKERYKRDRE--QWERQRRE-LESRVAELKEELRQS----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1862 eakreakkRAKAEEAALKQKEAAEMelgnQRKMAEETA---KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1938
Cdd:pfam07888 93 --------REKHEELEEKYKELSAS----SEELSEEKDallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1939 SAVKQKKELEEElikvRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAkkQRQIAEEEA 2018
Cdd:pfam07888 161 KAGAQRKEEEAE----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA--HRKEAENEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2019 ARQRAEAekiLKEKLTAINEATR-LKTEaeiaLKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ------ 2091
Cdd:pfam07888 235 LLEELRS---LQERLNASERKVEgLGEE----LSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARwaqere 307
|
330 340 350
....*....|....*....|....*....|
gi 1207141740 2092 -LKKSSDTELDRQKKIVEETLKQRKVVEEE 2120
Cdd:pfam07888 308 tLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1764-2021 |
7.88e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.26 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1764 EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAE 1843
Cdd:pfam15709 317 EEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1844 EEankktaaqeeaekqkeeakreakKRAKAEEAALKQKEaaemelgnQRKMAEETAKQKlaaEQELIRLRADFEHAEQQr 1923
Cdd:pfam15709 397 EE-----------------------ERQRQEEEERKQRL--------QLQAAQERARQQ---QEEFRRKLQELQRKKQQ- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1924 tvldDELQRLKndvnsAVKQK-KELEEELIKVRK------EMEILLQQKSKAEKEtmsntEKSKQllesEAAKMRELAEE 1996
Cdd:pfam15709 442 ----EEAERAE-----AEKQRqKELEMQLAEEQKrlmemaEEERLEYQRQKQEAE-----EKARL----EAEERRQKEEE 503
|
250 260
....*....|....*....|....*
gi 1207141740 1997 ATKLrsVAEEAKKQRQiaeeEAARQ 2021
Cdd:pfam15709 504 AARL--ALEEAMKQAQ----EQARQ 522
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1299-2105 |
7.91e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1299 EDILNKYENQLREVNKVPVN-EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkRMSQLHSERDVELEHYRQL 1377
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKlEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLEEETAQKNNALKKIREL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1378 VGNLRE------RWQAVFAQIELRQREldlLNRQMQAYR-ESYDWLirwiaDAKQRQDKLHavpiggSKGLQEqLTQEKK 1450
Cdd:pfam01576 270 EAQISElqedleSERAARNKAEKQRRD---LGEELEALKtELEDTL-----DTTAAQQELR------SKREQE-VTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1451 LLEEIEKNKD-KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQ 1529
Cdd:pfam01576 335 ALEEETRSHEaQLQEMRQKHTQALEELTEQLEQAKRNKANLEK-----AKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1530 YIKFIIETQRRLQDEEKAaeklKEEERKKMAEMQAELEK---------------QKQLA---------------ETHAK- 1578
Cdd:pfam01576 410 LEGQLQELQARLSESERQ----RAELAEKLSKLQSELESvssllneaegkniklSKDVSslesqlqdtqellqeETRQKl 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1579 ----AIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELKTLSEQEikakSQQVEEALLSRTRIEEEIHII 1654
Cdd:pfam01576 486 nlstRLRQLEDERNSLQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEED----AGTLEALEEGKKRLQRELEAL 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1655 RLQLETTM-------KQKNTAETELLQLrakAVDADKLR---NAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDA 1724
Cdd:pfam01576 558 TQQLEEKAaaydkleKTKNRLQQELDDL---LVDLDHQRqlvSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1725 AKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKtaATQLESKQVALTARLEEslkneqvMVIQLQEEA 1804
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKN--VHELERSKRALEQQVEE-------MKTQLEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1805 EHLkkqqaeadKAREQAEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakrEAKKRakaeeAALKQKEAA 1884
Cdd:pfam01576 706 DEL--------QATEDAKLRLEVNMQALKAQFERDLQARDEQG------------------EEKRR-----QLVKQVREL 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1885 EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlDDELQRLKNdvnsAVKQKKELEEELIKVRKEM-EILLQ 1963
Cdd:pfam01576 755 EAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGR---EEAVKQLKK----LQAQMKDLQRELEEARASRdEILAQ 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1964 QKskaeketmsNTEKSKQLLESEAAKMRELAeeatklrSVAEEAKKQRQIAEEEAARQRAEAekiLKEKLTAINEATRLk 2043
Cdd:pfam01576 828 SK---------ESEKKLKNLEAELLQLQEDL-------AASERARRQAQQERDELADEIASG---ASGKSALQDEKRRL- 887
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2044 tEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKK 2105
Cdd:pfam01576 888 -EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNK 948
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2438-2612 |
8.01e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.26 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2438 ELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEA--E 2515
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2516 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQEtegfqksLEAERKRQLEItAEAEKLKVKvTQLSDAQSKAEEEAKKFKKQA 2595
Cdd:pfam15709 431 KLQELQRKKQQEEAERAEAEKQRQKELEMQ-------LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEERRQKE 501
|
170
....*....|....*...
gi 1207141740 2596 DE-IKIRLQETEKHTSEK 2612
Cdd:pfam15709 502 EEaARLALEEAMKQAQEQ 519
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2352-2560 |
8.04e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.38 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2352 MAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAikQKAQVEDELSKVKIQMEdllklklk 2431
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE--KAAKQAEQAAKQAEEKQ-------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2432 iekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARL-----NIEAQEAARLRQ-----IAESDLAKQRELAEKMLEEKK 2501
Cdd:TIGR02794 119 ----KQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQaeeeaKAKAAAEAKKKAeeakkKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2502 QAIQEAAKLKAEAEKlqKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2560
Cdd:TIGR02794 195 KAKAEAAKAKAAAEA--AAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2655-2821 |
8.22e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2655 QKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2734
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2735 SAMDaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKnlREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT 2814
Cdd:pfam15709 434 ELQR---KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE--EERLEYQRQKQEAEEKARLEAEERRQKEEEAARLA 508
|
....*..
gi 1207141740 2815 MVETTKK 2821
Cdd:pfam15709 509 LEEAMKQ 515
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1958-2290 |
8.29e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1958 MEILLQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklrsVAEEAKKQRQIAEEEAARQRAeaekiLKEKLTAIN 2037
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQ------ERLRQEKEE------KAREVERRRKLEEAEKARQAE-----MDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2038 EATRLKTEAE-----IALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQlkkssDTELDRQKKIVEETlK 2112
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ-----ELEAARKVKILEEE-R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2113 QRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLalEEEKKRKEAEAKVKQIQAAEE 2192
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ--EEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2193 EAARQHKAAQEEVGRLMKLAEEAKKQKeIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEFEKA 2271
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRK-LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQmRKATEERSRL 568
|
330
....*....|....*....
gi 1207141740 2272 KKLAQEAEKAKDNAEKEAA 2290
Cdd:pfam17380 569 EAMEREREMMRQIVESEKA 587
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2321-2593 |
8.73e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2321 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKV---KVQLDETDKQKSVLDVELKRL 2397
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2398 KQEVSDAIKQKAQVeDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAAR 2477
Cdd:COG1340 98 RKELAELNKAGGSI-DKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2478 LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAER 2557
Cdd:COG1340 175 EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELKKLR 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207141740 2558 KRQLEITAEAEKlkvkvtqlSDAQSKAEEEAKKFKK 2593
Cdd:COG1340 251 KKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
230-337 |
8.98e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 48.50 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 230 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 296
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141740 297 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 337
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1736-2038 |
9.35e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.46 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1736 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLK-NEQVMVIQLQEEAEHLKKQQAEA 1814
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1815 DKaREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1894
Cdd:pfam13868 123 EK-QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1895 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMS 1974
Cdd:pfam13868 202 ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 1975 NTEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINE 2038
Cdd:pfam13868 280 EAEKRRMKRLEHRRELEKQIEEREEQR--AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1568-1959 |
1.06e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1568 KQKQLAEThAKAIAKAEQEANELKTKMKDevsKRQDVavdSEKQKHniqreLQELKTLSEQEIKAKSQQVEEALL----- 1642
Cdd:PRK10246 438 QQKRLAQL-QVAIQNVTQEQTQRNAALNE---MRQRY---KEKTQQ-----LADVKTICEQEARIKDLEAQRAQLqagqp 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1643 -------SRTRIEE----EIHIIRLQLETTMKQKNTAETELLQLRAKaVDAdklrnaaqeeaekLRKQV---AEETQKKR 1708
Cdd:PRK10246 506 cplcgstSHPAVEAyqalEPGVNQSRLDALEKEVKKLGEEGAALRGQ-LDA-------------LTKQLqrdESEAQSLR 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1709 KAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT-QLESKQVALTARLE 1787
Cdd:PRK10246 572 QEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1788 E-SLK-----NEQVMVIQLQEEAEHLKKQQAEADKAREQ---------------------AEKELETWRQKANEALRLR- 1839
Cdd:PRK10246 652 GyALTlpqedEEASWLATRQQEAQSWQQRQNELTALQNRiqqltplletlpqsddlphseETVALDNWRQVHEQCLSLHs 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1840 ---------LQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE---ETAKQKLAAEQ 1907
Cdd:PRK10246 732 qlqtlqqqdVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQtlvTQTAQALAQHQ 811
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 1908 ----ELIRLRADFEHAEQQRTVLDDEL-----------QRLKNDVNSAvKQKKELEEELIKVRKEME 1959
Cdd:PRK10246 812 qhrpDGLDLTVTVEQIQQELAQLAQQLrenttrqgeirQQLKQDADNR-QQQQALMQQIAQATQQVE 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2360-2764 |
1.06e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2360 EKTLKQKSSVEEELVKVKVQLDETDKQK-----SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEK 2434
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2435 ENQELMKKDKDNTKKLLEEEAEN------MKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA 2508
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2509 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2588
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV----LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2589 KKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQE--ADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQ 2666
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2667 EQLQQEKTILQQsfFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKE 2746
Cdd:TIGR04523 593 QKEKEKKDLIKE--IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
410
....*....|....*...
gi 1207141740 2747 AEEEMNGKQKEMQDLEKK 2764
Cdd:TIGR04523 671 SKTKIDDIIELMKDWLKE 688
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1904-2103 |
1.12e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1904 AAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLL 1983
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQA----EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1984 ESEA--AKMRELAEEATKLRSVAEEAKKQRQI-----AEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAE 2056
Cdd:TIGR02794 123 EAKAkqAAEAKAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141740 2057 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQ 2103
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1580-1846 |
1.15e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1580 IAKAEQEaNELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQElktlsEQEIKAKsQQVEEALLSRTRIEEEIhiirlqle 1659
Cdd:pfam15709 325 LEKREQE-KASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ-----EQLERAE-KMREELELEQQRRFEEI-------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1660 ttmkqkntaetellQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtqKKRKAEEELKRKSEAEKDaakekkkaledlekfK 1739
Cdd:pfam15709 390 --------------RLRKQRLEEERQRQEEEERKQRLQLQAAQE--RARQQQEEFRRKLQELQR---------------K 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1740 LQAEEAERhlkqAELEKQRQiqvveevakktaatqleskqvaltARLEESLKNEQVMVIQLQEEA--EHLKKQQAEADKA 1817
Cdd:pfam15709 439 KQQEEAER----AEAEKQRQ------------------------KELEMQLAEEQKRLMEMAEEErlEYQRQKQEAEEKA 490
|
250 260 270
....*....|....*....|....*....|....
gi 1207141740 1818 REQAEKEletwRQKANEALRLRL-----QAEEEA 1846
Cdd:pfam15709 491 RLEAEER----RQKEEEAARLALeeamkQAQEQA 520
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1320-2009 |
1.36e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1320 KEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE-VNKRMSQL-HSERdveLEHYRQLVGNLRERWQAVFAQIELRQR 1397
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhLNLVQTALrQQEK---IERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1398 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQeQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1477
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1478 DYELQLVTY------------KA--LVEPIASPLKKAKMESASDDIIQEY----------VTLRTRYSELMTLSSQYikf 1533
Cdd:COG3096 455 EEVLELEQKlsvadaarrqfeKAyeLVCKIAGEVERSQAWQTARELLRRYrsqqalaqrlQQLRAQLAELEQRLRQQ--- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1534 iiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQK-QLAETHAKAIAKA---EQEANELKTKMKdEVSKRQDVAVDSE 1609
Cdd:COG3096 532 --QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLeELEEQAAEAVEQRselRQQLEQLRARIK-ELAARAPAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1610 KQKHNIQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTA----ETELLQLR--------A 1677
Cdd:COG3096 609 DALERLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPggaeDPRLLALAerlggvllS 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1678 KAVDADKLRNAAQEEA--------------EKLRKQVAE-------------------------ETQKKR---KAEEELK 1715
Cdd:COG3096 688 EIYDDVTLEDAPYFSAlygparhaivvpdlSAVKEQLAGledcpedlyliegdpdsfddsvfdaEELEDAvvvKLSDRQW 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1716 RKSEAEKDAAKEKKKALEDLEKFKLQAEE-AERHLKQA-ELEK-QR-----------QIQVVEEVAKKTAATQLESKQVA 1781
Cdd:COG3096 768 RYSRFPEVPLFGRAAREKRLEELRAERDElAEQYAKASfDVQKlQRlhqafsqfvggHLAVAFAPDPEAELAALRQRRSE 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1782 LTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA------NKKTAAQEE 1855
Cdd:COG3096 848 LERELAQHRAQEQ----QLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLE 923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1856 AEK-------QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRK-MAEETAKQKLAAEQELI-RLRADFEHAEQQRTVL 1926
Cdd:COG3096 924 PLVavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAEEARREA 1003
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1927 DDELQRLKNDVNSA------------VKQK--KELEEEL----IKVRKEMEIL-------LQQKSKAEKETMSNTEKSKQ 1981
Cdd:COG3096 1004 REQLRQAQAQYSQYnqvlaslkssrdAKQQtlQELEQELeelgVQADAEAEERarirrdeLHEELSQNRSRRSQLEKQLT 1083
|
810 820 830
....*....|....*....|....*....|..
