|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
7-272 |
2.32e-92 |
|
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.
Pssm-ID: 400137 Cd Length: 272 Bit Score: 294.59 E-value: 2.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 7 TVSVNKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 85
Cdd:pfam07651 3 EVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 86 ELSDMSRMWGH-LSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELNL 164
Cdd:pfam07651 83 RISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 165 FQTVFNSLDMSRSVSVTTaGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKDL 238
Cdd:pfam07651 161 QKLLFRLLKCRPTGNALS-NECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKEF 239
|
250 260 270
....*....|....*....|....*....|....
gi 1845865226 239 FQRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 272
Cdd:pfam07651 240 YEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
772-970 |
5.36e-91 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 288.11 E-value: 5.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 772 GVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLV 851
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 852 VQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQ-IEETDSMDFSSMT 930
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1845865226 931 LTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELA 970
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
6-119 |
1.55e-83 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.
Pssm-ID: 340810 Cd Length: 114 Bit Score: 264.59 E-value: 1.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 6 MTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 85
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1845865226 86 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
6-119 |
1.84e-68 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.
Pssm-ID: 340803 Cd Length: 114 Bit Score: 223.70 E-value: 1.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 6 MTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 85
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 1845865226 86 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd17006 81 RLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
822-968 |
8.54e-59 |
|
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.
Pssm-ID: 460265 [Multi-domain] Cd Length: 149 Bit Score: 198.19 E-value: 8.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 822 KNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVN 901
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845865226 902 QATAAVVASTISGKSQIEE--TDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYE 968
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
8-119 |
3.93e-55 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.
Pssm-ID: 340811 Cd Length: 114 Bit Score: 186.61 E-value: 3.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 8 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNEL 87
Cdd:cd17014 3 ISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRSNI 82
|
90 100 110
....*....|....*....|....*....|..
gi 1845865226 88 SDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd17014 83 RETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
6-119 |
1.11e-41 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.
Pssm-ID: 340783 Cd Length: 117 Bit Score: 148.30 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 6 MTVSVNKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAMLCWKFCHVFHKLLRDGHP--NVLKDSLR 82
Cdd:cd16986 1 FEKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLD 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1845865226 83 -YKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd16986 80 aWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
6-126 |
3.25e-36 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 133.14 E-value: 3.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 6 MTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAM--LCWKFCHVFHKLLRDGHPNVLKDSLRY 83
Cdd:smart00273 3 LEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNwrVVYKALILLHYLLRNGSPRVILEALRN 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1845865226 84 KNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTRMEYHTKNPRFP 126
Cdd:smart00273 83 RNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
448-538 |
8.51e-28 |
|
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.
Pssm-ID: 465154 [Multi-domain] Cd Length: 99 Bit Score: 108.17 E-value: 8.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 448 HADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFAR--------TQEQQDVLENLKHELATSRQELQVLHSNLETSAQ 519
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERakeeaqmkLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 1845865226 520 SEAKWLTQIAELEKEQGSL 538
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
6-119 |
3.33e-25 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.
Pssm-ID: 340804 Cd Length: 115 Bit Score: 101.23 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 6 MTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 85
Cdd:cd17007 1 LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1845865226 86 ELSDMSRMW-GHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd17007 81 WLESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-602 |
2.07e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 348 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAmddcEFLRTEL----DELKRQREDTEKAQRSLTEI 423
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELeeleLELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 424 ERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATS 503
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 504 RQELQVLHSNLETSAQSEAKwltQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLA 583
Cdd:COG1196 381 LEELAEELLEALRAAAELAA---QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250
....*....|....*....
gi 1845865226 584 giRKAAEREIQEALSQLEE 602
Cdd:COG1196 458 --EEALLELLAELLEEAAL 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-597 |
1.15e-12 |
|
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: 72.40 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 335 NKDEKDHLIERLYREISGLTGQLDNMKIESQramlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREdte 414
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE--- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 415 KAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSvarqaqvDLEREKKELADSFARTQEQqdvLE 494
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA-------ATERRLEDLEEQIEELSED---IE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 495 NLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQV 574
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL-EGL 934
|
250 260
....*....|....*....|...
gi 1845865226 575 KDQRKTLLAGIRKAAEREIQEAL 597
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAE 957
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
399-602 |
3.00e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 399 LRTELDELKRQREDTEKAqRSLTEIERKAQAN---------EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQ 469
Cdd:COG1196 198 LERQLEPLERQAEKAERY-RELKEELKELEAEllllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 470 VDLEREKKELADSFARTQEQqdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEEL 549
Cdd:COG1196 277 EELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1845865226 550 SALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgiRKAAEREIQEALSQLEE 602
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEE 404
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-603 |
2.77e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 337 DEKDHLIERLYREISGLTgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK- 415
Cdd:COG1196 281 LELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAe 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 416 ---AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDV 492
Cdd:COG1196 360 laeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 493 LENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQ 572
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
250 260 270
....*....|....*....|....*....|.
gi 1845865226 573 QVKDQRKTLLAGIRKAAEREIQEALSQLEEP 603
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-602 |
1.35e-10 |
|
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: 65.46 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 368 MLQLKGRVSELEAELAEQQhlgrqamDDCEFLRTELDELKRQRED----TEKAQRSLTEIERKAQANEQRYSKLKEKYSE 443
Cdd:TIGR02168 672 ILERRREIEELEEKIEELE-------EKIAELEKALAELRKELEEleeeLEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 444 LVQNHADLLRKNAEVTKQVSV-------ARQAQVDLEREKKELADSFARTQEQ-----------QDVLENLKHELATSRQ 505
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEEleerleeAEEELAEAEAEIEELEAQIEQLKEElkalrealdelRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 506 ELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGI 585
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-ALLRSELEELSEEL 903
|
250
....*....|....*..
gi 1845865226 586 RKaAEREIQEALSQLEE 602
Cdd:TIGR02168 904 RE-LESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
343-630 |
2.29e-10 |
|
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: 65.08 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 343 IERLYREISGLTGQLDNMKIESQRA--MLQLKGRVSELEAELAeqqhlgrqaMDDCEFLRTELDELKRQREdteKAQRSL 420
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAerYKELKAELRELELALL---------VLRLEELREELEELQEELK---EAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 421 TEIERKAQANEqrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENlkhEL 500
Cdd:TIGR02168 256 EELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA---QL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 501 ATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQ-----QVK 575
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnneiERL 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1845865226 576 DQRKTLLAGIRKAAEREIQEALSQLEEPTLISCAGSTDHLLSKVSSVSSCLEQLE 630
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-600 |
2.33e-10 |
|
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: 63.63 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 363 ESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAqrsLTEIERKAQANEQRYSKLKEKYS 442
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 443 ELVQNHADLLRKnaevtkQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEA 522
Cdd:COG4942 101 AQKEELAELLRA------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845865226 523 KWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQEALSQL 600
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
343-602 |
2.56e-10 |
|
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: 64.69 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 343 IERLYREISGLTGQLDNMKIESQRamlqLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK----AQR 418
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 419 SLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKH 498
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 499 ELATSRQELQvlhsnlETSAQSEAkwltQIAELEKEQGSLATVAAQREEEL---SALRDQLESTQIKLAGAQESMCQQVK 575
Cdd:TIGR02168 835 ATERRLEDLE------EQIEELSE----DIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELR 904
|
250 260
....*....|....*....|....*..
gi 1845865226 576 DQRKTllagiRKAAEREIQEALSQLEE 602
Cdd:TIGR02168 905 ELESK-----RSELRRELEELREKLAQ 926
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
409-602 |
1.15e-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: 61.32 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 409 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQE 488
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 489 QqdvLENLKHELATSRQELQ----------VLHSNLETSAQSEAKWLTQIAELEKEQG-----SLATVAAQReEELSALR 553
Cdd:COG4942 98 E---LEAQKEELAELLRALYrlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAeelraDLAELAALR-AELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1845865226 554 DQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKaAEREIQEALSQLEE 602
Cdd:COG4942 174 AELEALLAELEEERAAL-EALKAERQKLLARLEK-ELAELAAELAELQQ 220
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
336-600 |
7.10e-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: 60.08 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 336 KDEKDHLIE--RLYREISGLTGQLDNMKIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQRED 412
Cdd:TIGR02169 204 RREREKAERyqALLKEKREYEGYELLKEKEALERQKeAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 413 T-------------------EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQV----------- 462
Cdd:TIGR02169 284 LgeeeqlrvkekigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRdklteeyaelk 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 463 SVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVA 542
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1845865226 543 AQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRKAAEREIQEALSQL 600
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR--VEKELSKLQRELAEAEAQA 499
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
8-117 |
1.11e-08 |
|
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.