gi 1207141740 1982 LLESEAA----KMRELAEEATKLRSVAEEAKK 2009
Cdd:COG3096 1084 RCEAEMDslqkRLRKAERDYKQEREQVVQAKA 1115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2345-2540 |
1.39e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2345 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMED 2424
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2425 LLKLKLKIEK-----------ENQELMKKDKDNTKKLLEE------EAENMK-KLAEEAARLNIEAQEAARLRQIAESDL 2486
Cdd:COG3883 98 SGGSVSYLDVllgsesfsdflDRLSALSKIADADADLLEElkadkaELEAKKaELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2487 AKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQ 2540
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1609-2088 |
1.41e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1609 EKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNA 1688
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1689 AQ--EEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfklQAEEAERHLKQAELEKQRQIqvveev 1766
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEELEERLEELR----------------------ELEEELEELEAELAELQEEL------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1767 akktaATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEK-ELETWRQKANEALR-------- 1837
Cdd:COG4717 180 -----EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKearlllli 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1838 ----------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1907
Cdd:COG4717 255 aaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1908 ELIRLRADFEHAEQQRTvLDDELQRLKNDVNSAVkQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQL---LE 1984
Cdd:COG4717 335 SPEELLELLDRIEELQE-LLREAEELEEELQLEE-LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELeeqLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1985 SEAAKMRELAEEATKlrsvaEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKA 2064
Cdd:COG4717 413 ELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
490 500
....*....|....*....|....*
gi 1207141740 2065 EEEGYQRKVLEDQA-AQHKQAIEEK 2088
Cdd:COG4717 488 LAEEWAALKLALELlEEAREEYREE 512
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1805-2091 |
1.43e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 51.13 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1805 EHLKKQQAEadKAREQAEKELetwrqKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAAL-KQKEA 1883
Cdd:PRK07735 8 EDLKKEAAR--RAKEEARKRL-----VAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALaKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1884 A-----EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1958
Cdd:PRK07735 81 GteevtEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1959 EILLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKKqrqiaeeeAARQRAEAEKILKEKLTAIN- 2037
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQ----KAAEAGEGTEEVTEEEKAKAKAKA--------AAAAKAKAAALAKQKASQGNg 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141740 2038 --EATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA-------QHKQAIEEKIGQ 2091
Cdd:PRK07735 229 dsGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEEPSvnqpylnKYVEVIKEKLGE 291
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1740-2607 |
1.46e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1740 LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvALTARlEESLKNEQVMVIQLQEEAEHLKKQQAEADKARE 1819
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRD-QITSK-EAQLESSREIVKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1820 ---QAEKELETWRQKANEALRLRLQAEEEAnKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEaaeMELGNQRKMAE 1896
Cdd:TIGR00606 263 kimKLDNEIKALKSRKKQMEKDNSELELKM-EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1897 ETAKQKLAAEQELIRLRADFEH-------AEQQRTVLDDELQRLKND------VNSAVKQKKELEEELIKVRKEMEILLQ 1963
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQehirardSLIQSLATRLELDGFERGpfserqIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1964 QKSKAEKETMSNTE-KSKQLLESEAAKMRELAEEATKLRSVAEEAKK----QRQIAEEEAARQRAEAEKILKEKltaiNE 2038
Cdd:TIGR00606 419 SKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQELRKAERELSKAEK----NS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2039 ATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ-------RKVLEdQAAQHKQAIEEKIGQLKKSSDTELDRQ------KK 2105
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhtttRTQME-MLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnKK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2106 IVEETL----KQRKVVEEEIHILKLNFEKASSGKQELELelkklkgiaDETQKSKAKAEEEAEKFRklaleeekkrkeae 2181
Cdd:TIGR00606 574 QLEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINN---------ELESKEEQLSSYEDKLFD-------------- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2182 akvkqiqaaeeeaARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSA----------AEQKAQNVL 2251
Cdd:TIGR00606 631 -------------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAELQEFI 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2252 VQ-QNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEke 2330
Cdd:TIGR00606 698 SDlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2331 asrraeAEAAALKLKQEADSEMAKYKKLAEKTlkqkSSVEEELVKVKVQLDETDKQKSVLDV-ELKRLKQEVSDAIKQKA 2409
Cdd:TIGR00606 776 ------TIMPEEESAKVCLTDVTIMERFQMEL----KDVERKIAQQAAKLQGSDLDRTVQQVnQEKQEKQHELDTVVSKI 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2410 QVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQ 2489
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2490 RELAEKMLEEKKQAIQEAAKLKAEAE--------------------KLQKQKDQAQVEAQklLEAKKEMQQRLDQETEGF 2549
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKnihgymkdienkiqdgkddyLKQKETELNTVNAQ--LEECEKHQEKINEDMRLM 1003
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2550 QKSLEAERKR------QLEITAEAEKLK---------------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEK 2607
Cdd:TIGR00606 1004 RQDIDTQKIQerwlqdNLTLRKRENELKeveeelkqhlkemgqMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1750-1906 |
1.54e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.61 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1750 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1829
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1830 QKANEALRLRLQAE------EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKL 1903
Cdd:TIGR02794 126 AKQAAEAKAKAEAEaerkakEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
...
gi 1207141740 1904 AAE 1906
Cdd:TIGR02794 206 AAE 208
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1317-1487 |
1.55e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.37 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1317 VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ----RATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQI 1392
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAaheeRVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1393 ELRQRELDLLNRQMQAYRESYDwLIRWIADAKQRQDKLhaVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGY 1472
Cdd:cd00176 96 EERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEEL 172
|
170
....*....|....*
gi 1207141740 1473 IDAIKDYELQLVTYK 1487
Cdd:cd00176 173 LEEGHPDADEEIEEK 187
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1197-1779 |
1.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1197 ESRTVNRLRQMVDKEPLKACTQRATEQKKVqtelEGIKKDLDKVVEKSEAVLATSQQSS-SAPVLRSEIDITQKKMEHVY 1275
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKKADAAKKKAEEAKkAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1276 GLSSVylDKLKTIDlvirSTQGAEDILNKYEnqlrEVNKVPVNEKEIEASQTQLQKLRSEAEGKQATfdrleEELQRATE 1355
Cdd:PTZ00121 1364 EKAEA--AEKKKEE----AKKKADAAKKKAE----EKKKADEAKKKAEEDKKKADELKKAAAAKKKA-----DEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1356 VNKRMSQLHSERDvELEHYRQLVGNLRERWQAVFAQIELRQ-RELDLLNRQMQAYRESyDWLIRWIADAKQRQDKLHAVP 1434
Cdd:PTZ00121 1429 EKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1435 IGGSKGLQEQLTQEKKLLEEIEK--NKDKVEDCQKF--AKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDII 1510
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1511 QEyvTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEerkkmaemqaelEKQKQLAETHAKAIAKAEQEANEL 1590
Cdd:PTZ00121 1587 KK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA------------EEEKKKVEQLKKKEAEEKKKAEEL 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1591 KTKMKDEVSKRQDVAVDSEKQKhniqRELQELKTLSEQEIKAKSQQVEEALLSRtRIEEeihiirlqlettMKQKNTAET 1670
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDK----KKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEE------------LKKKEAEEK 1715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1671 EllqlrakavDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlEKFKLQAEEAERHLK 1750
Cdd:PTZ00121 1716 K---------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE-----------------EKKKIAHLKKEEEKK 1769
|
570 580
....*....|....*....|....*....
gi 1207141740 1751 QAELEKQRQIQVVEEVAKKTAATQLESKQ 1779
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1781-2087 |
1.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1781 ALTARLE-----ESLKNEQVMVIQLQEEAEhlkkQQAEADKAREQAEKELETWRQKANEALRLRLQ---AEEEANKKTaa 1852
Cdd:PRK04863 288 ALELRRElytsrRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAASDHLNLVQTALRQQEKierYQADLEELE-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1853 qeeaekqkeeakreakkrAKAEEAALKQKEAAEmelgnQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD 1927
Cdd:PRK04863 362 ------------------ERLEEQNEVVEEADE-----QQEENEA---RAEAAEEEVDELKsqlADYQQAldVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1928 --------DELQRLKNDVNSAVKQKKELEEELikVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAAKM---- 1990
Cdd:PRK04863 416 yqqavqalERAKQLCGLPDLTADNAEDWLEEF--QAKEQEATeellsLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrse 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1991 -----RELAEEATKLRSVAEEAK---------KQRQIAEEEAARQRAEAEKILKEKLTAINEATRLkteaeiaLKEKEAE 2056
Cdd:PRK04863 494 awdvaRELLRRLREQRHLAEQLQqlrmrlselEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-------QEELEAR 566
|
330 340 350
....*....|....*....|....*....|.
gi 1207141740 2057 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 2087
Cdd:PRK04863 567 LESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
367-443 |
1.76e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 46.53 E-value: 1.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 367 DNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSiAERDLGVTRLLDPEDVDVPHPDEKSIITYVSS 443
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQ 95
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4322-4350 |
1.77e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.77e-05
10 20
....*....|....*....|....*....
gi 1207141740 4322 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4350
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1833-2065 |
1.86e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1833 NEALRLRLQAEEEANKKTAaqeeaEKQKEEAKREAKKRAKAEEAALKQkeaaEMELGNQRKMAEETAKQKLAAEQeliRL 1912
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ----EREIETARIAEAEAELAKKKAEE---RR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1913 RADFEHAEQQRTVlddELQRlkndvnsaVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqllESEAAKMRE 1992
Cdd:COG2268 256 EAETARAEAEAAY---EIAE--------ANAEREVQRQLEIAEREREIELQEKEAEREE------------AELEADVRK 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141740 1993 LAeeatklrsvaeEAKKQRQIAEEEaarqrAEAEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 2065
Cdd:COG2268 313 PA-----------EAEKQAAEAEAE-----AEAEAI-RAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE 368
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1559-1714 |
1.94e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1559 MAEMQAELEKQKQLAETHA-KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKAKSQQV 1637
Cdd:COG2268 194 IAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAK---KKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1638 EEALLSRTrIEEEIHIIRLQLETTMKQKNtAETELLQLRA---KAVDADKLRNAAQEEAE------KLRKQvAEETQKKR 1708
Cdd:COG2268 271 AEANAERE-VQRQLEIAEREREIELQEKE-AEREEAELEAdvrKPAEAEKQAAEAEAEAEaeairaKGLAE-AEGKRALA 347
|
....*.
gi 1207141740 1709 KAEEEL 1714
Cdd:COG2268 348 EAWNKL 353
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
229-330 |
2.08e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 47.03 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 229 VQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1207141740 305 NIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2211-2629 |
2.17e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2211 LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNA---EK 2287
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddlEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2288 EAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYK-KLAEKTLKQK 2366
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELReREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2367 SsVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLklklkiekenqelmkkdkdn 2446
Cdd:PRK02224 437 T-ARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVE-------------------- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2447 tKKLleEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEekkqaiqEAAKLKAEAEKLQKQKDQAQV 2526
Cdd:PRK02224 496 -ERL--ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE-------RAAELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2527 EAQKLLEAKKEMQQRLdqetegfqksleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2606
Cdd:PRK02224 566 EAEEAREEVAELNSKL------------AELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
410 420
....*....|....*....|...
gi 1207141740 2607 KHTSEKHTVVEKLEVQRLQSKQE 2629
Cdd:PRK02224 634 ERKRELEAEFDEARIEEAREDKE 656
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2459-2610 |
2.19e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2459 KKLAEEAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-----AKLKAEAEKLQKQKDQAQVEAQKLLE 2533
Cdd:COG4913 288 RRLELLEAELEELRAELARLEA-ELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 2534 AKKEMQQRLDQETEGFQksleaerKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTS 2610
Cdd:COG4913 367 LLAALGLPLPASAEEFA-------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2378-2545 |
2.28e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2378 VQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE----E 2453
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2454 EAENMKKlAEEAARLNIEAQEAARLrqiaesDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQAQVEAQKLL 2532
Cdd:COG1579 90 EYEALQK-EIESLKRRISDLEDEIL------ELMERIEELEEELAELEAELAELeAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|...
gi 1207141740 2533 EAKKEMQQRLDQE 2545
Cdd:COG1579 163 AEREELAAKIPPE 175
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2478-2924 |
2.37e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2478 LRQIAES-DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQK----------QKDQAQVEAQKLLEAKKEMQQRLDQET 2546
Cdd:pfam05483 50 LEQVANSgDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkQKENKLQENRKIIEAQRKAIQELQFEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2547 EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQS 2626
Cdd:pfam05483 130 EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2627 KQEadgLHKAIADLEKEKEKlkkeaadLQKQSKEMANVQQEQLQqekTILQQSffAEKETLLKKEKAIEEEKKKLEKQFE 2706
Cdd:pfam05483 210 RLE---MHFKLKEDHEKIQH-------LEEEYKKEINDKEKQVS---LLLIQI--TEKENKMKDLTFLLEESRDKANQLE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2707 DEVK-KAEALKAEQERQRKLMEEeRKKLQSAMDAAIKKQKEAEEEMN-----------GKQKEMQDLEKKRIEQEKLLAE 2774
Cdd:pfam05483 275 EKTKlQDENLKELIEKKDHLTKE-LEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNKAKAAHSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2775 ENKN-------LREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT-----MVETTKKVLNGSTEVDGVKKDvplaFDG 2842
Cdd:pfam05483 354 FEATtcsleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkevELEELKKILAEDEKLLDEKKQ----FEK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2843 IREKVPASRLHEIGVLSKKEYD------KLKKGKTTVQELSKNDKVKMCLKGKDCIGGVIVEPNQKMsiyQALKDKMITQ 2916
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREKEihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK---LLLENKELTQ 506
|
....*...
gi 1207141740 2917 STAIMLLE 2924
Cdd:pfam05483 507 EASDMTLE 514
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2185-2591 |
2.40e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.82 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2185 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEK--QVI-----LVQEAAQKCSAAEQKAQNVLVQQNKD 2257
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqQVIdnfpkLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2258 SMAQDKLK---EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedAEKLRKEAEKEasrr 2334
Cdd:PRK10929 106 ALEQEILQvssQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE----------------------ARRQLNEIERR---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2335 aeaeaaaLKLKQEADS--EMAKYKKLAEKTLKQKSSVEE-ELVkvkvQLDETDKQksvldvELKRLKQEVsdAIKQKAQV 2411
Cdd:PRK10929 160 -------LQTLGTPNTplAQAQLTALQAESAALKALVDElELA----QLSANNRQ------ELARLRSEL--AKKRSQQL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2412 EDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLeeeAENMKKLAEEAARLNIEAQE----AARLRQIAESDLa 2487
Cdd:PRK10929 221 DAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSI---VAQFKINRELSQALNQQAQRmdliASQQRQAASQTL- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2488 kQRELAEKMLEEKKQ------AIQEAakLKAEAEKL-------QKQKDQAQVEAQKL-LEAKKEMQQRLDQE-------- 2545
Cdd:PRK10929 297 -QVRQALNTLREQSQwlgvsnALGEA--LRAQVARLpempkpqQLDTEMAQLRVQRLrYEDLLNKQPQLRQIrqadgqpl 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 2546 TEGFQKSLEAERKRQ---------------LEITaeaeKLKVKVTQLSDAQSKAEEEAKKF 2591
Cdd:PRK10929 374 TAEQNRILDAQLRTQrellnsllsggdtliLELT----KLKVANSQLEDALKEVNEATHRY 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1560-1786 |
2.50e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1560 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEE 1639
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1640 AllsRTRIEEEIHIIRLQLETTMKQKNTAETELL------------------QLRAKAVDADKLRnAAQEEAEKLRKQVA 1701
Cdd:COG4942 95 L---RAELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqylkyLAPARREQAEELR-ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1702 EETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVA 1781
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1207141740 1782 LTARL 1786
Cdd:COG4942 251 LKGKL 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2444-2678 |
2.52e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2444 KDNTKKLLEEEAENMKKLAEEAARLNIEAQEAAR----LRQ-IAESDLAKQR-----ELAEKMLEE--KKQAIQEAAKLK 2511
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEevleLEQkLSVADAARRQfekayELVCKIAGEveRSQAWQTARELL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2512 AEAEKLQKQKDQAQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2589
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2590 KFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQeadglhkAIADLEKEKEKLKKEAADL--QKQSKEMANVQQE 2667
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGE-------ALADSQEVTAAMQQLLEREreATVERDELAARKQ 654
|
250
....*....|.
gi 1207141740 2668 QLQQEKTILQQ 2678
Cdd:COG3096 655 ALESQIERLSQ 665
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1921-2577 |
2.55e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.91 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1921 QQRTVLDDELQRLKndvnsavkqkkELEEElikVRKEMEILLQQKSKAEKETMSntekskqlLESEAAKMRELAEEATKL 2000
Cdd:pfam07111 63 QQAELISRQLQELR-----------RLEEE---VRLLRETSLQQKMRLEAQAME--------LDALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2001 RSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEAtrlkteAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQ 2080
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQA------HEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2081 HKQAIEEKIGQLKKSSDtELDRQKKIVEETlkqRKVVEE----EIHILKLNFEKassgKQELELELKKLKGIADETQKSK 2156
Cdd:pfam07111 195 AQKEAELLRKQLSKTQE-ELEAQVTLVESL---RKYVGEqvppEVHSQTWELER----QELLDTMQHLQEDRADLQATVE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2157 AKAEEEAEKFRKLALEEEKKRKEaeakVKQIQAAEEEAARQHKAA----QEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL 2232
Cdd:pfam07111 267 LLQVRVQSLTHMLALQEEELTRK----IQPSDSLEPEFPKKCRSLlnrwREKVFALMVQLKAQDLEHRDSVKQLRGQVAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2233 VQEAAqkcsAAEQKAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEaallHKKAEEAERQKKAAEAEAAK 2312
Cdd:pfam07111 343 LQEQV----TSQSQEQAILQRALQDKAAE--VEVERMSAKGLQMELSRAQEARRRQ----QQQTASAEEQLKFVVNAMSS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2313 QAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKykKLAEKTLKQKSSVEEELV-----KVKVQLDETDKQK 2387
Cdd:pfam07111 413 TQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMAR--KVALAQLRQESCPPPPPAppvdaDLSLELEQLREER 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2388 SVLDVELKR----LKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkiekenQELMKKdkdntkkllEEEAENMKKLAE 2463
Cdd:pfam07111 491 NRLDAELQLsahlIQQEVGRAREQGEAERQQLSEVAQQLE-------------QELQRA---------QESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2464 EAARLNIEA-QEAARLRQiaesDLAKQRELAEKMLEEKKQAIQeaAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2542
Cdd:pfam07111 549 VARQGQQEStEEAASLRQ----ELTQQQEIYGQALQEKVAEVE--TRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRA 622
|
650 660 670
....*....|....*....|....*....|....*
gi 1207141740 2543 DQETEgfqKSLEAERKRQLEITAEAEKLKVKVTQL 2577
Cdd:pfam07111 623 TQEKE---RNQELRRLQDEARKEEGQRLARRVQEL 654
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1314-1788 |
2.60e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1314 KVPVNEKEIEASQTQLQklrsEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGN--LRERWQAVFAQ 1391
Cdd:COG4717 65 KPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1392 IELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKG 1471
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1472 YIDAIKDyELQLVTYKALVEPIASPLKKAKMESASDDIIqeyVTLRTRYSELMTLSSQYIKFIIetqrrlqdeekAAEKL 1551
Cdd:COG4717 221 ELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLF-----------LVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1552 KEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIK 1631
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1632 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1711
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 1712 EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQ-IQVVEEVAKKTAATQLESKQVALTARLEE 1788
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAaLKLALELLEEAREEYREERLPPVLERASE 523
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2462-2667 |
2.61e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2462 AEEAARLNIEAQEAARLRQIAESDLAKQ-RELAEKMLEEKkQAIQEAAKLKAEAEKLQKQKDQAqveAQKLLEAKKEMQQ 2540
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQaEELQQKQAAEQ-ERLKQLEKERLAAQEQKKQAEEA---AKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2541 RLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQlSDAQSKAEEEAKkfKKQADEIKIRLQETEKHTSEKhtvvEKLE 2620
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAE-AEAAKKAAAEAK--KKAEAEAAAKAAAEAKKKAEA----EAKK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141740 2621 VQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE 2667
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1697-1905 |
2.62e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1697 RKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQVVEeVAKKTAATQLE 1776
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERET--------------------EIAIAQANREAEEAELEQEREIETAR-IAEAEAELAKK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1777 skqvaltarleeslkneqvmviqlQEEAEhlkkqqAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEA 1856
Cdd:COG2268 250 ------------------------KAEER------REAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEA 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207141740 1857 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1905
Cdd:COG2268 300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3247-3282 |
2.70e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.70e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1207141740 3247 LNLLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPE 3282
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2188-2366 |
2.79e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.84 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2188 QAAEEEAARQHK--AAQEEVGRLMKLAEEAKKQkeiAEKEAEKQvilVQEAAQKcSAAEQKAQnvlvqqnkdSMAQDKLK 2265
Cdd:TIGR02794 119 KQAEEAKAKQAAeaKAKAEAEAERKAKEEAAKQ---AEEEAKAK---AAAEAKK-KAEEAKKK---------AEAEAKAK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2266 EEFE---KAKKLAQEAEKAKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEaeaaal 2342
Cdd:TIGR02794 183 AEAEakaKAEEAKAKAEAAKAKAAAEAA---AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR------ 253
|
170 180
....*....|....*....|....