Pssm-ID: 340767 Cd Length: 120 Bit Score: 54.20 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 8 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 84
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 1845865226 85 NELSDMSRmW--GHLSEGYGQ--LCSIYLKLLRTRME 117
Cdd:cd03564 83 GHIFNLSN-FkdDSSPEAWDLsaFIRRYARYLEERLE 118
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
328-565 |
1.53e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 58.49 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 328 FNNQNGVNKDekdhLIERLYREISGLTGQLDNMK---------IESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEF 398
Cdd:PHA02562 165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQqqiktynknIEEQRK--KNGENIARKQNKYDELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 399 LRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYselvqnhadllRKNAEV---TKQVSVARQAQVDLERE 475
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY-----------EKGGVCptcTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 476 KKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQ 555
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250
....*....|
gi 1845865226 556 LESTQIKLAG 565
Cdd:PHA02562 388 LDKIVKTKSE 397
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
337-539 |
4.57e-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: 56.31 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 337 DEKDHLIERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQ------- 409
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 410 ---------------REDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLER 474
Cdd:COG4942 113 lyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845865226 475 EKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwLTQIAELEKEQGSLA 539
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLP 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
390-602 |
5.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 390 RQAMDDCEFLRTELDELKRQREDTEKAQR---SLTEIERKAQaneqRYSKLKEKYSELvqnhaDLLRKNAevtkQVSVAR 466
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAEL-----EYLRAAL----RLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 467 QAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSaqseakwltQIAELEKEQGSLATVAAQRE 546
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD---------RLEQLEREIERLERELEERE 358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1845865226 547 EELSALRDQLESTQIKLAGAQESMCQQVK--DQRKTLLAGIRKAAEREIQEALSQLEE 602
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAeaAALLEALEEELEALEEALAEAEAALRD 416
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-602 |
7.85e-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: 56.60 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 414 EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVL 493
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 494 E----NLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ-- 567
Cdd:TIGR02168 746 EeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRer 825
|
170 180 190
....*....|....*....|....*....|....*...
gi 1845865226 568 -ESMCQQVKDQRKTL--LAGIRKAAEREIQEALSQLEE 602
Cdd:TIGR02168 826 lESLERRIAATERRLedLEEQIEELSEDIESLAAEIEE 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-558 |
8.20e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 361 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAmdDCEFLRTELDELKRQREDTEKAQRSLteiERKAQANEQRYSKLKEK 440
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARL---EAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 441 YSELVQNHADLLRKNAEvtkqvsvarQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQS 520
Cdd:COG4913 325 LDELEAQIRGNGGDRLE---------QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190
....*....|....*....|....*....|....*...
gi 1845865226 521 EAKWLtqiAELEKEQGSLATVAAQREEELSALRDQLES 558
Cdd:COG4913 396 LEEEL---EALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
343-602 |
1.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 343 IERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF--LRTELDELKRQREDTEKAQRSL 420
Cdd:COG4913 612 LAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 421 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKK-----ELADSFARTQE---QQDV 492
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGdavEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 493 LENLKHELATSRQELQVLHSNLEtSAQSEAK--WLTQIAELEkeqgslATVAAqrEEELSALRDQLEstQIKLAGAQESM 570
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELE-RAMRAFNreWPAETADLD------ADLES--LPEYLALLDRLE--EDGLPEYEERF 836
|
250 260 270
....*....|....*....|....*....|..
gi 1845865226 571 CQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 602
Cdd:COG4913 837 KELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
366-578 |
1.28e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 366 RAMLqlkgrVSELEAELAE----QQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKy 441
Cdd:COG4717 44 RAML-----LERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 442 selvqnhadllRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETS-AQS 520
Cdd:COG4717 118 -----------LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELlEQL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1845865226 521 EAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQR 578
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
388-601 |
1.82e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 388 LGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVqnhaDLLrknaevtkqvSVARQ 467
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI----DVA----------SAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 468 AQvDLEREKKELADSfartqeqQDVLENLKHELATSRQELQVLHSnletsaqseakwltQIAELEKEQGSLATVAAQREE 547
Cdd:COG4913 670 IA-ELEAELERLDAS-------SDDLAALEEQLEELEAELEELEE--------------ELDELKGEIGRLEKELEQAEE 727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1845865226 548 ELSALRDQLESTQIKLAGAQESMCQQVKDQ--RKTLLAGIRKAAEREIQEALSQLE 601
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAalGDAVERELRENLEERIDALRARLN 783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-513 |
2.96e-07 |
|
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: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 336 KDEKDHL--IERLYREISGLTGQLDnmKIESQRAMLQLKG---RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQR 410
Cdd:COG4913 248 REQIELLepIRELAERYAAARERLA--ELEYLRAALRLWFaqrRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 411 EDTEKAQRS-----LTEIERKAQANEQRYSKLKEK---YSELVQN-HADLLRKNAEVTKQVSVARQAQVDLEREKKELAD 481
Cdd:COG4913 326 DELEAQIRGnggdrLEQLEREIERLERELEERERRrarLEALLAAlGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
170 180 190
....*....|....*....|....*....|..
gi 1845865226 482 SFARTQEQqdvLENLKHELATSRQELQVLHSN 513
Cdd:COG4913 406 ALAEAEAA---LRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-602 |
3.80e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 370 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 449
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 450 DLLRKNAEVTKQVSVARQaqvdLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLE--TSAQSEAKWLT- 526
Cdd:PRK03918 270 ELKKEIEELEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKelEEKEERLEELKk 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845865226 527 QIAELEKEQGSLATvAAQREEELSALRDQLESTQIKLAGAQesmcqqvKDQRKTLLAGIRKAAErEIQEALSQLEE 602
Cdd:PRK03918 346 KLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLT-------PEKLEKELEELEKAKE-EIEEEISKITA 412
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
366-589 |
1.39e-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: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 366 RAMLqLKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELKRQRedtekaqrslTEIERKAQANEQRYSKLKEKY 441
Cdd:pfam07888 28 RAEL-LQNRLEECLQERAEllqaQEAANRQREKEKERYKRDREQWERQR----------RELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 442 SELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFA----RTQEQQDVLENLKHE---LATSRQELQVLHSNL 514
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKtltqRVLERETELERMKERakkAGAQRKEEEAERKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 515 ETSAQSEAKWLTQiaeLEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ------ESMCQQVKDQRKTLLAGIRKA 588
Cdd:pfam07888 177 QAKLQQTEEELRS---LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeaenEALLEELRSLQERLNASERKV 253
|
.
gi 1845865226 589 A 589
Cdd:pfam07888 254 E 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
335-602 |
1.58e-06 |
|
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: 52.43 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 335 NKDEKDHLIERLYREISGLTGQLDNMK-----IESQRAMLQLKGR---------VSELEAELAEqqhlgrqamddcefLR 400
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARsqansIQSQLEIIQEQARnqnsmymrqLSDLESTVSQ--------------LR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 401 TELDELKRQREDT-EKAQRSLteIERKAQANEQRYSklKEKYSELVQNHADLLRK-NAEVTKqvsvaRQAQVDLEREK-K 477
Cdd:pfam15921 331 SELREAKRMYEDKiEELEKQL--VLANSELTEARTE--RDQFSQESGNLDDQLQKlLADLHK-----REKELSLEKEQnK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 478 ELADsfaRTQEQQDVLENLKHELATSRQELQVLHSNLET-SAQSEAKWLTQIAELEKEQGSLatvaaqreEELSALRDQL 556
Cdd:pfam15921 402 RLWD---RDTGNSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESL--------EKVSSLTAQL 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1845865226 557 ESTQIKLagaqESMCQQVKDQRKTLlagirKAAEREIQEALSQLEE 602
Cdd:pfam15921 471 ESTKEML----RKVVEELTAKKMTL-----ESSERTVSDLTASLQE 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
370-560 |
5.03e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 370 QLKGRVSELEAELAE--QQHLGRQAMDDCEFLRTELDELKRQredtekaqrsLTEIERKAQANEQRYSKLKEKYSELVQN 447
Cdd:COG3206 186 ELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQ----------LAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 448 HADLLRknaevTKQVSVARQAQVDLEREKKELAdsfARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWL-T 526
Cdd:COG3206 256 LPELLQ-----SPVIQQLRAQLAELEAELAELS---ARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALqA 327
|
170 180 190
....*....|....*....|....*....|....*..
gi 1845865226 527 QIAELEKEQGSL---ATVAAQREEELSALRDQLESTQ 560
Cdd:COG3206 328 REASLQAQLAQLearLAELPELEAELRRLEREVEVAR 364
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
339-601 |
5.05e-06 |
|
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: 50.89 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 339 KDHLIERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEA----ELAEQQHLG------RQAMDDCEFLRTELDE--- 405
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSrvdlKLQELQHLKnegdhlRNVQTECEALKLQMAEkdk 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 406 ----LKRQRED----------------TEKAQRSLTEIERKAQANEQRYSKLKE--KYSELVQNHADLLRKNAEVTKQVS 463
Cdd:pfam15921 563 vieiLRQQIENmtqlvgqhgrtagamqVEKAQLEKEINDRRLELQEFKILKDKKdaKIRELEARVSDLELEKVKLVNAGS 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 464 VARQAQVDLEREKKELADSFARTQEQQDVL----ENLKHELATSRQELQVLHSNLET---SAQSEAKWL-TQIAELEKEQ 535
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLsedyEVLKRNFRNKSEEMETTTNKLKMqlkSAQSELEQTrNTLKSMEGSD 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 536 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQ-------------------RKTLLAG---IRKAAEREI 593
Cdd:pfam15921 723 GHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhflkeeknklsqelstvatEKNKMAGeleVLRSQERRL 802
|
....*...