gi 1207141740 2343 klKQEADSEMAKYKKLAEKTLKQK 2366
Cdd:TIGR02794 254 --GAAAGSEVDKYAAIIQQAIQQN 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2584-2800 |
2.99e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2584 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2663
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2664 VQQEQLQQEKTIlqqsffaekETLLKKEkaieeekkklekQFEDEVKKAEALKAEQERQRKLMEE---ERKKLQSAMDAA 2740
Cdd:COG3883 94 ALYRSGGSVSYL---------DVLLGSE------------SFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2741 IKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2800
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1787-1952 |
3.03e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1787 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAE-EEANKKTAAQEEAEKQKEEAKR 1865
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1866 EAKKRAkaeEAALKQKEAAEMELGNQRKMAEETAKQKLaaeqelirlradfEHAEQQRTVLDDELQRLKNDVNSavkQKK 1945
Cdd:pfam05262 289 EIKKND---EEALKAKDHKAFDLKQESKASEKEAEDKE-------------LEAQKKREPVAEDLQKTKPQVEA---QPT 349
|
....*..
gi 1207141740 1946 ELEEELI 1952
Cdd:pfam05262 350 SLNEDAI 356
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
1006-1051 |
3.05e-05 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 3.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1207141740 1006 VQAVCDFKQME---ITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSI 1051
Cdd:cd11768 2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPSN 50
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1439-2097 |
3.72e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1439 KGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKAlvepiasplKKAKMESASDDIIQEYVTLRT 1518
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK---------EKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1519 RYSELMTLssqyikfiIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQlaethakAIAKAEQEANELK---TKMK 1595
Cdd:TIGR04523 202 LLSNLKKK--------IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT-------EISNTQTQLNQLKdeqNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1596 DEVSKRQDVAVDSEKQKHNIQRELQELKTlseqEIKAKSQQVEEALLSRtrieeeihiIRLQLETTMKQKNTAETELLQl 1675
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKS----EISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQISQ- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1676 rakavdADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHL-KQAEL 1754
Cdd:TIGR04523 333 ------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1755 EKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1834
Cdd:TIGR04523 407 NQQKDEQI------KKLQQEKELLEKEIERLKETIIKNNS-EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1835 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKrAKAEEAALKQKEaaemelgnqrkmaEETAKQKLAAEQELIRLRA 1914
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD-LTKKISSLKEKI-------------EKLESEKKEKESKISDLED 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1915 DFEHAEQQRTvlDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELA 1994
Cdd:TIGR04523 546 ELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1995 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAE--IALKEKEAENDRLKRKAEEEGYQRK 2072
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiIELMKDWLKELSLHYKKYITRMIRI 703
|
650 660
....*....|....*....|....*
gi 1207141740 2073 VLEDQAAQHKQAIEEKIGQLKKSSD 2097
Cdd:TIGR04523 704 KDLPKLEEKYKEIEKELKKLDEFSK 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1539-1747 |
3.80e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1539 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRE 1618
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1619 LQELKTLSEQ---EIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNtaetELLQLRAKAVDADKLRNAAQEEAEK 1695
Cdd:COG4942 110 LRALYRLGRQpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 1696 LRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF--KLQAEEAER 1747
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAA 239
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2185-2593 |
3.88e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 50.14 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2185 KQIQAAEEEAARQHKAAQEEVgrlmKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAaeqKAQNVLVQQNKDSMAQDKl 2264
Cdd:pfam09731 89 VKIPRQSGVSSEVAEEEKEAT----KDAAEAKAQLPKSEQEKEKALEEVLKEAISKAE---SATAVAKEAKDDAIQAVK- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2265 keefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAerqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKL 2344
Cdd:pfam09731 161 ----AHTDSLKEASDTAEISREKATDSALQKAEAL--------------------AEKLKEVINLAKQSEEEAAPPLLDA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2345 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqLDETDKQksVLDVELKRLKQEVSDAIKQK-AQVEDELSKVkiqME 2423
Cdd:pfam09731 217 APETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKE-LVASERI--VFQQELVSIFPDIIPVLKEDnLLSNDDLNSL---IA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2424 DLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQIAESdlakqrelaekmLEEKKQA 2503
Cdd:pfam09731 291 HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSA-RLEEVRAADEAQLRLE------------FEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2504 IQEAAKLKAEAEklqkQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS-LEAERKRQLEITAEAeKLKVK-VTQLSDAQ 2581
Cdd:pfam09731 358 IRESYEEKLRTE----LERQAEAHEEHLKDVLVEQEIELQREFLQDIKEkVEEERAGRLLKLNEL-LANLKgLEKATSSH 432
|
410
....*....|..
gi 1207141740 2582 SKAEEEAKKFKK 2593
Cdd:pfam09731 433 SEVEDENRKAQQ 444
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1562-1717 |
4.09e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1562 MQAELEKQKQLAETHAKaIAKAEQEANELK---TKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVE 1638
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKELPaelAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1639 --EALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKR 1716
Cdd:COG1579 77 kyEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
.
gi 1207141740 1717 K 1717
Cdd:COG1579 157 E 157
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
236-326 |
4.10e-05 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 45.75 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 236 KWVNKHLVKAQR---HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 308
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1207141740 309 DDIADGNPKLTLGLIWTI 326
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
2391-2625 |
4.43e-05 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 48.24 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2391 DVELKRLK------QEVSDAIKQKAQVEDELSKVKIQMEDLLKLklkiekenqelmkKDKDNTkklLEEEAENMKKLAEE 2464
Cdd:cd07647 8 DTLLQRLKegkkmcKELEDFLKQRAKAEEDYGKALLKLSKSAGP-------------GDEIGT---LKSSWDSLRKETEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2465 AARLNIEaqeaarlrqiaesdLAKQ-RELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLd 2543
Cdd:cd07647 72 VANAHIQ--------------LAQSlREEAEKLEEFREKQKEERKKTEDIMKRSQKNK---KELYKKTMKAKKSYEQKC- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2544 QETEGFQKSleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEVQR 2623
Cdd:cd07647 134 REKDKAEQA--YEKSSSGAQPKEAEKLKKKAAQCKTSAEEADSAYKSSIGCLEDAR---VEWESEHATACQVFQNMEEER 208
|
..
gi 1207141740 2624 LQ 2625
Cdd:cd07647 209 IK 210
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1567-2001 |
4.75e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1567 EKQKQLaethakaiakaeQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQelkTLSEQeIKAKSQQVEEAllsRTR 1646
Cdd:pfam10174 363 KKTKQL------------QDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE---NLQEQ-LRDKDKQLAGL---KER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1647 IEEeihiirLQLETTmkqknTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAK 1726
Cdd:pfam10174 424 VKS------LQTDSS-----NTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1727 EKKKALEDL-EKFKLQAEEA---ERHLKQAELEkqrqIQVVEEVAKKTAATQLESKQVALTARLEESLKNE-QVMVIQLQ 1801
Cdd:pfam10174 493 EKESSLIDLkEHASSLASSGlkkDSKLKSLEIA----VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQEVA 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1802 EEAEHLKKQQAEADK---AREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakreakkraKAEEAAL 1878
Cdd:pfam10174 569 RYKEESGKAQAEVERllgILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI------------------KHGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1879 KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLradfehaEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1958
Cdd:pfam10174 631 KKKGAQLLEEARRREDNLADNSQQLQLEELMGAL-------EKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL 703
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1207141740 1959 EILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 2001
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1629-1907 |
5.13e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1629 EIKAKSQQVEEALLSRTRIEEEIhiIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKR 1708
Cdd:PRK05035 437 EIRAIEQEKKKAEEAKARFEARQ--ARLEREK-------AAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1709 KAEEELKRKSEAEKDAakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvalTARLEE 1788
Cdd:PRK05035 508 IKAGARPDNSAVIAAR---------EARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANA---EAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1789 SLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAK 1868
Cdd:PRK05035 576 DPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP---KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141740 1869 KRAKAEEAALKQKEAAEMELGNQRKMAEETA----KQKLAAEQ 1907
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1801-2029 |
5.13e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1801 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEalRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAK-AEEAALK 1879
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLE--KERLAAQEQKKQA-----------EEAAKQAALKQKqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1880 QKEAAemelgnqrkmaeetakqKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEElikVRKEME 1959
Cdd:PRK09510 141 AAAAA-----------------KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKK----AAAEAKKKAEAE---AAAKAA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1960 ILLQQKSKAEKETMSNTEkSKQLLESEAAKMRELAEEATKlrSVAEEAKKQRQIAEEEAARQRAEAEKIL 2029
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAE-AKKKAAAEAKAAAAKAAAEAK--AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1781-2213 |
5.15e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1781 ALTARLE-----ESLKNEQVMVIQLQEEAEHLkkqqaeadkarEQAEKELETWRQKANEALRLRLQAEEEANKKtaaqee 1855
Cdd:COG3096 287 ALELRRElfgarRQLAEEQYRLVEMARELEEL-----------SARESDLEQDYQAASDHLNLVQTALRQQEKI------ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1856 aekqkeeakreAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD- 1927
Cdd:COG3096 350 -----------ERYQEDLEELTERLEEQEEVveEAAEQLAEAEA---RLEAAEEEVDSLKsqlADYQQAldVQQTRAIQy 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1928 -DELQRLKN----------DVNSAVKQKKELEEELIKVRKEMeILLQQKSKAEKETMSNTEKSKQLLESEAA-------- 1988
Cdd:COG3096 416 qQAVQALEKaralcglpdlTPENAEDYLAAFRAKEQQATEEV-LELEQKLSVADAARRQFEKAYELVCKIAGeversqaw 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1989 -KMRELAEEATKLRSVAEEAKK-QRQIAE-EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 2065
Cdd:COG3096 495 qTARELLRRYRSQQALAQRLQQlRAQLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2066 EEGYQRKVLEdqaaQHKQAIEEKIGQLKKS------SDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKqele 2139
Cdd:COG3096 575 EAVEQRSELR----QQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVER---- 646
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2140 lelkklkgiaDETQkskakaeeeaekFRKLALeeekkrkeaeakvkqiqaaEEEAARQHKAAQEEVGRLMKLAE 2213
Cdd:COG3096 647 ----------DELA------------ARKQAL-------------------ESQIERLSQPGGAEDPRLLALAE 679
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
230-338 |
5.18e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 46.59 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 230 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 296
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141740 297 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 338
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1906-2066 |
5.73e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1906 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLles 1985
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEY--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1986 eAAKMRELaEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEatrLKTEAEIALKEKEAENDRLKRKAE 2065
Cdd:COG1579 92 -EALQKEI-ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
.
gi 1207141740 2066 E 2066
Cdd:COG1579 167 E 167
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2443-2604 |
5.87e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.23 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2443 DKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmleekkqAIQEAAKLKAEAEKLQKQKD 2522
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2523 QAQVEAQKLLEAKKEMQQRLDQETEGFQKSlEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRL 2602
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKR-EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
..
gi 1207141740 2603 QE 2604
Cdd:pfam05262 331 EP 332
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1866-2114 |
5.87e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1866 EAKKRAKAEEAALKQKEAAEMELGNQrkmAEETAKQKLAAEQELIRLRADFEHAEQQRTVlddELQRLKndvnsAVKQKK 1945
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQ---AEEAEKQRAAEQARQKELEQRAAAEKAAKQA---EQAAKQ-----AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1946 ELEEELIKVRKEmeillqQKSKAEKEtmsntekSKQLLESEAAKMRElaEEATKlrSVAEEAKKQRQIAE---EEAARQR 2022
Cdd:TIGR02794 120 QAEEAKAKQAAE------AKAKAEAE-------AERKAKEEAAKQAE--EEAKA--KAAAEAKKKAEEAKkkaEAEAKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2023 AEAE-KILKEKLTAINEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ-LKKSSDTEL 2100
Cdd:TIGR02794 183 AEAEaKAKAEEAKAKAEAAKAKAAAE-AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGaRGAAAGSEV 261
|
250
....*....|....
gi 1207141740 2101 DRQKKIVEETLKQR 2114
Cdd:TIGR02794 262 DKYAAIIQQAIQQN 275
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1614-1953 |
6.27e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1614 NIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEA 1693
Cdd:COG4372 32 QLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1694 EKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1773
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1774 QLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQ 1853
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1854 EEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRL 1933
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1207141740 1934 KNDVNSAVKQKKELEEELIK 1953
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2185-2323 |
6.66e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2185 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQkeiAEKEAEKQVilvQEAAQKCSAAEQKAQNVLVQQNKdSMAQDKL 2264
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKKA---EAEAAKKAAAEAKKKAEAEAAAK-AAAEAKK 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2265 KEEFEKAKKLAQEAEK-----AKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2323
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKkaaaeAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1517-1933 |
8.61e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.75 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1517 RTRYSELMTLSSQYIKF---IIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTK 1593
Cdd:COG5278 106 QARLDELEALIDQWLAEleqVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1594 MKDEVSKRQDVAVDSEKQKHNIQRELQELkTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELL 1673
Cdd:COG5278 186 LALAELLLLALARALAALLLLLLLEAELA-AAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1674 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1753
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1754 LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN 1833
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1834 EALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLR 1913
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410 420
....*....|....*....|
gi 1207141740 1914 ADFEHAEQQRTVLDDELQRL 1933
Cdd:COG5278 505 LAALLLAAAEAALAAALAAA 524
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2671-2800 |
8.71e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 48.05 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2671 QEKTILQQsFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRklmeEERKKLQSAMDAAIKKQKEAEEE 2750
Cdd:pfam02841 173 KAEEVLQE-FLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLR----EKQKEEEQMMEAQERSYQEHVKQ 247
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2751 MngKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2800
Cdd:pfam02841 248 L--IEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQD 295
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1788-2072 |
8.74e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1788 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1867
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE-LNAQVKELREEAQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1868 KKRAKAEEAALKQKEAaemELGNQRKMAEETAKQKLAAEQELIRLRAdfehaEQQRTVLD--------DELQRLKNDVNs 1939
Cdd:COG1340 80 RDELNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEW-----RQQTEVLSpeeekelvEKIKELEKELE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1940 AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 2019
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHE----EMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1207141740 2020 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRK 2072
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKG 279
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2451-2662 |
9.22e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.79 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2451 LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdlAKQRELAekmLEEKKQAIQEAAKLKAEA-EKLQKQKDQAQVEAQ 2529
Cdd:pfam15709 309 MESEEERSEEDPSKALLEKREQEKASRDRLRAER--AEMRRLE---VERKRREQEEQRRLQQEQlERAEKMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2530 KLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAEAEK-------LKVKVTQLS-DAQSKAEEEAKKFKKQADEIKIR 2601
Cdd:pfam15709 384 RRFEEIRLRKQRLEEER---QRQEEEERKQRLQLQAAQERarqqqeeFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQ 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 2602 LQETEKHTSEKhTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMA 2662
Cdd:pfam15709 461 LAEEQKRLMEM-AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2487-2754 |
9.28e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2487 AKQRELAEKMLEEKKQAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLdQETEGFQKSLEAErkrqleitae 2566
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAE---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2567 aeklkvkvtqLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVeklevqrLQSKQEADGLHKAIADLEKEKEK 2646
Cdd:COG4942 85 ----------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL-------LLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2647 LKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLM 2726
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|....*...
gi 1207141740 2727 EEERKKLQSAMDAAIKKQKEAEEEMNGK 2754
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1914-2287 |
1.06e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1914 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKetmsntekskqllESEAAKMR-E 1992
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ-------------DYQAASDHlN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1993 LAEEAtklrsVAEEAKKQRQIAEEEAARQRAEAEKILKEkltainEATRLKTEAEIALKEKEAENDRLkrKAEEEGYQRK 2072
Cdd:PRK04863 339 LVQTA-----LRQQEKIERYQADLEELEERLEEQNEVVE------EADEQQEENEARAEAAEEEVDEL--KSQLADYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2073 --VLEDQAAQHKQAIE--EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGI 2148
Cdd:PRK04863 406 ldVQQTRAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2149 ADETQKSkakaeEEAEKFRKLaLEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQeevgRLMKLAEEAKKQKEIAEKEAEK 2228
Cdd:PRK04863 486 AGEVSRS-----EAWDVAREL-LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2229 QVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEK 2287
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3907-3943 |
1.10e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1207141740 3907 IDLLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEF 3943
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2200-2413 |
1.12e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2200 AAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVilvQEAAQKCSAAEQKAQnvlvQQNKDSMAQDKLKEEFEKAKKLAQEAE 2279
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQA---EELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2280 KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAlKLKQEADSEM-AKYKKL 2358
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAeAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2359 AEKTLKQKSSVEEELVKVKvqldETDKQKSVLDVELKRLKQEVSDAIKQKAQVED 2413
Cdd:PRK09510 211 AAAEAKKKAAAEAKAAAAK----AAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1958-2424 |
1.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1958 MEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEE-AKKQRQIAEEEAARQRAEAEKILKEKLTAI 2036
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2037 NEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKV--LEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 2113
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2114 RKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAeee 2193
Cdd:COG4717 208 LAELEEELEEAQ---EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL--- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2194 aarqhkaaqeEVGRLMKLAEEAKKQKEIAEKEAEKqvilVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKK 2273
Cdd:COG4717 282 ----------VLGLLALLFLLLAREKASLGKEAEE----LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2274 LAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaAKQAKAQEDAEKLRKEAEKeasrrAEAEAAALKLKQEADSEMA 2353
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAA----------LLAEAGVEDEEELRAALEQ-----AEEYQELKEELEELEEQLE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2354 KYKKLAEKTLKQ--KSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQK--AQVEDELSKVKIQMED 2424
Cdd:COG4717 413 ELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1657-2080 |
1.15e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1657 QLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLE 1736
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1737 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADK 1816
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1817 AREQAEKELETWRQKANEALRLRLQAEEEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE 1896
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALA-----ELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1897 ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT 1976
Cdd:COG5278 346 LLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1977 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 2056
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1207141740 2057 NDRLKRKAEEEGYQRKVLEDQAAQ 2080
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1755-2072 |
1.17e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.11 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1755 EKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETW 1828
Cdd:pfam15558 4 ERDRKIAALMLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQsqeqwqAEKEQRKARLGREERRRAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1829 RQKANEAL---RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALkQKEAAEMELGNQRKMAE--------- 1896
Cdd:pfam15558 84 RREKQVIEkesRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL-QALREQNSLQLQERLEEachkrqlke 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1897 --------ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKA 1968
Cdd:pfam15558 163 reeqkkvqENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1969 EKETMSNTEKSKQLLESEAAKMRelaeeatKLRSVAEEAKKQR--QIAEEEAARQRaeAEKILKEKLTAINEATRLKTEA 2046
Cdd:pfam15558 243 EEKEEERQEHKEALAELADRKIQ-------QARQVAHKTVQDKaqRARELNLEREK--NHHILKLKVEKEEKCHREGIKE 313
|
330 340
....*....|....*....|....*.
gi 1207141740 2047 EIALKEKEAENDRLKRKAEEEGYQRK 2072
Cdd:pfam15558 314 AIKKKEQRSEQISREKEATLEEARKT 339
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1734-2034 |
1.18e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1734 DLEKFKLQAEEAERHLKQAELEKQRQIQvveevakktAATQLEsKQVALTARLEEslkneQVMVIQ---LQEEAEHLKKQ 1810
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRS---------QLEQAK-EGLSALNRLLP-----RLNLLAdetLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1811 QAEADKAR----------EQAEKELETWRQKANEALRLRLQAEEeankktaaqeeaekqkeeakreakkrAKAEEAALKQ 1880
Cdd:PRK04863 903 LDEAEEAKrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDYQQ--------------------------AQQTQRDAKQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1881 KEAAEMELgNQRK--MAEETAKQKLAAEQEL-IRLRADFEHAEQQRTVLDDEL--------------QRLKNDVNSAVKQ 1943
Cdd:PRK04863 957 QAFALTEV-VQRRahFSYEDAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQM 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1944 KKELEEEL--IKVR--KEMEILLQQKSKAEKETMSNT-------EKSKQLLESE----AAKMRELAEEATKLRSVAEEAK 2008
Cdd:PRK04863 1036 LQELKQELqdLGVPadSGAEERARARRDELHARLSANrsrrnqlEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAK 1115
|
330 340
....*....|....*....|....*.
gi 1207141740 2009 KqRQIAEEEAARQRAEAEKILKEKLT 2034
Cdd:PRK04863 1116 A-GWCAVLRLVKDNGVERRLHRRELA 1140
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2706-2798 |
1.19e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2706 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2785
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90
....*....|...
gi 1207141740 2786 LQSSQKASYTKEI 2798
Cdd:COG4942 113 LYRLGRQPPLALL 125
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2456-2677 |
1.33e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2456 ENMKKLAEE-AARLNIEAQEAARLRQIAESDLAKQREL--AEKMLEEKKQAIQEAAKLKAEAEKLQkQKDQAQVEAQKLL 2532
Cdd:PRK10929 75 DNFPKLSAElRQQLNNERDEPRSVPPNMSTDALEQEILqvSSQLLEKSRQAQQEQDRAREISDSLS-QLPQQQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2533 eakKEMQQRLdqETEGFQKSLEAERKRQLeITAEAEKLKVKVTQLSDAQSKAEE-------EAKKFKKQADEIKIRLQET 2605
Cdd:PRK10929 154 ---NEIERRL--QTLGTPNTPLAQAQLTA-LQAESAALKALVDELELAQLSANNrqelarlRSELAKKRSQQLDAYLQAL 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2606 EKH-TSEKHTVVEK-LEVQRLQSKQEADgLHKAIADLEKEKEKLkkeAADLQKQSKEMANVQQEQLQQEKTILQ 2677
Cdd:PRK10929 228 RNQlNSQRQREAERaLESTELLAEQSGD-LPKSIVAQFKINREL---SQALNQQAQRMDLIASQQRQAASQTLQ 297
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1227-2136 |
1.34e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1227 QTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSE---IDITQKKMEHVYGLSSVYLDKLKTiDLVIRSTQGAEDIlN 1303
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKnelLDIIVEIKKHIHGEINKDLNKILE-DFKNKEKELSNKI-N 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1304 KYENQLREVNKVPVNEKEIEA---SQTQLQKLRSEaEGKQaTFDRLEEELQ----RATEVNKRMSQLHSERD---VELEH 1373
Cdd:TIGR01612 773 DYAKEKDELNKYKSKISEIKNhynDQINIDNIKDE-DAKQ-NYDKSKEYIKtisiKEDEIFKIINEMKFMKDdflNKVDK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1374 YRQLVGNLRERWQA---VFAQI------ELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVP--IGGSKGLQ 1442
Cdd:TIGR01612 851 FINFENNCKEKIDSeheQFAELtnkikaEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDeyIKICENTK 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1443 EQL----TQEKKLLEEIEKNKDKVEDCQKFAKGYIDaikDYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRT 1518
Cdd:TIGR01612 931 ESIekfhNKQNILKEILNKNIDTIKESNLIEKSYKD---KFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKA 1007
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1519 RY--SELMTLSSQYI---KFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQ--KQLAETHAKAIAKAEQEA---N 1588
Cdd:TIGR01612 1008 NLgkNKENMLYHQFDekeKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINItnfN 1087
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1589 ELKTKMK----------------DEVSK-RQDVAVDSEKQKHNIqRELQELKTLSEQ---EIKAKSQQVEEaLLSRTRIE 1648
Cdd:TIGR01612 1088 EIKEKLKhynfddfgkeenikyaDEINKiKDDIKNLDQKIDHHI-KALEEIKKKSENyidEIKAQINDLED-VADKAISN 1165
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1649 EEIHIIRLQLETTM----KQKNTAE------TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEE------ 1712
Cdd:TIGR01612 1166 DDPEEIEKKIENIVtkidKKKNIYDeikkllNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmikam 1245
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1713 --------ELKRKSEAEKDAAKEKKKALEDLEKFKLQAEE-------AERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1777
Cdd:TIGR01612 1246 eayiedldEIKEKSPEIENEMGIEMDIKAEMETFNISHDDdkdhhiiSKKHDENISDIREKSLKIIEDFSEESDINDIKK 1325
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1778 KqvaLTARLEESLKNEQVMVIQLQEEAE-----HLKKQQAEADKAREQAeKELETWRQKANEAL----RLRLQAEEEANK 1848
Cdd:TIGR01612 1326 E---LQKNLLDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYT-KEIEENNKNIKDELdkseKLIKKIKDDINL 1401
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1849 KTAAQEEAEKQKEEAKREAKKRAK-------AEEAALKQ--KEAAEME-----LGNQRKMAEETAKQKLAAEQELIRLRA 1914
Cdd:TIGR01612 1402 EECKSKIESTLDDKDIDECIKKIKelknhilSEESNIDTyfKNADENNenvllLFKNIEMADNKSQHILKIKKDNATNDH 1481
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1915 DFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAE-KETMSNTEK-SKQLLESEAAKMRE 1992
Cdd:TIGR01612 1482 DFNINELKEHI--DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAiKNKFAKTKKdSEIIIKEIKDAHKK 1559
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1993 LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRL------KTEAEIALKEKEA----------- 2055
Cdd:TIGR01612 1560 FILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFlkisdiKKKINDCLKETESiekkissfsid 1639
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2056 -ENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKigqlKKSSDtELDRQKKIVEETLKQRK------VVEEEIHILKLNF 2128
Cdd:TIGR01612 1640 sQDTELKENGDNLNSLQEFLESLKDQ-KKNIEDK----KKELD-ELDSEIEKIEIDVDQHKknyeigIIEKIKEIAIANK 1713
|
....*...
gi 1207141740 2129 EKASSGKQ 2136
Cdd:TIGR01612 1714 EEIESIKE 1721
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2196-2785 |
1.39e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2196 RQHKAA-QEEVGRLMKLAEEAKkQKEIAE------KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ--DKLKE 2266
Cdd:pfam12128 230 IQAIAGiMKIRPEFTKLQQEFN-TLESAElrlshlHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEkrDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2267 EfekakKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAaalkLKQ 2346
Cdd:pfam12128 309 E-----LSAADAAVAKDRSELEALEDQHGAFLDA------------------DIETAAADQEQLPSWQSELEN----LEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2347 EADSEMAKYKKLAEKTLKQKSSVEEELV-KVKVQLDETDKQKSVLDvelkRLKQEVSDAI-KQKAQVEDELSKVKIQMED 2424
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGIKDKLAKIREARD----RQLAVAEDDLqALESELREQLEAGKLEFNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2425 LlklklkiekenqelmkkdkdntKKLLEEEAENMKklaeeaARLNIEAQEAARLRQIAESDlakqrELAEKMLEEKKQAI 2504
Cdd:pfam12128 438 E----------------------EYRLKSRLGELK------LRLNQATATPELLLQLENFD-----ERIERAREEQEAAN 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2505 QEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-ETEGFQKS------LEAE----RKRQLEITAEAEKLKVK 2573
Cdd:pfam12128 485 AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElELQLFPQAgtllhfLRKEapdwEQSIGKVISPELLHRTD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2574 VTQLSDAQSKAEE-------------EAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADL 2640
Cdd:pfam12128 565 LDPEVWDGSVGGElnlygvkldlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2641 EKEKEKLKKeaaDLQKQSKEManvQQEQLQQEKTILQQSFFAEKEtlLKKEKAIEEEKKKLEKQFEDEVKKaEALKAEQE 2720
Cdd:pfam12128 645 RTALKNARL---DLRRLFDEK---QSEKDKKNKALAERKDSANER--LNSLEAQLKQLDKKHQAWLEEQKE-QKREARTE 715
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 2721 RQ--RKLMEEERKKLQSAMDAAI-KKQKEAEEEMNGKQKEM-QDLEKKRIEQEKL--LAEENKNLREKLQQ 2785
Cdd:pfam12128 716 KQayWQVVEGALDAQLALLKAAIaARRSGAKAELKALETWYkRDLASLGVDPDVIakLKREIRTLERKIER 786
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2463-2756 |
1.40e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.94 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2463 EEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2542
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2543 DQETEGFQKSLEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEE-----AKKFKKQADEIKIRLQETEKHTSEKHTVVE 2617
Cdd:pfam02029 140 YQENKWSTEVRQAEEE------GEEEEDKSEEAEEVPTENFAKEEvkdekIKKEKKVKYESKVFLDQKRGHPEVKSQNGE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2618 KlEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA----DLQKQSKEMANVQQEQLQQEktilQQSFFAEKETLLKKEKA 2693
Cdd:pfam02029 214 E-EVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqkleELRRRRQEKESEEFEKLRQK----QQEAELELEELKKKREE 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2694 IEEEKKKLEKQFEDEvkKAEALKAEQERQRKLMEE-ERKKlqsaMDAAIKKQKEAEEEMNGKQK 2756
Cdd:pfam02029 289 RRKLLEEEEQRRKQE--EAERKLREEEEKRRMKEEiERRR----AEAAEKRQKLPEDSSSEGKK 346
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2389-2759 |
1.45e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2389 VLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARL 2468
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2469 NIEAQEAARLRQIAESDLAKQRELAE--KMLEEKKQAIQ-EAAKLKAEAEKLQKQKDQAQVEaQKLLEAKKEMQQrldQE 2545
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEdiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE-RKQLQAKLQQTE---EE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2546 TEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKA---EEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2622
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2623 RLQSKQEadgLHKAiadlekekeklKKEAADLQKQSKEMANVQQE---QLQQEKTILQQSFFAEKETLLKKEKAIEEEKK 2699
Cdd:pfam07888 267 RDRTQAE---LHQA-----------RLQAAQLTLQLADASLALREgraRWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2700 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQ 2759
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4572-4609 |
1.46e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141740 4572 QRFLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTA 4609
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1879-2084 |
1.46e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1879 KQKEAAEMElgNQRKMAEETAKQKLAAEQElirlradfehAEQQRtVLDDELQRLKndvnsAVKQKKELEEElikvrkEM 1958
Cdd:PRK09510 70 QQKSAKRAE--EQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERLA-----AQEQKKQAEEA------AK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1959 EILLQQKsKAEKETMSNTEKSKqlLESEAAKMReLAEEATKlrsvAEEAKKQRQIAE-----EEAARQRAEAEKILKEKL 2033
Cdd:PRK09510 126 QAALKQK-QAEEAAAKAAAAAK--AKAEAEAKR-AAAAAKK----AAAEAKKKAEAEaakkaAAEAKKKAEAEAAAKAAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 2034 TAINEATRLKTEAEIALKEKEAENDRlKRKAEEEGYQRKVLEDQAAQHKQA 2084
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAEA-KAAAAKAAAEAKAAAEKAAAAKAA 247
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1618-1951 |
1.67e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1618 ELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKavdadklRNAAQEEAEKLR 1697
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1698 KQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1777
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1778 KQVALTARLEESLKNEQVmVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1857
Cdd:COG4372 167 AALEQELQALSEAEAEQA-LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1858 KQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDV 1937
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 1207141740 1938 NSAVKQKKELEEEL 1951
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2464-2600 |
1.68e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2464 EAARLNIeAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQEAAKLKaeaEKLQKQKDQAQ-VEAQKLLEAKKEMQQRL 2542
Cdd:PRK00409 505 EEAKKLI-GEDKEKLNELIASLEELERELEQK-AEEAEALLKEAEKLK---EELEEKKEKLQeEEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2543 DQETEgfqkslEAERK-RQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKI 2600
Cdd:PRK00409 580 KEAKK------EADEIiKELRQLQKGGYASVKAHELIEARKrlnkaneKKEKKKKKQKEKQEELKV 639
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
230-337 |
1.69e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 45.00 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 230 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 296
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141740 297 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 337
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
231-296 |
1.70e-04 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 43.80 E-value: 1.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 231 KKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 296
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2488-2801 |
1.72e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2488 KQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL---LEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT 2564
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLeeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2565 AEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAdlEKEK 2644
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2645 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2724
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 2725 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQ 2801
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1930-2099 |
1.82e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1930 LQRLKNDVNSAVKQKKELEEElikvrKEMEilLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKK 2009
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ-----QAEE--LQQKQAAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2010 QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENdrlKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 2089
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKKKAA 212
|
170
....*....|
gi 1207141740 2090 GQLKKSSDTE 2099
Cdd:PRK09510 213 AEAKKKAAAE 222
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2711-2812 |
1.87e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2711 KAEALKAEQERQRKLMEEER-------KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2783
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKeaeaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100
....*....|....*....|....*....