gi 1845865226 594 QEALSQLE 601
Cdd:pfam15921 803 KEKVANME 810
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
329-604 |
5.58e-06 |
|
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: 50.34 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 329 NNQNGVNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKR 408
Cdd:COG5185 140 VEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 409 QREDTEKAQRSLTEIERKAQANEQRYSKLK---EKYSELVQNHADL----LRKNAEVTKQVSVARQAQVDLEREKKELAD 481
Cdd:COG5185 220 TLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLEKLVEQNTDLrlekLGENAESSKRLNENANNLIKQFENTKEKIA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 482 SFARTQEQQDVLENLKHELATSRQELQVLHSNLETsaqsEAKWLTQIAELEKEQGSLATV----------------AAQR 545
Cdd:COG5185 300 EYTKSIDIKKATESLEEQLAAAEAEQELEESKRET----ETGIQNLTAEIEQGQESLTENleaikeeienivgeveLSKS 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1845865226 546 EEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEEPT 604
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL-KAADRQIEELQRQIEQAT 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-559 |
7.02e-06 |
|
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: 50.06 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 337 DEKDHLIERLYREISGLTGQLDNMKIE--SQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDT 413
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEElkALREALDeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 414 EKAQRSLT-EIERKAQANEQRYSKLKEKYSEL--VQNHADLLRKNAE-VTKQVSVARQAQVDLEREKKELADSFARTQEQ 489
Cdd:TIGR02168 851 SEDIESLAaEIEELEELIEELESELEALLNERasLEEALALLRSELEeLSEELRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 490 QDVLEN--------LKHELATSRQELQVLHSNLETS---AQSEAKWLTQ------------IAELEKEQGSLATVAAQRE 546
Cdd:TIGR02168 931 LEGLEVridnlqerLSEEYSLTLEEAEALENKIEDDeeeARRRLKRLENkikelgpvnlaaIEEYEELKERYDFLTAQKE 1010
|
250
....*....|...
gi 1845865226 547 EELSAlRDQLEST 559
Cdd:TIGR02168 1011 DLTEA-KETLEEA 1022
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
370-601 |
7.79e-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: 50.17 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 370 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQAN---------------EQRY 434
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQmkdlqreleearasrDEIL 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 435 SKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNL 514
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNT 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 515 ETSAQSEAKWLTQIAELEKEQGSLATVAAQREeelsALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgirkAAEREIQ 594
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQLTTELAAERSTSQKSE----SARQQLERQNKELKAKLQEMEGTVKSKFKSSIA----ALEAKIA 977
|
....*..
gi 1845865226 595 EALSQLE 601
Cdd:pfam01576 978 QLEEQLE 984
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
377-556 |
8.31e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 377 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 456
Cdd:PRK04863 500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 457 EVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKH----ELATSR---QELQVLHSNLETSAQSEAKWLTQIA 529
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeEFEDSQdvtEYMQQLLERERELTVERDELAARKQ 655
|
170 180
....*....|....*....|....*..
gi 1845865226 530 ELEKEQGSLATVAAQREEELSALRDQL 556
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAERF 682
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
330-602 |
1.09e-05 |
|
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: 49.35 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 330 NQNGVNKDEKDHLIERLYREisgltgqldNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELD---EL 406
Cdd:pfam17380 280 HQKAVSERQQQEKFEKMEQE---------RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErerEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 407 KRQREDTEKaqRSLTEIERKAQANEQrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF--- 483
Cdd:pfam17380 351 ERIRQEERK--RELERIRQEEIAMEI------SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKvem 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 484 ---------ARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR----EEELS 550
Cdd:pfam17380 423 eqiraeqeeARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkilEKELE 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845865226 551 A--------------LRDQLESTQIKLA-------GAQESMCQQVKDQRKTLLAGIRKAA-EREIQEALSQLEE 602
Cdd:pfam17380 503 ErkqamieeerkrklLEKEMEERQKAIYeeerrreAEEERRKQQEMEERRRIQEQMRKATeERSRLEAMERERE 576
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
343-602 |
1.09e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 343 IERLYREISGLTGQLDNmKIESQRAMlQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQRedtEKAQRSLTE 422
Cdd:PRK02224 178 VERVLSDQRGSLDQLKA-QIEEKEEK-DLHERLNGLESELAE--------------LDEEIERYEEQR---EQARETRDE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 423 IERKAQANEQR---YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFART-------QEQQDV 492
Cdd:PRK02224 239 ADEVLEEHEERreeLETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeavEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 493 LEN----LKHELATSRQELQVLHSNLETSA------QSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQI 561
Cdd:PRK02224 319 LEDrdeeLRDRLEECRVAAQAHNEEAESLRedaddlEERAEELrEEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1845865226 562 KLAGAQE-------------SMCQQVKDQRKTLLAGIRKAAEReIQEALSQLEE 602
Cdd:PRK02224 399 RFGDAPVdlgnaedfleelrEERDELREREAELEATLRTARER-VEEAEALLEA 451
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
377-556 |
1.16e-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: 49.57 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 377 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 456
Cdd:COG3096 499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 457 EVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELA---TSRQEL----QVLHSNLETSAQSEAKWLTQIA 529
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGealADSQEVtaamQQLLEREREATVERDELAARKQ 654
|
170 180
....*....|....*....|....*..