gi 1207141740 2784 QQLQSSQKASYTKEIEIQTDKVPEEELVQ 2812
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1743-2119 |
2.19e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.44 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1743 EEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESlkneqvmviqlqeeaEHLKKQQAEADKAREQAE 1822
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVS---------------SEVAEEEKEATKDAAEAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1823 KELETWRQKANEALRLRLQ-AEEEANKKTAAQEEAekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMaEETAKQ 1901
Cdd:pfam09731 117 AQLPKSEQEKEKALEEVLKeAISKAESATAVAKEA---------KDDAIQAVKAHTDSLKEASDTAEISREKA-TDSALQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1902 KLAAEQELIRLRADFEHAEQQrTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ 1981
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1982 LLESEAAKMREL-AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 2060
Cdd:pfam09731 266 IFPDIIPVLKEDnLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEA 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2061 KRKAEeegYQRKVLEDQaaqhkQAIEEKIgqlkkssDTELDRQKKIVEETLKQRKVVEE 2119
Cdd:pfam09731 346 QLRLE---FEREREEIR-----ESYEEKL-------RTELERQAEAHEEHLKDVLVEQE 389
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2478-2637 |
2.32e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2478 LRQIAESDLAKQRELAEKMLEE--------KKQAIQEA----AKLKAEAEKLQKQKDQaqvEAQKLLEAKKEMQQRLDQE 2545
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEakkeaeaiKKEALLEAkeeiHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2546 TEGFQK---SLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFkkQADEIK-IRLQETEKHTSEK--HTVVEKL 2619
Cdd:PRK12704 102 LELLEKreeELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKeILLEKVEEEARHEaaVLIKEIE 179
|
170
....*....|....*...
gi 1207141740 2620 EvqrlQSKQEADGLHKAI 2637
Cdd:PRK12704 180 E----EAKEEADKKAKEI 193
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2346-2579 |
2.66e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.33 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2346 QEADSEMAKYKKLAEKTLKQKSsvEEELVKVKVQLDETDKQKSVLDVELKRLKQEVsdaikqkAQVEDELSKVKIQMEdl 2425
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQR--EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2426 lklklkIEKENQELMKKdkdnTKKLLEEEAENMKKL----AEEAARL-NIEAQ-EAARlrqiaESDLAKQRELAEKMLEE 2499
Cdd:pfam05667 381 ------ELEKQYKVKKK----TLDLLPDAEENIAKLqalvDASAQRLvELAGQwEKHR-----VPLIEEYRALKEAKSNK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2500 KKqaiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSleAERKRQLEITAEAEKLKVKVTQ-LS 2578
Cdd:pfam05667 446 ED----ESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRS--AYTRRILEIVKNIKKQKEEITKiLS 519
|
.
gi 1207141740 2579 D 2579
Cdd:pfam05667 520 D 520
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2958-2995 |
2.74e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.74e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141740 2958 TKLLSAERAVTGFKDPFTGDTISVFEAMKKGLITEDQA 2995
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2475-2679 |
3.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2475 AARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLE 2554
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2555 AERKRQ-----LEITAEAEKLK------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKL--EV 2621
Cdd:COG3883 94 ALYRSGgsvsyLDVLLGSESFSdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2622 QRLQSKQEADgLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQS 2679
Cdd:COG3883 174 EAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3324-3359 |
3.17e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.17e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1207141740 3324 RLLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEM 3359
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1674-1835 |
3.33e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1674 QLRAKAVDADKLRN--AAQEEAEKLRKQVAE-----ETQKKRKAEEELKRKSEAEKDAAKEKKKALED-----LEKFKLQ 1741
Cdd:PRK09510 69 QQQKSAKRAEEQRKkkEQQQAEELQQKQAAEqerlkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEaaakaAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1742 AEEAERHL----KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1817
Cdd:PRK09510 149 AEAEAKRAaaaaKKAAAEAKKKAE--AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170
....*....|....*...
gi 1207141740 1818 REQAEKELETWRQKANEA 1835
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAA 244
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1820-2132 |
3.40e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 46.82 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1820 QAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQ--RKMAEE 1897
Cdd:pfam15964 321 SSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKemKKEREE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1898 TAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQrlkndvnSAVKQKKELEEELIKVRKEMEILLQQkSKAEKEtmsntE 1977
Cdd:pfam15964 401 LGATMLALSQNVAQLEAQVEKVTREKNSLVSQLE-------EAQKQLASQEMDVTKVCGEMRYQLNQ-TKMKKD-----E 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1978 KSKQLLESEAAKMRELA---EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKIlkekltaineaTRLKTEAEIALKEKE 2054
Cdd:pfam15964 468 AEKEHREYRTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQDAARAREECLKL-----------TELLGESEHQLHLTR 536
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2055 AENDRLKRKAEEEGyqrKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 2132
Cdd:pfam15964 537 LEKESIQQSFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT 611
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4462-4495 |
3.47e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.47e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141740 4462 EETGPVAGILDTDTLEKVSVTEAMHRNLVDNITG 4495
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1626-1877 |
3.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1626 SEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELlqlrakavdadklrNAAQEEAEKLRKQVAEETQ 1705
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------------EALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1706 KKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQ---RQIQVVEEVakKTAATQLESKQval 1782
Cdd:COG3883 80 EIEERREELGE-----RARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKiadADADLLEEL--KADKAELEAKK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1783 tARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEE 1862
Cdd:COG3883 150 -AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*
gi 1207141740 1863 AKREAKKRAKAEEAA 1877
Cdd:COG3883 229 AAAAAAAAAAAAAAA 243
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2357-2634 |
3.64e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2357 KLAEKTLKQKSSVEEelvkVKVQLDETDKQKSVLDVELKRLKQEVSD-----------AIkQKAQVEDELSKVKIQMEDL 2425
Cdd:PRK04863 359 ELEERLEEQNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtrAI-QYQQAVQALERAKQLCGLP 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2426 LKLKLKIEKENQELMKKDKDNTKKLLEEE-----AENMKKLAEEAARL------NIEAQEAARLRQIAESDLAKQRELAE 2494
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAE 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2495 KM---------LEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITA 2565
Cdd:PRK04863 514 QLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 2566 EAEKLKVKVTQLSDAQSKAEE------EAKKFKKQADEIKIRLQETEKHTSEkhtVVEKLEVQRLQSKQEADGLH 2634
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALARlreqsgEEFEDSQDVTEYMQQLLERERELTV---ERDELAARKQALDEEIERLS 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2385-2636 |
3.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2385 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLkiekenqelmkkdkdntkklLEEEAENMKKLAEE 2464
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE--------------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2465 AARLNieaQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ 2544
Cdd:COG4913 670 IAELE---AELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2545 ETEgfqKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKL-EVQR 2623
Cdd:COG4913 746 ELR---ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN---REWPAETADLDADLESLpEYLA 819
|
250
....*....|...
gi 1207141740 2624 LQSKQEADGLHKA 2636
Cdd:COG4913 820 LLDRLEEDGLPEY 832
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1915-2799 |
3.85e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1915 DFEHAEQQRTVLDDELQRLKNDVNSAVK-QKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ-LLESEAAKMRE 1992
Cdd:TIGR00606 55 DFPPGTKGNTFVHDPKVAQETDVRAQIRlQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHgEKVSLSSKCAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1993 LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR----LKTEAEIAL------KEKEAENDRLKR 2062
Cdd:TIGR00606 135 IDREMISHLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRyikaLETLRQVRQtqgqkvQEHQMELKYLKQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2063 KAEEEGYQRKVLEDQAAQhkQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekasSGKQELELEL 2142
Cdd:TIGR00606 215 YKEKACEIRDQITSKEAQ--LESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK-------SRKKQMEKDN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2143 KKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeakvKQIQAAEEEAARQHKaaqeEVGRLMKLAEEAKKQKeiA 2222
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQ----------------RTVREKERELVDCQR----ELEKLNKERRLLNQEK--T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2223 EKEAEKQVILVQEAAQKCsaaEQKAQNVLVQQNKDSMAQDKLKE------EFEKAKKLAQE--AEKAKDNAEKEAALLHK 2294
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQE---HIRARDSLIQSLATRLELDGFERgpfserQIKNFHTLVIErqEDEAKTAAQLCADLQSK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2295 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2374
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2375 KVKVQLDEtdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD--NTKKL-- 2450
Cdd:TIGR00606 501 KEVKSLQN---EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpNKKQLed 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2451 -LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLaKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2529
Cdd:TIGR00606 578 wLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-ESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2530 KLLEAKKEMQQRLDQETEGFQKSL---EAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR----- 2601
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrq 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2602 --LQETEKHTSEKHTVVEKL--EVQRLQSKQEADglhkaiADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQ 2677
Cdd:TIGR00606 737 siIDLKEKEIPELRNKLQKVnrDIQRLKNDIEEQ------ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQ 810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2678 QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALK---------------------------AEQERQRKLMEEER 2730
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktnelkseklqiGTNLQRRQQFEEQL 890
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 2731 KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSS--QKASYTKEIE 2799
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkNIHGYMKDIE 961
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1742-2067 |
4.37e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1742 AEEAERHLKQAELEKQRQIQVVEEVAK------KTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAd 1815
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGqvtesvEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1816 karEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKeeakreaKKRAKAEEAALKQKEAAEMELGNQRKMA 1895
Cdd:pfam02029 83 ---LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR-------LGRYKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1896 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN 1975
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1976 T----EKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQiaeEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALK 2051
Cdd:pfam02029 233 SqereEEAEVFLEAEQ-KLEELRRRRQEKESEEFEKLRQKQ---QEAELELEELKKKREER-RKLLEEEEQRRKQEEAER 307
|
330
....*....|....*.
gi 1207141740 2052 EKEAENDRLKRKAEEE 2067
Cdd:pfam02029 308 KLREEEEKRRMKEEIE 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1260-1464 |
4.77e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1260 LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAediLNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGK 1339
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAAL------EAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1340 QATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRW 1419
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207141740 1420 IADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVED 1464
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2196-2520 |
4.88e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2196 RQHKAAQEEVGRLMKLAEEAK-----KQ----KEIAEKEAEKqvilvQEAAQKCSAAEQKAqnvlVQQNKDSMAQDKLKE 2266
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeaRQarleREKAAREARH-----KKAAEARAAKDKDA----VAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2267 EFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqaKAQEDAEKLRKEAekeasrraeaeaaalklkQ 2346
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAE--------------KQAAAAADPKKAA------------------V 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2347 EADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqldetdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLL 2426
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAV-------AAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIAR 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2427 KLKLKIEKENQElmkkdkdntkklLEEEAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRElaekmLEEKKQAIqE 2506
Cdd:PRK05035 624 AKAKKAEQQANA------------EPEEPVDPRKAAVAAAI----ARAKARKAAQQQANAEPEEA-----EDPKKAAV-A 681
|
330
....*....|....
gi 1207141740 2507 AAKLKAEAEKLQKQ 2520
Cdd:PRK05035 682 AAIARAKAKKAAQQ 695
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2710-2799 |
5.03e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.65 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2710 KKAEALKAEQ-ERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMngKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQS 2788
Cdd:cd16269 200 IEAERAKAEAaEQERKLLEEQQRELEQKLEDQERSYEEHLRQL--KEKMEEERENLLKEQERALESKLKEQEALLEEGFK 277
|
90
....*....|.
gi 1207141740 2789 SQKASYTKEIE 2799
Cdd:cd16269 278 EQAELLQEEIR 288
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2458-2597 |
5.53e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2458 MKKLAEEAARLNIEAQEAARlRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL--LEAK 2535
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAE-EKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLdnLENQ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2536 KEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2597
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE 168
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2377-2619 |
5.60e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2377 KVQLDETDKQKSVLDVELKRLKQEVsdAIKQKAQVE-DELSKVKIQ----MEDLLKLKLKIEKENQELMKKDKDNTKKLL 2451
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQI--KTYNKNIEEqRKKNGENIArkqnKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2452 EEEAENMKKLAEEAARLNIEAQEAARLrqiaesdlakqrelaEKMLEEK------KQAIQEAAKLkaeAEKLQKQKDQAQ 2525
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKV---------------IKMYEKGgvcptcTQQISEGPDR---ITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2526 VEAQKLLEAKKEMQQRLDQETE------GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2599
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEqskkllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|
gi 1207141740 2600 IRLQETEKHTSEKHTVVEKL 2619
Cdd:PHA02562 393 KTKSELVKEKYHRGIVTDLL 412
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1875-2118 |
6.58e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1875 EAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKV 1954
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1955 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLT 2034
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2035 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQR 2114
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
....
gi 1207141740 2115 KVVE 2118
Cdd:COG4372 288 LEEA 291
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1928-2601 |
6.77e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1928 DELQRLKNDVNSaVKQK-----KELEEELIKVRKEMEILLQQKSKAEK---ETMSN-----TEKSKQLLESEAAKMRELA 1994
Cdd:TIGR01612 1111 DEINKIKDDIKN-LDQKidhhiKALEEIKKKSENYIDEIKAQINDLEDvadKAISNddpeeIEKKIENIVTKIDKKKNIY 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1995 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKV 2073
Cdd:TIGR01612 1190 DEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKK-KSEHMIKAMEAYIEDlDEIKEKSPEIENEMGI 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2074 LEDQAAQ--------------------HKQAI----------------EEKIGQLKKSSDTELDRQKKIVEETLKQRKVV 2117
Cdd:TIGR01612 1269 EMDIKAEmetfnishdddkdhhiiskkHDENIsdirekslkiiedfseESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2118 EEEIHILKLNFEKA--SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfrKLALEEEKKRKEAEAKVKQIqaaeEEAA 2195
Cdd:TIGR01612 1349 ANIYNILKLNKIKKiiDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD---DINLEECKSKIESTLDDKDI----DECI 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2196 RQHKAAQEEVgrlmkLAEEAKKQKEIAE-KEAEKQVILVqeaAQKCSAAEQKAQNVLVQQnKDSMAQD------KLKEEF 2268
Cdd:TIGR01612 1422 KKIKELKNHI-----LSEESNIDTYFKNaDENNENVLLL---FKNIEMADNKSQHILKIK-KDNATNDhdfninELKEHI 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2269 EKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER--QKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQ 2346
Cdd:TIGR01612 1493 DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKTKKDSEIIIKEIKDAHK----------KFIL 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2347 EADSEMAKYKKLAektlKQKSSVEEELVKV-KVQLDETDKQKSVLDVELKRLK-----QEVSDAIKQKAQVEDELSKVKI 2420
Cdd:TIGR01612 1563 EAEKSEQKIKEIK----KEKFRIEDDAAKNdKSNKAAIDIQLSLENFENKFLKisdikKKINDCLKETESIEKKISSFSI 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2421 QMEDLLKLKLKIEKEN-QELMKKDKDNtKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEK-MLE 2498
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSlQEFLESLKDQ-KKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKeEIE 1717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2499 EKKQAIQEAAKLKAEA------------EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAE 2566
Cdd:TIGR01612 1718 SIKELIEPTIENLISSfntndlegidpnEKLEEYNTEIGDIYEEFIELYNIIAGCLETVS---KEPITYDEIKNTRINAQ 1794
|
730 740 750
....*....|....*....|....*....|....*
gi 1207141740 2567 AEKLKVKvtqlsdaqskaeEEAKKFKKQADEIKIR 2601
Cdd:TIGR01612 1795 NEFLKII------------EIEKKSKSYLDDIEAK 1817
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
719-813 |
6.83e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.93 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 719 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 795
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIeegHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1207141740 796 LQYAKLLTSSKTRLRSLD 813
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2469-2748 |
6.92e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2469 NIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiqEAAKLKAEAEKlQKQKDqAQVEAQKLLEAKKemQQRLDQETEG 2548
Cdd:NF012221 1533 NVVATSESSQQADAVSKHAKQDDAAQNALADKERA--EADRQRLEQEK-QQQLA-AISGSQSQLESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2549 FQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQ-ADEIKIRLQEteKHTSEKHTVVEKLEVQRLQSK 2627
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQE--QLDDAKKISGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2628 QEADGLHKAIADLEkekeklkkeaADLQKQSKEMANVQQEqLQQEKTilqQSFFAEKETLLKKEKAIEEEkkklekqfed 2707
Cdd:NF012221 1682 DNQQKVKDAVAKSE----------AGVAQGEQNQANAEQD-IDDAKA---DAEKRKDDALAKQNEAQQAE---------- 1737
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141740 2708 evKKAEAL--KAEQERQRKLMEEERKKLQSAMDAAIKKQKEAE 2748
Cdd:NF012221 1738 --SDANAAanDAQSRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2253-2599 |
7.24e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.77 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2253 QQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKA----EEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE 2328
Cdd:NF033838 112 EAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAkdqkEEDRRNYPTNTYKTLELEIAESDVEVKKAELE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2329 --KEASRRAEAEAAALKLKQEADSEMAKYKKLaEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2406
Cdd:NF033838 192 lvKEEAKEPRDEEKIKQAKAKVESKKAEATRL-EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2407 QKAQVEDElSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAARLR-QIAESD 2485
Cdd:NF033838 271 GEPATPDK-KENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKV--EEAKKKAKDQKEEDRRNYPTNTYKTLElEIAESD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2486 LAKQRELAEKMLEEKKQAIQEAAKLKAEAEklqkqkdqaqveaqklLEAKKEMQQRLDQ-ETEGFQKSLEAERKrqleiT 2564
Cdd:NF033838 348 VKVKEAELELVKEEAKEPRNEEKIKQAKAK----------------VESKKAEATRLEKiKTDRKKAEEEAKRK-----A 406
|
330 340 350
....*....|....*....|....*....|....*..
gi 1207141740 2565 AEAEKLKVKVTQLSDAQS--KAEEEAKKFKKQADEIK 2599
Cdd:NF033838 407 AEEDKVKEKPAEQPQPAPapQPEKPAPKPEKPAEQPK 443
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1667-1899 |
7.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1667 TAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaLEDLEKFKLQAEEAe 1746
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL--------------QAEIDKLQAEIAEA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1747 rhlkQAELEKQRqiqvvEEVAKKTAATQLESKQVALTARLEES----------------LKNEQVMVIQLQEEAEHLKKQ 1810
Cdd:COG3883 78 ----EAEIEERR-----EELGERARALYRSGGSVSYLDVLLGSesfsdfldrlsalskiADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1811 QAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGN 1890
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
....*....
gi 1207141740 1891 QRKMAEETA 1899
Cdd:COG3883 229 AAAAAAAAA 237
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3576-3609 |
7.69e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.69e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141740 3576 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPE 3609
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| DUF2968 |
pfam11180 |
Protein of unknown function (DUF2968); This family of proteins has no known function. |
2455-2531 |
7.70e-04 |
|
Protein of unknown function (DUF2968); This family of proteins has no known function.
Pssm-ID: 431707 [Multi-domain] Cd Length: 180 Bit Score: 43.52 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2455 AENMKKLAE-EAARLNIEAQEAARLRQIAES---------DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2524
Cdd:pfam11180 88 ARQTAQLADvEIRRAQLEAQKAQTERQIAASearaarlqaDLQVARQQEQQVASRQKQTRQEAAALEAQRQAAQAQLRAL 167
|
....*..
gi 1207141740 2525 QVEAQKL 2531
Cdd:pfam11180 168 QRQIRQL 174
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2922-2955 |
8.15e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 8.15e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141740 2922 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPE 2955
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2379-2612 |
8.20e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2379 QLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKL------LE 2452
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkeeRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2453 EEAENMKKLAEEAARLNIEAQEAARLR-----------------QIAESDLAKQRELAEKM------LEEKKQAIQEAAK 2509
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGgsidklrkeierlewrqQTEVLSPEEEKELVEKIkelekeLEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2510 LKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2589
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE-ADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|...
gi 1207141740 2590 KFKKQADEIKIRLQETEKHTSEK 2612
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKE 263
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2346-2550 |
8.43e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2346 QEADSEMAKYKK---------LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA--QVEDE 2414
Cdd:COG3206 192 EEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2415 LSKVKIQMedllklklkiekenQELMKKDKDNT---KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQre 2491
Cdd:COG3206 272 LAELEAEL--------------AELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ-- 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2492 laekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQ 2550
Cdd:COG3206 336 -----LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
230-327 |
8.86e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 42.65 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 230 QKKTFTKWVN---------KHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 296
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1207141740 297 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 327
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1915-2084 |
9.16e-04 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 45.69 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1915 DFEHAEQQRTVLDDELQRL---------KNDVNSAVKQKKELEEELIkvrkemeillqQKSKAEKetmsnTEKSKQLLES 1985
Cdd:pfam04147 126 DDDSEEEEDGQLDLKRVRRahfgggeddEEEEPERKKSKKEVMEEVI-----------AKSKLHK-----YERQKAKEED 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1986 EAakMRE-----LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE--KILKEkLTAINEAT---RLKTEAEIALKEKE- 2054
Cdd:pfam04147 190 EE--LREeldkeLKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLVRE-LAFDKRAKpsdRTKTEEELAEEEKEr 266
|
170 180 190
....*....|....*....|....*....|....
gi 1207141740 2055 ---AENDRLKR-KAEEEGYQRKvlEDQAAQHKQA 2084
Cdd:pfam04147 267 lekLEEERLRRmRGEEDEEEED--GKKKKKHKSA 298
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2355-2570 |
9.47e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2355 YKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiek 2434
Cdd:PRK09510 64 YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA--------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2435 enQELMKKDKDNTKKLLEEEAenmKKLAEEAARlnieAQEAARLRQIAESDlAKQRELAEKMLEEKKQAiQEAAKLKAEA 2514
Cdd:PRK09510 135 --EEAAAKAAAAAKAKAEAEA---KRAAAAAKK----AAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAA-KAAAEAKKKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2515 EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2570
Cdd:PRK09510 204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2449-2679 |
9.87e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 44.43 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2449 KLLEEEAENMKKLAEEaarlniEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ-KQKDQAQVE 2527
Cdd:pfam17045 38 DIREEELLSARNTLER------KHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQrKQLKEAREE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2528 AQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLeitaeaekLKVKVTQLsDAQSKA-EEEAKKFKKQADEIKI--RLQE 2604
Cdd:pfam17045 112 AKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQ--------YQQQVASL-EAQRKAlAEQSSLIQSAAYQVQLegRKQC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2605 TEKHTSEKHTVVEKLEVQR---LQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKeMANVQQEQLQQEKTILQQS 2679
Cdd:pfam17045 183 LEASQSEIQRLRSKLERAQdslCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELR-MSQRQLQVLQNELMELKAT 259
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1674-1965 |
9.90e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1674 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1753
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1754 LEKQRQIQVVEEVAKKTAATQLESKQVALTAR----LEESLKNEQVMVIQLQ----EEAEHLKKQQAEADKAREQA---- 1821
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekEEEREEDERILEYLKEkaerEEEREAEREEIEEEKEREIArlra 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1822 EKELETWRQKANEALRLRLQAEE---EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1898
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEqerKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 1899 AKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1965
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1793-1959 |
1.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1793 EQVMVIQLQE---EAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKtaaqeeAEKQKEEAKREAKK 1869
Cdd:COG1579 5 DLRALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1870 RAKAEEAA-LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELE 1948
Cdd:COG1579 79 EEQLGNVRnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|.
gi 1207141740 1949 EELIKVRKEME 1959
Cdd:COG1579 159 EELEAEREELA 169
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1807-2126 |
1.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1807 LKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1886
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1887 ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS 1966
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1967 KAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 2046
Cdd:COG4372 168 ALEQE---LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2047 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL 2126
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3613-3649 |
1.22e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141740 3613 KLLSAEKAVTGYKDPYTGNKISLLQAMQKQLVLREHA 3649
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1495-1845 |
1.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1495 SPLKKA--KMESASD------DIIQEYVTLRTRYSELMTLSSQYIK---FIIETQRRLQDEEK--------AAEKLKEEE 1555
Cdd:PRK04863 226 SGVRKAfqDMEAALRenrmtlEAIRVTQSDRDLFKHLITESTNYVAadyMRHANERRVHLEEAlelrrelyTSRRQLAAE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1556 RKKMAEMQAELEKQK--------------------QLAETHAKAIAKAEQEANELKTKMKD--EVSKRQDVAVD-SEKQK 1612
Cdd:PRK04863 306 QYRLVEMARELAELNeaesdleqdyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEqnEVVEEADEQQEeNEARA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1613 HNIQRELQELKT--------LSEQEIKA-KSQQVEEAL-----------LSRTRIEEEIHIIRLQLEttmkqknTAETEL 1672
Cdd:PRK04863 386 EAAEEEVDELKSqladyqqaLDVQQTRAiQYQQAVQALerakqlcglpdLTADNAEDWLEEFQAKEQ-------EATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1673 LQLRAKAVDADKLRNAAQEEAEKLRKQVAE--ETQKKRKAEEELK--RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERH 1748
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVRKIAGEvsRSEAWDVARELLRrlREQRHLAEQLQQLRMRLSELEQRLRQQQRAERL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1749 LKQAElekQRQIQVVEevakktAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHlkkQQAEADKAREQAEKELETW 1828
Cdd:PRK04863 539 LAEFC---KRLGKNLD------DEDELEQLQEELEARL-ESLSESVSEARERRMALRQ---QLEQLQARIQRLAARAPAW 605
|
410
....*....|....*...
gi 1207141740 1829 RQkANEAL-RLRLQAEEE 1845
Cdd:PRK04863 606 LA-AQDALaRLREQSGEE 622
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1688-2017 |
1.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1688 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1767
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1768 KktAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAN 1847
Cdd:COG4372 122 K--ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1848 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLD 1927
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1928 DELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA 2007
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
330
....*....|
gi 1207141740 2008 KKQRQIAEEE 2017
Cdd:COG4372 360 SKGAEAGVAD 369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1865-2121 |
1.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1865 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1944
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1945 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA---AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQ 2021
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdleQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2022 RAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELD 2101
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260
....*....|....*....|
gi 1207141740 2102 RQKKIVEETLKQRKVVEEEI 2121
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEE 262
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
283-327 |
1.37e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1207141740 283 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 327
Cdd:cd21294 78 FQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
225-333 |
1.40e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.90 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 225 ERDRVQKKTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 295
Cdd:cd21330 9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141740 296 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1690-1905 |
1.41e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1690 QEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhLKQAELEKQRQIQVVE----- 1764
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAK-AKAAALAKQKREGTEEvteee 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1765 -EVAKKTAATQLESKQVALTArleeslkneqvmviQLQEEAEHLKKQQAEADKAREQAEKeletwRQKANEALRLRLQAE 1843
Cdd:PRK07735 90 kAKAKAKAAAAAKAKAAALAK--------------QKREGTEEVTEEEKAAAKAKAAAAA-----KAKAAALAKQKREGT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 1844 EEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1905
Cdd:PRK07735 151 EEV-----TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKA 207
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
223-331 |
1.50e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.90 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 223 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 298
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 1207141740 299 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 331
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1341-1936 |
1.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1341 ATFDRLEEELQRATE---VNKRMSQLHSERDVELEHYRQLVGnLRERWQAVFAQielrqRELDLLNRQMQAYRESYDWLI 1417
Cdd:COG4913 235 DDLERAHEALEDAREqieLLEPIRELAERYAAARERLAELEY-LRAALRLWFAQ-----RRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1418 RWIADAKQRQDKLHAVpiggSKGLQEQLTQ-----EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVT----YKA 1488
Cdd:COG4913 309 AELERLEARLDALREE----LDELEAQIRGnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1489 LVEPIASplKKAKMESASDDIIQEYVTLRTRYSELMtlssqyikfiiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK 1568
Cdd:COG4913 385 LRAEAAA--LLEALEEELEALEEALAEAEAALRDLR-----------RELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1569 QKQLAETHAKAIA-----KAEQEA---------NELKTKM------KDEVSKrqdvAVDSEKQKHNIQ-------RELQE 1621
Cdd:COG4913 452 ALGLDEAELPFVGelievRPEEERwrgaiervlGGFALTLlvppehYAAALR----WVNRLHLRGRLVyervrtgLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1622 LKTLSEQ----EIKAKSQQVEEALlsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAV-----DADKLR------ 1686
Cdd:COG4913 528 RPRLDPDslagKLDFKPHPFRAWL--EAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGNGTrhekdDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1687 --NAAQEEAekLRKQVAEETQKKRKAEEELKrkseaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQvVE 1764
Cdd:COG4913 606 fdNRAKLAA--LEAELAELEEELAEAEERLE-----------------------ALEAELDALQERREALQRLAEYS-WD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1765 EVAKKTAATQLESKQVALtarleESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEE 1844
Cdd:COG4913 660 EIDVASAEREIAELEAEL-----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1845 EANKKTAAQEEAEKQkeeakrEAKKRAKAEEAALKQKEAAEmELGNQRKMAEETAKQklaAEQELIRLRADF------EH 1918
Cdd:COG4913 735 RLEAAEDLARLELRA------LLEERFAAALGDAVERELRE-NLEERIDALRARLNR---AEEELERAMRAFnrewpaET 804
|
650 660
....*....|....*....|...
gi 1207141740 1919 AEQQRTVLD-----DELQRLKND 1936
Cdd:COG4913 805 ADLDADLESlpeylALLDRLEED 827
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
232-324 |
1.58e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.93 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 232 KTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLKHRQV 301
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 1207141740 302 KLVNIRNDDIADGNpKLTLGLIW 324
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
1865-2075 |
1.70e-03 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.09 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1865 REAKKRAKAEEAALkQKEAAemelgNQRKMAEETAKQKLAAEQE---------LIRLRADFEHAEQQRTVLD-------- 1927
Cdd:NF033875 66 SETPKTAVSEEATV-QKDTT-----SQPTKVEEVASEKNGAEQSsatpndttnAQQPTVGAEKSAQEQPVVSpettnepl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1928 ---DELQRLKNDVNSAVKQKKELE-----EELIKVRKEMEILLQQKSKaekETMSNTEkSKQLleseAAKMRElaeeatk 1999
Cdd:NF033875 140 gqpTEVAPAENEANKSTSIPKEFEtpdvdKAVDEAKKDPNITVVEKPA---EDLGNVS-SKDL----AAKEKE------- 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2000 lrsVAEEAKKQRQIAEEEAARQRAEAEKILKEKltaineatrlkteAEIALKEkeaendrlkrKAEEEGYQRKVLE 2075
Cdd:NF033875 205 ---VDQLQKEQAKKIAQQAAELKAKNEKIAKEN-------------AEIAAKN----------KAEKERYEKEVAE 254
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2367-2607 |
2.01e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2367 SSVEEELVKVKVQLDETDKQKSVLDVEL-KRLKQEVSDAIKQKAQVEDELSKVkiqMEDLLKLKLKIEKENQELMKKdkd 2445
Cdd:COG5185 206 SIKESETGNLGSESTLLEKAKEIINIEEaLKGFQDPESELEDLAQTSDKLEKL---VEQNTDLRLEKLGENAESSKR--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2446 ntkklLEEEAENMKKLAEEAARLNIEAQEAARLRQ-IAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2523
Cdd:COG5185 280 -----LNENANNLIKQFENTKEKIAEYTKSIDIKKaTESLEEQLAAAEAEQELEESKRETETGiQNLTAEIEQGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2524 AQVEAQKLLEAKKEMQQ--RLDQETEGFQKSLEAERKRQLEITAEAEK-LKVKVTQLSDAQSKAEEEAKKFKKQADEIKI 2600
Cdd:COG5185 355 NLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGyAQEILATLEDTLKAADRQIEELQRQIEQATS 434
|
....*..