gi 1845865226 530 ELEKEQGSLATVAAQREEELSALRDQL 556
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLALAERL 681
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
353-530 |
1.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 353 LTGQLDNMKIESQRAMlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTEL---DELKRQREDTEKAQRSLTeiERKAQA 429
Cdd:PRK04863 501 LLRRLREQRHLAEQLQ-QLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLddeDELEQLQEELEARLESLS--ESVSEA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 430 NEQRysklkekySELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKK----ELADSFARTQEQQDVLENLKH------E 499
Cdd:PRK04863 578 RERR--------MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeEFEDSQDVTEYMQQLLEREREltverdE 649
|
170 180 190
....*....|....*....|....*....|.
gi 1845865226 500 LATSRQELQVLHSNLETSAQSEAKWLTQIAE 530
Cdd:PRK04863 650 LAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
361-602 |
1.37e-05 |
|
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: 49.40 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 361 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKaqaNEQRYSKLKEK 440
Cdd:pfam01576 259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK---REQEVTELKKA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 441 YSELVQNH----ADLLRKNA----EVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSR----QELQ 508
Cdd:pfam01576 336 LEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRkkleGQLQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 509 VLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQRE-------EELSALRDQL--------ESTQIKLAGAqeSMCQQ 573
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniklsKDVSSLESQLqdtqellqEETRQKLNLS--TRLRQ 493
|
250 260 270
....*....|....*....|....*....|....*
gi 1845865226 574 VKDQRKTLLAGI------RKAAEREIQEALSQLEE 602
Cdd:pfam01576 494 LEDERNSLQEQLeeeeeaKRNVERQLSTLQAQLSD 528
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-516 |
1.38e-05 |
|
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: 49.30 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 334 VNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQamddcefLRTELDELKR 408
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienLNGKKEELEEELEELEAALRD-------LESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 409 QREDTEK----AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA---DLLRKNAEVTKQVSVARQAQVDLEREKKELA- 480
Cdd:TIGR02169 890 ERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRa 969
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1845865226 481 ---------DSFARTQEQQDVLENLKHELATSRQELQVLHSNLET 516
Cdd:TIGR02169 970 lepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
412-562 |
1.51e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.12 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 412 DTEKAQRSLTEIERKAQANEQRYSKLKEkyseLVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFArTQEQqd 491
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEA----ELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAV-SQQE-- 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845865226 492 vLENLKHELATSRQELQVLHSNLEtSAQSEAKWLTQIAELEKEqgslatvAAQREEELSALRDQLESTQIK 562
Cdd:COG1566 150 -LDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQ-------VAQAEAALAQAELNLARTTIR 211
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
329-602 |
1.60e-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: 48.86 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 329 NNQNGVNKDEkdhlIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCE----------F 398
Cdd:TIGR04523 376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 399 LRTELDELKRQREDTEKAQRSLT-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSVARQAQVDLER 474
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 475 EKKELADsfaRTQEQQDVLENLKHELATSRQELQVLHSNLETSaqseaKWLTQIAELEKEQGSLATVAAQREEELSALRD 554
Cdd:TIGR04523 532 EKKEKES---KISDLEDELNKDDFELKKENLEKEIDEKNKEIE-----ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1845865226 555 QLEsTQIKLAGAQESMCQQVKDQRKTLLAGIRKaaereIQEALSQLEE 602
Cdd:TIGR04523 604 EIE-EKEKKISSLEKELEKAKKENEKLSSIIKN-----IKSKKNKLKQ 645
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
374-528 |
1.62e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.55 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 374 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 453
Cdd:PRK12705 37 RILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSA 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845865226 454 KNAEVTkqvsvARQAQVDLEREKKEladSFARTQEQQDVLENLKHELatsRQELQVLHSNLETSAQSEAKWLTQI 528
Cdd:PRK12705 117 RELELE-----ELEKQLDNELYRVA---GLTPEQARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
398-602 |
1.62e-05 |
|
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: 48.91 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 398 FLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADL----------LRKNAEVTKQVSVA-R 466
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqleqeEEKLKERLEELEEDlS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 467 QAQVDLEREKKELADSFARTQEQQDVLENLKHELAT-----SRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATV 541
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845865226 542 AAQREEELSALRDQLESTQIklagaQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEE 602
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEEL-EEELEELEAALRDLES 882
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
404-602 |
1.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 404 DELKRQREDTEKAQrsltEIERKAQANEQRYSKLKEKYSElvQNHADLLRKNAEVTKQVSVARQaqvdlEREKKELADSF 483
Cdd:PTZ00121 1381 DAAKKKAEEKKKAD----EAKKKAEEDKKKADELKKAAAA--KKKADEAKKKAEEKKKADEAKK-----KAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 484 ARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKL 563
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190
....*....|....*....|....*....|....*....