gi 1207141740 2601 RLQETEK 2607
Cdd:COG5185 435 SNEEVSK 441
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4189-4220 |
2.08e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.08e-03
10 20 30
....*....|....*....|....*....|..
gi 1207141740 4189 KLLSAERAVTGYKDPYSGKVISLFQAMKKGLI 4220
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1548-1784 |
2.14e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1548 AEKLKEEERKKMAEMQAELEK-QKQLAETHAKaIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKT-L 1625
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAaQAELDALQAE-LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1626 SEQEIKAKSQQVEEALLSRTRIEEEIHiiRLQLETTMKQKNTAETELLQLRAKAVDADKlrNAAQEEAEKLRKQVAEETQ 1705
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLD--RLSALSKIADADADLLEELKADKAELEAKK--AELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 1706 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTA 1784
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2262-2570 |
2.15e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2262 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAA 2341
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2342 LKLKQEADSEMAKYKKLAEKTLKQKSSVEEelvkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ 2421
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDE-------FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2422 MEDLLKLKLKIEKENQELMKKDKDN-----TKKLLEEEAENMKKLAEEAARLNIEAQEA---ARLRQIAESDLAKQRElA 2493
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAErdelrAKLYQEEQERKERQKEREEAEKKARQRQElqqAREEQIELKERRLAEE-A 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2494 EKMLEEKKQAIQEAAKL----KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET-EGFQKSLEAERKRQLEITAEAE 2568
Cdd:pfam13868 257 EREEEEFERMLRKQAEDeeieQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEElEEGERLREEEAERRERIEEERQ 336
|
..
gi 1207141740 2569 KL 2570
Cdd:pfam13868 337 KK 338
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1804-2028 |
2.23e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1804 AEHLKKQQAEADKAREQAEKELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEeAALKQKEA 1883
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR-AELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1884 AEMELGNQRKMAEETAKQkLAAEQELIRLRADFEHAEQQRTVL-------DDELQRLKNDVNSAVKQ-KKELEEELIKVR 1955
Cdd:COG3206 241 RLAALRAQLGSGPDALPE-LLQSPVIQQLRAQLAELEAELAELsarytpnHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141740 1956 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI 2028
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1983-2113 |
2.24e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1983 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAarqRAEAEKILKEkltAINEATRLKTEaeiALKEKEAENDRLKR 2062
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2063 KAEEEGYQ-----RKVLEDQAAQHKQAIEEKIgqLKKSSDTelDRQKKIVEETLKQ 2113
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKI--LGKELDA--AAQAALVDRFIAE 151
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1896-2026 |
2.28e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1896 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsN 1975
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE---R 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141740 1976 TEKSKQLLEsEAAKMRELAEEAT------KLRSVAEEAKKQR----QIAEEEAARQRAEAE 2026
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETrilidqQLRKAGWEADSKTlrfsKGARPEKGRNLAIAE 274
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3286-3322 |
2.43e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141740 3286 KLLSAERAVCGYKDPYTGKTVSLFEAMQKDLIKKEQG 3322
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
230-327 |
2.47e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 40.97 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 230 QKKTFTKWVNKHLVK---------AQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 295
Cdd:cd21293 2 EKGSYVDHINRYLGDdpflkqflpIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1207141740 296 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 327
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1322-1848 |
2.51e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1322 IEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLrERWQAVFAQIELRQRELDL 1401
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNL-EKKQKKFDQMLAEEKAISA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1402 lnrqmqAYRESYDwliRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK-NKDKVEDCQKFAKGYIDAIKDYE 1480
Cdd:pfam01576 619 ------RYAEERD---RAEAEAREKETRALS--------LARALEEALEAKEELERtNKQLRAEMEDLVSSKDDVGKNVH 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1481 lQLVTYKALVEPIASPLkKAKMESASDDI-IQEYVTLRTRYSeLMTLSSQYikfiietQRRLQDEEKAAEKLKEEERKKM 1559
Cdd:pfam01576 682 -ELERSKRALEQQVEEM-KTQLEELEDELqATEDAKLRLEVN-MQALKAQF-------ERDLQARDEQGEEKRRQLVKQV 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1560 AEMQAELE---KQKQLAETHAKaiaKAEQEANELKTKMkDEVSKRQDVAVDSEK----QKHNIQRELQELKtLSEQEIKA 1632
Cdd:pfam01576 752 RELEAELEderKQRAQAVAAKK---KLELDLKELEAQI-DAANKGREEAVKQLKklqaQMKDLQRELEEAR-ASRDEILA 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1633 KSQQVEEALLSrtrIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVA---EETQKKRK 1709
Cdd:pfam01576 827 QSKESEKKLKN---LEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAqleEELEEEQS 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1710 AEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK---KTAATQLESKQVALTARL 1786
Cdd:pfam01576 904 NTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKskfKSSIAALEAKIAQLEEQL 983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1787 EESLKNEQVMVIQLQEEAEHLKK-------QQAEADKAREQAEKELETWRQkaneaLRLRL-QAEEEANK 1848
Cdd:pfam01576 984 EQESRERQAANKLVRRTEKKLKEvllqvedERRHADQYKDQAEKGNSRMKQ-----LKRQLeEAEEEASR 1048
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1908-2056 |
2.53e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.28 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1908 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAE----KETMSNTEKSKQLL 1983
Cdd:pfam05911 682 ENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAEtqlkCMAESYEDLETRLT 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1984 ESEaAKMRELAEEATKLRSVAEEakkQRQIAEEEAAR--------QRAEAEKILKEklTAINEATRLKTEAEI-ALKEKE 2054
Cdd:pfam05911 762 ELE-AELNELRQKFEALEVELEE---EKNCHEELEAKclelqeqlERNEKKESSNC--DADQEDKKLQQEKEItAASEKL 835
|
..
gi 1207141740 2055 AE 2056
Cdd:pfam05911 836 AE 837
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2359-2676 |
2.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2359 AEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenQE 2438
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA-----------QE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2439 LMKKDKDNTKKLLEEeaenMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2518
Cdd:COG4372 102 ELESLQEEAEELQEE----LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2519 KQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEI 2598
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2599 KIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2676
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1937-2474 |
2.59e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.18 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1937 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA---KKQRQI 2013
Cdd:COG5185 3 QRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQndvKKSESS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2014 AEEEAARQRA-EAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 2089
Cdd:COG5185 83 VKARKFLKEKkLDTKILQEYVNSLIKLPNYEWSADILislLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2090 GQLKKSSDTELDRQKK--IVEETLKQRKVVEEEihiLKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2167
Cdd:COG5185 163 DIFGKLTQELNQNLKKleIFGLTLGLLKGISEL---KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2168 KLALEEEKKRKEA---EAKVKQIQAAEEEAARQH----KAAQEEVGRLMKLAEEAKKQkeIAEKEAEKQVILVQEAAQKC 2240
Cdd:COG5185 240 DPESELEDLAQTSdklEKLVEQNTDLRLEKLGENaessKRLNENANNLIKQFENTKEK--IAEYTKSIDIKKATESLEEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2241 SAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedA 2320
Cdd:COG5185 318 LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEE------------------L 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2321 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEK-------TLKQKSSVEEELVKVKVQLDE--TDKQKSVLD 2391
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRqieelqrQIEQATSSNEEVSKLLNELISelNKVMREADE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2392 VELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIE 2471
Cdd:COG5185 460 ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
...
gi 1207141740 2472 AQE 2474
Cdd:COG5185 540 ALE 542
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4114-4152 |
2.66e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.66e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 4114 YLEGISSIAGVFVEATKDRLSVYQAMKKTMIRPGTAFEL 4152
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2448-2595 |
2.70e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2448 KKLLEEEAENMKKLAEEAARLNIEAQEAAR---LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2524
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2525 QVEAQKLLEAKKEMQQRLDQETEGFQK--SLEAERKRQ-----LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2595
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKlllklLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
2517-2599 |
2.77e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 42.60 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2517 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgfQKSLEAERKRQLeiTAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2596
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDD--EKQELLAEYRAL--KAELESLEVYNRQLERLVASQEQEIASLERQIE 86
|
...
gi 1207141740 2597 EIK 2599
Cdd:pfam11932 87 EIE 89
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1865-2301 |
2.79e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1865 REAKKRAKAEEAALKQKEAAEMElgnQRKMAEETAKQKLAAEQELIRLRADFEHAEQQrtvlddelqrlkndvnsAVKQK 1944
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEE-----------------AREAK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1945 KELEEELIKVRKEMEillQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE----EEAAR 2020
Cdd:COG3064 62 AEAEQRAAELAAEAA---KKLAEAEKAA----AEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAkrkaEEEAK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2021 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTEL 2100
Cdd:COG3064 135 RKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2101 DRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEA 2180
Cdd:COG3064 215 ALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2181 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMA 2260
Cdd:COG3064 295 LVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGA 374
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1207141740 2261 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2301
Cdd:COG3064 375 LLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAA 415
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2368-2606 |
2.95e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2368 SVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklKIEKENQELMKKDKDnt 2447
Cdd:PRK01156 194 SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-------MKNRYESEIKTAESD-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2448 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2527
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141740 2528 AQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2606
Cdd:PRK01156 345 KSRYDDLNNQILE-LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2448-2597 |
3.41e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2448 KKLLEEEAENMKKLAE---EAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2523
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLE-AKEEIHKLRNEFEKELRERRNELQKLeKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2524 AQVEAQKLLEAKKEMQQRLDQ--ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2597
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQEleKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1539-1849 |
3.44e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1539 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEAN---ELKTKMKDEVSKRQDVAVDSEKQKHNI 1615
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrqELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1616 QRELQELKTLSEQEIKAKSQQVEEALlsrtriEEEIHIIRLQLEttMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEK 1695
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLR------EEIDEFNEEQAE--WKELEKEEEREEDERILEYLKEKAEREEEREAER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1696 LRKQVAEETQKKRKAEEELKRKseaekdaakeKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQL 1775
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQ----------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141740 1776 ESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELE-TWRQKANEALRLRLQAEEEANKK 1849
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEkQIEEREEQRAAEREEELEEGERL 320
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1940-2066 |
3.48e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.29 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1940 AVKQKKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 2019
Cdd:pfam20492 4 AEREKQELEERLKQYEEETK-------KAQEELEESEETAEELEE----ERRQAEEEAERLEQKRQEAEEEKERLEESAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141740 2020 RQRAEAEKILKEKLTAINEATRLKTEAEialkEKEAENDRLKRKAEE 2066
Cdd:pfam20492 73 MEAEEKEQLEAELAEAQEEIARLEEEVE----RKEEEARRLQEELEE 115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4468-4498 |
3.50e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.08 E-value: 3.50e-03
10 20 30
....*....|....*....|....*....|.
gi 1207141740 4468 AGILDTDTLEKVSVTEAMHRNLVDNITGQRL 4498
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2357-2687 |
3.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2357 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkieken 2436
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2437 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEK 2516
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2517 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2596
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2597 EIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2676
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
330
....*....|.
gi 1207141740 2677 QQSFFAEKETL 2687
Cdd:COG4372 312 ALEDALLAALL 322
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2451-2597 |
3.78e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.43 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2451 LEEEAENMKKLAEEAARLNIEAQE--AARLRQIAESDLAKQ-RELAEKMLEEKKQAIQ----EAAKLKAEAEKLQKQKDQ 2523
Cdd:PRK07735 37 LEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAALAKQkREGTEEVTEEEKAKAKakaaAAAKAKAAALAKQKREGT 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2524 AQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2597
Cdd:PRK07735 117 EEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGE 190
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1217-1640 |
3.88e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1217 TQRATEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ 1296
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1297 GAE-DILNKYENQLREVNKVPVNEKEIEASQ----TQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVEL 1371
Cdd:pfam05483 436 GKEqELIFLLQAREKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1372 EHYRQLVGNLRERWQAVFAQIE-LRQRELDLLNrQMQAYRESY----DWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLT 1446
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIEnLEEKEMNLRD-ELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1447 QEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMEsasddiIQEYVTLRTRYSELMTL 1526
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK------FEEIIDNYQKEIEDKKI 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1527 SSQYIKFIIETQRRLQDEE-KAAEKLKEEERKKMAEMQAELEKQKQlaeTHAKAIAKAEQEANELKTKMKDEVSKRqdva 1605
Cdd:pfam05483 669 SEEKLLEEVEKAKAIADEAvKLQKEIDKRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAK---- 741
|
410 420 430
....*....|....*....|....*....|....*
gi 1207141740 1606 VDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEA 1640
Cdd:pfam05483 742 AALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1988-2131 |
4.02e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1988 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEE 2067
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2068 GYQRKVLEDQAAQHKQAIEE------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKA 2131
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2565-2774 |
4.07e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2565 AEAEKLKVKVtqlsdAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEK 2644
Cdd:PRK09510 75 KRAEEQRKKK-----EQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2645 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKEtllkkekaieeekkkLEKQFEDEVKKaealKAEQERQRK 2724
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAE---------------AAAKAAAEAKK----KAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2725 LMEEERKKlqSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE 2774
Cdd:PRK09510 211 AAAEAKKK--AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2451-2786 |
4.20e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2451 LEEEAENMKKLAEE----AARLNIeAQEAARLR-QI--AESDLAkqrELAEKmLEEKKQAIQEAAKLKAEAEKlqkQKDQ 2523
Cdd:PRK04863 316 LAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER-LEEQNEVVEEADEQQEENEA---RAEA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2524 AQveaQKLLEAKKEM---QQRLD-QETEG--FQKSLEA-ERKRQL----------------EITAEAEKLKVKV----TQ 2576
Cdd:PRK04863 388 AE---EEVDELKSQLadyQQALDvQQTRAiqYQQAVQAlERAKQLcglpdltadnaedwleEFQAKEQEATEELlsleQK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2577 LSDAQSKAEEEAKKFK---KQADEI-KIRLQETEKHTSEKHTVvEKLEVQRLQSKQEAdglHKAIADLEKEKEKLKKEAA 2652
Cdd:PRK04863 465 LSVAQAAHSQFEQAYQlvrKIAGEVsRSEAWDVARELLRRLRE-QRHLAEQLQQLRMR---LSELEQRLRQQQRAERLLA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2653 DLQKQSKEMANVQQ--EQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME--- 2727
Cdd:PRK04863 541 EFCKRLGKNLDDEDelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsg 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 2728 ---EERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLAEENKNLrEKLQQL 2786
Cdd:PRK04863 621 eefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI---ERLSQPGGSED-PRLNAL 678
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1607-1818 |
4.42e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1607 DSEKQKHNIQRElqelktlSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdADKlr 1686
Cdd:COG2268 200 DARIAEAEAERE-------TEIAIAQANREAEEA---ELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEA-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1687 nAAQEEAEKLRKQVAEETQKKRKAEE-ELKRKseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQRQIQVVE- 1764
Cdd:COG2268 267 -AYEIAEANAEREVQRQLEIAEREREiELQEK------------------EAEREEAELEADVRKPAEAEKQAAEAEAEa 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141740 1765 --EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-LQEEAEHLKKQQAEADKAR 1818
Cdd:COG2268 328 eaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEkLPEIAEAAAKPLEKIDKIT 384
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
2449-2571 |
4.56e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.17 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2449 KLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdLAKQrelAEKMLEEKKQAIQEAAKLKAEA-----EKLQKQKDQ 2523
Cdd:PRK00290 499 GLSDEEIERMVKDAEANAEEDKKRKELVEARNQADS-LIYQ---TEKTLKELGDKVPADEKEKIEAaikelKEALKGEDK 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2524 AQVEA--QKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLK 2571
Cdd:PRK00290 575 EAIKAktEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDDVVDAEFEEVK 624
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2462-2606 |
4.61e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2462 AEEAARLNIEAQEAARLRQIAESDLAKQRELAEKML--EEKKQAIQEAAKLKAEAEKL-QKQKDQAQVEAQKLLEAKKEM 2538
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLEKEEEERLRkeELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEER 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141740 2539 QQRLDQETEGFQKSLEAERKRQLEitaEAEKLKVKVTQLsdaQSKAEEEAKKFKKQADEIKIRLQETE 2606
Cdd:pfam05672 89 EQREQEEQERLQKQKEEAEAKARE---EAERQRQEREKI---MQQEEQERLERKKRIEEIMKRTRKSD 150
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1684-1849 |
4.67e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1684 KLRNAAQEEAEKLRKQVAEETQK-----KRKAEEELKrkseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQR 1758
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKeaeaiKKEALLEAK--------------------EEIHKLRNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1759 Q----IQVVEEVAKKTAAtqLESKQVALTARlEESLKNEQVMVIQLQEEAEHLKKQQAE---------ADKAR----EQA 1821
Cdd:PRK12704 87 LekrlLQKEENLDRKLEL--LEKREEELEKK-EKELEQKQQELEKKEEELEELIEEQLQelerisgltAEEAKeillEKV 163
|
170 180
....*....|....*....|....*...