gi 1845865226 564 AGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 602
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
420-605 |
2.47e-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: 46.84 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 420 LTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKhe 499
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 500 latsrqELQVLhsnletsaqseakwLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRK 579
Cdd:COG1579 90 ------EYEAL--------------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL-EEKKAELD 148
|
170 180
....*....|....*....|....*....
gi 1845865226 580 TLLAGIRKAAER---EIQEALSQLEEPTL 605
Cdd:COG1579 149 EELAELEAELEEleaEREELAAKIPPELL 177
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
411-576 |
2.76e-05 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 46.21 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 411 EDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHAD------LLRKNAEVTKQVSVARQAQV---------DLERE 475
Cdd:pfam05010 8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEfektiaQMIEEKQKQKELEHAEIQKVleekdqalaDLNSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 476 KKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE-LEKEQGSLATVAAQREEELSALRD 554
Cdd:pfam05010 88 EKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEkLDQANEEIAQVRSKAKAETAALQA 167
|
170 180
....*....|....*....|..
gi 1845865226 555 QLESTQIKLAGAQESMCQQVKD 576
Cdd:pfam05010 168 SLRKEQMKVQSLERQLEQKTKE 189
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
337-602 |
3.59e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 337 DEKDHLIERLYREISGLTGQLDNmkIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQA------------------- 392
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGN--AEDFLEELReerdeLREREAELEATLRTARERVEEAealleagkcpecgqpvegs 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 393 -----MDDC----EFLRTELDELKRQREDTEKAQRSLTEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS 463
Cdd:PRK02224 465 phvetIEEDrervEELEAELEDLEEEVEEVEERLERAED----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 464 VARQAQVDLE---REKKELADSFA-RTQEQQDVLENLKHELATSRQELQVLhSNLETSAQSEAKWLTQIAELEKEQGSLA 539
Cdd:PRK02224 541 ELRERAAELEaeaEEKREAAAEAEeEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALA 619
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845865226 540 TVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgirkaaerEIQEALSQLEE 602
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--------QVEEKLDELRE 674
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
370-569 |
3.70e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 370 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLT-EIERKAQANEQRYSKLKE--------- 439
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQaEIAEAEAEIEERREELGEraralyrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 440 ---KYSELV---QNHADLLRKNAEVTKQVSVARQAQVDLEREKKELAdsfartqEQQDVLENLKHELATSRQELQVLHSN 513
Cdd:COG3883 100 gsvSYLDVLlgsESFSDFLDRLSALSKIADADADLLEELKADKAELE-------AKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1845865226 514 LEtSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQES 569
Cdd:COG3883 173 LE-AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
346-575 |
3.91e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 346 LYREISGLTGQldnmkIESQRAML-QLKGRVSELeaelaeQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRS----- 419
Cdd:PRK04863 849 LERALADHESQ-----EQQQRSQLeQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 420 --LTEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVSVA-RQA 468
Cdd:PRK04863 918 naLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKLRQRlEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 469 QVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLH-----------SNLETSAQSEAKWL--------TQIA 529
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKqelqdlgvpadSGAEERARARRDELharlsanrSRRN 1077
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1845865226 530 ELEKEQGSLatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVK 575
Cdd:PRK04863 1078 QLEKQLTFC-------EAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
365-602 |
4.30e-05 |
|
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: 47.66 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 365 QRAMLQLKGRVSELEAELAEQQHLGRQamddceflrteldELKRQREDTEKAQRSLTEIERKAQAnEQRYSKLKEKYSEL 444
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTS-------------ERKQRASLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNI 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 445 VQNHADLLRKNAEVTKQVSVARQAQvdlEREKKELADSFARTQEQQDVLENLKHELATSRQELQVL------HSNLETSA 518
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHAL---LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSIRV 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 519 QSEAKWLTQIAELEKEQGSLATVAAQREE---ELSALRDQLEStqIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQE 595
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWKEMlaqCQTLLRELETH--IEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
....*..