gi 1207141740 1822 EKELETwrQKANEALRLRLQAEEEANKK 1849
Cdd:PRK12704 164 EEEARH--EAAVLIKEIEEEAKEEADKK 189
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2196-2300 |
4.85e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.31 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2196 RQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLA 2275
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREA-------QQNYERELVLHAEDIKALQALREELNELKAEI 73
|
90 100
....*....|....*....|....*
gi 1207141740 2276 QEAEKAKDNAEKEAALLHKKAEEAE 2300
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQK 98
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1912-2299 |
4.94e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1912 LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMR 1991
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1992 ELAEEATKLrSVAEEAKKQRqIAEEEAARQRAEAEKILKEkltaiNEATRLKTEAEIA---LKEKEAENDRLKRKAEEEG 2068
Cdd:pfam07888 112 ELSEEKDAL-LAQRAAHEAR-IRELEEDIKTLTQRVLERE-----TELERMKERAKKAgaqRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2069 YQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIveeTLKQRKVVEEEIHILKLNF--EKASSGKQELELELKKLK 2146
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL---TTAHRKEAENEALLEELRSlqERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2147 GIAdeTQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE---------EVGRLMKLAEEAKK 2217
Cdd:pfam07888 262 SMA--AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrieklsaELQRLEERLQEERM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2218 QKEIAEKE--AEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKlKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK 2295
Cdd:pfam07888 340 EREKLEVElgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK-QELLEYIRQLEQRLETVADAKWSEAALTSTE 418
|
....
gi 1207141740 2296 AEEA 2299
Cdd:pfam07888 419 RPDS 422
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1751-2068 |
4.99e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.30 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1751 QAELEKQRQiQVVEevAKKTAATQLESKQVALTARLEESLKNE---QVMVIQLQEEAEHLKKQQAEADKAREQAEKELET 1827
Cdd:PLN03229 435 EGEVEKLKE-QILK--AKESSSKPSELALNEMIEKLKKEIDLEyteAVIAMGLQERLENLREEFSKANSQDQLMHPVLME 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1828 WRQKANEALRLRL-QAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR-KMA---EETAKQK 1902
Cdd:PLN03229 512 KIEKLKDEFNKRLsRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKeKMEalkAEVASSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1903 LAAEQELirlradfehaeqqrtvlDDELqrlkndVNSAVKQKKELEEELIKVRKEME---ILLQQKSKAEKETMSNTEKS 1979
Cdd:PLN03229 592 ASSGDEL-----------------DDDL------KEKVEKMKKEIELELAGVLKSMGlevIGVTKKNKDTAEQTPPPNLQ 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1980 KQL--LESEAAKMRELAEEATKLRSVAEEAKKqrQIAEEEAARQRAEAEKI------LKEKLTAINEATRLKT-----EA 2046
Cdd:PLN03229 649 EKIesLNEEINKKIERVIRSSDLKSKIELLKL--EVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSELKEkfeelEA 726
|
330 340
....*....|....*....|....
gi 1207141740 2047 EIALKEK--EAENDRLKRKAEEEG 2068
Cdd:PLN03229 727 ELAAAREtaAESNGSLKNDDDKEE 750
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2441-2587 |
5.31e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2441 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQ---EAAKLKAEAEKL 2517
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141740 2518 QKQKDQA---QVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2587
Cdd:COG1579 102 KRRISDLedeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1675-1833 |
5.52e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1675 LRAKAVDADKLRNAAQEEAEK------LRKQVAEETQK---KRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA 1745
Cdd:pfam13904 61 LAAKQRQRQKELQAQKEEREKeeqeaeLRKRLAKEKYQewlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1746 ERHLKQAELEKQRQIQvveevAKKtaatqleskqvaltarleeslkneqvmviqlQEEAEHLKKQQAEADKAREQAEKEL 1825
Cdd:pfam13904 141 KEVLQEWERKKLEQQQ-----RKR-------------------------------EEEQREQLKKEEEEQERKQLAEKAW 184
|
....*...
gi 1207141740 1826 ETWRQKAN 1833
Cdd:pfam13904 185 QKWMKNVK 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1983-2225 |
6.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1983 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTeAEIALKEKEAENDRLK 2061
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2062 RKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekassgkqelele 2141
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---------------- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2142 lkklkgiadetqkskakaeeeaEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEI 2221
Cdd:COG4913 366 ----------------------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
....
gi 1207141740 2222 AEKE 2225
Cdd:COG4913 424 LEAE 427
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
2437-2544 |
6.45e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 40.06 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2437 QELMKKDKDNTKKLLEEEAEnmkkLAEEAARLNIEAQEAARlrQIAESDLAKQRELAEKMLEEKKQAIqeAAKLKAEAEK 2516
Cdd:PRK08476 40 NASIKNDLEKVKTNSSDVSE----IEHEIETILKNAREEAN--KIRQKAIAKAKEEAEKKIEAKKAEL--ESKYEAFAKQ 111
|
90 100
....*....|....*....|....*....
gi 1207141740 2517 LQKQKDQAQVEAQ-KLLEAKKEMQQRLDQ 2544
Cdd:PRK08476 112 LANQKQELKEQLLsQMPEFKEALNAKLSK 140
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1563-1823 |
6.47e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1563 QAELEKQKQlaethAKAiAKAEQEANELKTKMKDEVSKrqdvAVDSEKQKHNIQRELQELKTLSEQEIKA-KSQQVEEAL 1641
Cdd:PRK05035 459 QARLEREKA-----ARE-ARHKKAAEARAAKDKDAVAA----ALARVKAKKAAATQPIVIKAGARPDNSAvIAAREARKA 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1642 LSRTRIEEEihiirlqlettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKlrKQVAEETQKKRKAEEEL---KRKS 1718
Cdd:PRK05035 529 QARARQAEK-------------QAAAAADPKKAAVAAAIARAKAKKAAQQAANA--EAEEEVDPKKAAVAAAIaraKAKK 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1719 EAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAtqleskqVALTARLEESLKNEQVMVI 1798
Cdd:PRK05035 594 AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-------VAAAIARAKARKAAQQQAN 666
|
250 260
....*....|....*....|....*
gi 1207141740 1799 QLQEEAEHLKKQQAEADKAREQAEK 1823
Cdd:PRK05035 667 AEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2704-2775 |
6.64e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 6.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2704 QFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMN--GKQKEMQDLEKKRIEQEKLLAEE 2775
Cdd:pfam20492 17 QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKErlEESAEMEAEEKEQLEAELAEAQE 90
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1980-2094 |
6.74e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1980 KQLLESEAAKMRELA----EEATKlrsVAEEAKKQRQI-AEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 2054
Cdd:PRK12704 26 KKIAEAKIKEAEEEAkrilEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141740 2055 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKK 2094
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1734-1950 |
6.84e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1734 DLEKFKLQAEEAERHLKQAE-----LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1808
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKkeekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1809 KQQAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAkaeEAALKQKEAAEMEL 1888
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAEL---EAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141740 1889 GNQRKmaeETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1950
Cdd:COG4942 184 EEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
828-908 |
6.99e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.22 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 828 WLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTAALQTQWSWILQL 907
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 1207141740 908 C 908
Cdd:pfam00435 96 A 96
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4152-4186 |
7.03e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 7.03e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141740 4152 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEF 4186
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2184-2598 |
7.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2184 VKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE-----KEAEKQVILVQEAAQKCSAAEQ---KAQNVLVQQN 2255
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAelaELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2256 KDSMAQDklKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaAEAEAAKQAKAQEDAEKLRKEAEKEASRRA 2335
Cdd:COG4717 184 EQLSLAT--EEELQDLAEELEELQQRLAELEEELEEAQEELEELEE----ELEQLENELEAAALEERLKEARLLLLIAAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2336 EAEAAALKLKQEADSEM----------------AKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQ 2399
Cdd:COG4717 258 LLALLGLGGSLLSLILTiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2400 EVSDAIKQKAQVEDELSkvKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNiEAQEaaRLR 2479
Cdd:COG4717 338 ELLELLDRIEELQELLR--EAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE-ELEE--QLE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2480 QIAESDLAKQRELAEKMLEEKKQAIQEAAKLkAEAEKLQKQKDQAQVEAQ-KLLEAKKEMQQRLDQetegfQKSLEAERK 2558
Cdd:COG4717 413 ELLGELEELLEALDEEELEEELEELEEELEE-LEEELEELREELAELEAElEQLEEDGELAELLQE-----LEELKAELR 486
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1207141740 2559 RQLEitaEAEKLKVKVTQLSDAQSKAEEE-AKKFKKQADEI 2598
Cdd:COG4717 487 ELAE---EWAALKLALELLEEAREEYREErLPPVLERASEY 524
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2706-2788 |
7.38e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.67 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2706 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEE----MNGKQKEM--QDLEK--KRIEQeklLAEEN- 2776
Cdd:pfam13779 495 QERLSEALERGASDEEIAKLMQELREALDDYMQALAEQAQQNPQDlqqpDDPNAQEMtqQDLQRmlDRIEE---LARSGr 571
|
90
....*....|...
gi 1207141740 2777 -KNLREKLQQLQS 2788
Cdd:pfam13779 572 rAEAQQMLSQLQQ 584
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1932-2049 |
7.57e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1932 RLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 2011
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141740 2012 qiaeEEAARQRAEAEKILKEKLTAINEATRLK----TEAEIA 2049
Cdd:COG0542 481 ----EQRYGKIPELEKELAELEEELAELAPLLreevTEEDIA 518
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
2489-2605 |
7.94e-03 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 40.33 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2489 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKR-QLEITAEA 2567
Cdd:pfam16535 37 QQQKGLELSDEFQTALSEAEEATDAYEKAINKLKNAKSKAKAAEKKIDQAQTRLQSLAPDSPGKAKLEAAEqQAGIKKDA 116
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141740 2568 EKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQET 2605
Cdd:pfam16535 117 LQADRTLDKALDAASKLTTKAMAKEKEADDFSAKFQGT 154
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1750-2089 |
8.00e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1750 KQAELEKQRQIQVVEEVAKKTAATQLESKQV-ALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETW 1828
Cdd:COG5022 822 LQKTIKREKKLRETEEVEFSLKAEVLIQKFGrSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVN 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1829 RQKANEALRLRLQAEEEANKKTAaqeeaekqkeeakreakkrakaeeaaLKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1908
Cdd:COG5022 902 LELESEIIELKKSLSSDLIENLE--------------------------FKTELIARLKKLLNNIDLEEGPSIEYVKLPE 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1909 LIRLRadfehaeQQRTVLDDELQRLKNdvnsAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESE-- 1986
Cdd:COG5022 956 LNKLH-------EVESKLKETSEEYED----LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPve 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1987 ----AAKMRELAEEATKLRSVAEEaKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKR 2062
Cdd:COG5022 1025 vaelQSASKIISSESTELSILKPL-QKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340
....*....|....*....|....*..
gi 1207141740 2063 KAEEEGYQRKVLEDQAAQHKQAIEEKI 2089
Cdd:COG5022 1104 TNRNLVKPANVLQFIVAQMIKLNLLQE 1130
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
1016-1050 |
8.03e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 37.63 E-value: 8.03e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141740 1016 EITVHKGDECALVNNSQPYkWKVRDSSGNEAVVPS 1050
Cdd:cd11764 15 ELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
2448-2519 |
8.13e-03 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 40.81 E-value: 8.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141740 2448 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESD--LAKQRELAEKMLEEKKQAiqeAAKLKAEAEKLQK 2519
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQdrRAEELEELKHLLEERKEA---LEKLRAEAREEAE 71
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2485-2768 |
8.60e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2485 DLAKQRELAEKMLEEKK----QAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLdqetegfqKSLEAERKrq 2560
Cdd:COG1340 12 ELEEKIEELREEIEELKekrdELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV--------KELKEERD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2561 lEITAEAEKLKVKVTQL---SDAQSKAEEEAKKFKKQADEIKIRlQETEKHTSEKH-TVVEKLEV--QRLQSKQEADGLH 2634
Cdd:COG1340 82 -ELNEKLNELREELDELrkeLAELNKAGGSIDKLRKEIERLEWR-QQTEVLSPEEEkELVEKIKEleKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 2635 KAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQ--SFFAEKETLlkkekaieeekkklEKQFEDEVKKA 2712
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEadELRKEADEL--------------HKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141740 2713 EALKAEQERqrklMEEERKKLQSAMDAAIKKQKEAEEEmngKQKEMQDLEKKRIEQ 2768
Cdd:COG1340 226 DELHEEIIE----LQKELRELRKELKKLRKKQRALKRE---KEKEELEEKAEEIFE 274
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1808-1961 |
8.61e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1808 KKQQAEADK---AREQAEK-ELEtwRQK-----ANEALR---LRLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEE 1875
Cdd:PTZ00491 662 KSQEAAARHqaeLLEQEARgRLE--RQKmhdkaKAEEQRtklLELQAESAAVESSG--------------QSRAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1876 AALKQKEAAEMELGNQRkmaeeTAKQKLAAEQELIRLRadfehaeqQRTVLDDELQRLKNDVnsAVKQKKELEE-ELIKV 1954
Cdd:PTZ00491 726 EARLIEAEAEVEQAELR-----AKALRIEAEAELEKLR--------KRQELELEYEQAQNEL--EIAKAKELADiEATKF 790
|
....*..
gi 1207141740 1955 RKEMEIL 1961
Cdd:PTZ00491 791 ERIVEAL 797
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
223-334 |
9.08e-03 |
|
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409187 Cd Length: 130 Bit Score: 39.57 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 223 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 298
Cdd:cd21338 15 APDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQD 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 1207141740 299 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 334
Cdd:cd21338 95 GGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1930-2066 |
9.21e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.60 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1930 LQRLKNDVNSAVKQKKELEEELikvrKEMEillQQKSKAEKETMSNTEKSKQL------LESEAAKMRELAEEATKLRSV 2003
Cdd:pfam12718 2 MNSLKLEAENAQERAEELEEKV----KELE---QENLEKEQEIKSLTHKNQQLeeevekLEEQLKEAKEKAEESEKLKTN 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141740 2004 AEEAKKQRQIAEEEAarqrAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE 2066
Cdd:pfam12718 75 NENLTRKIQLLEEEL----EESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEE 133
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1808-1905 |
9.31e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.14 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1808 KKQQAEADKAREQAEKELETWRQKANEalrLRLQAEEEANKKtaaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEME 1887
Cdd:PRK05759 48 ERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQI----------------IEEAKAEAEAEAARIKAQAQAE 108
|
90
....*....|....*...
gi 1207141740 1888 LGNQRKMAEETAKQKLAA 1905
Cdd:PRK05759 109 IEQERKRAREELRKQVAD 126
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1688-1923 |
9.33e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1688 AAQEEAEKLRKQVaEETQKKRKAEEELKRKseaekdAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1767
Cdd:COG4942 17 AQADAAAEAEAEL-EQLQQEIAELEKELAA------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1768 KKTAA--TQLESKQVALTARLEESLKNEQ---VMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQA 1842
Cdd:COG4942 90 KEIAElrAELEAQKEELAELLRALYRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141740 1843 EEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ 1922
Cdd:COG4942 170 EAERAEL-----------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 1207141740 1923 R 1923
Cdd:COG4942 239 A 239
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3538-3576 |
9.75e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.75e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141740 3538 YLQGSDCIAGVFFQKTKEKLSIYQAMKQKLLTSDTGMSL 3576
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| |