gi 1845865226 596 ALSQLEE 602
Cdd:TIGR00618 748 LMHQART 754
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-602 |
4.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 361 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSK-LKE 439
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 440 KYSElvQNHADLLRKNAEVTKQVSVARQAQVDLER---------EKKELADSFARTQEQQDVLENLKHELATSRQELQvl 510
Cdd:PTZ00121 1465 KAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKkadeakkaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-- 1540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 511 hsnlETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE--LSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKA 588
Cdd:PTZ00121 1541 ----KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVM-KLYEEEKKMKAEEAKKA 1615
|
250
....*....|....*
gi 1845865226 589 AEREIQ-EALSQLEE 602
Cdd:PTZ00121 1616 EEAKIKaEELKKAEE 1630
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
397-599 |
4.62e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 397 EFLRTELDELKRQREDTE------KAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQ--------- 461
Cdd:COG3206 178 EFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQlgsgpdalp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 462 -------VSVARQAQVDLEREKKELAdsfARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwltqiaeleke 534
Cdd:COG3206 258 ellqspvIQQLRAQLAELEAELAELS---ARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE----------- 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845865226 535 qgslatVAAQREEELSALRDQLESTQIKLAGAQ---ESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 599
Cdd:COG3206 324 ------ALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-542 |
4.97e-05 |
|
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: 47.37 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 343 IERLYREISGLTGQLDNMKIEsqRAMLQ-----LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQ 417
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKR--RDKLTeeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 418 -RSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsFARTQEQQDVLEnl 496
Cdd:TIGR02169 409 dRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL---YDLKEEYDRVEK-- 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1845865226 497 khELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKE-QGSLATVA 542
Cdd:TIGR02169 484 --ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiQGVHGTVA 528
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
364-530 |
5.93e-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: 47.25 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 364 SQRAMLQ----LKGRVSELEAELAEQQHLGRQAMDDCEFLRTEL---DELKRQREDTEKAQRSLTEierkaQANEQRysk 436
Cdd:COG3096 506 SQQALAQrlqqLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLdaaEELEELLAELEAQLEELEE-----QAAEAV--- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 437 lkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE----LADSFARTQEQQDVLENL------KHELATSRQE 506
Cdd:COG3096 578 --EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQsgeaLADSQEVTAAMQQLLEREreatveRDELAARKQA 655
|
170 180
....*....|....*....|....
gi 1845865226 507 LQVLHSNLETSAQSEAKWLTQIAE 530
Cdd:COG3096 656 LESQIERLSQPGGAEDPRLLALAE 679
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-602 |
5.99e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 342 LIERLYREISGLTGQLDnmKIESQRAML-QLKGRVSELEAELAEQQHLGRqAMDDCEFLRTELDELKrqredTEKAQRSL 420
Cdd:PRK03918 315 RLSRLEEEINGIEERIK--ELEEKEERLeELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLK-----KRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 421 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDL--------EREKKELADSFarTQEQQDV 492
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEY--TAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 493 LENLKhELATSRQELQVLHSNLETSAQSEAKWLT------QIAELEKEQGSLATVAAQREEELSalrDQLESTQIKLAGA 566
Cdd:PRK03918 465 EKELK-EIEEKERKLRKELRELEKVLKKESELIKlkelaeQLKELEEKLKKYNLEELEKKAEEY---EKLKEKLIKLKGE 540
|
250 260 270
....*....|....*....|....*....|....*.
gi 1845865226 567 QESMCQQVKdqRKTLLAGIRKAAEREIQEALSQLEE 602
Cdd:PRK03918 541 IKSLKKELE--KLEELKKKLAELEKKLDELEEELAE 574
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
407-594 |
6.74e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 407 KRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFART 486
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 487 QEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGA 566
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180
....*....|....*....|....*...
gi 1845865226 567 QESMCQQVKDQRKTLLAGIRKAAEREIQ 594
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAE 197
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
391-602 |
9.23e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 391 QAMDDCEFLRTELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEKYSELvQNHADLLRKNAEVTKQVSVARQAQV 470
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 471 dlerekKELADSFARTQEQQDVLENLKheLATSRQEL--QVlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE 548
Cdd:COG3883 89 ------GERARALYRSGGSVSYLDVLL--GSESFSDFldRL--SALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1845865226 549 LSALRDQLESTQIKLAGAQESmcqqvKDQRKTLLAGIRKAAEREIQEALSQLEE 602
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
465-602 |
1.51e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 465 ARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLET-----SAQSE-AKWLTQIAELEKEQGSL 538
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvaSAEREiAELEAELERLDASSDDL 687
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845865226 539 ATVAAQREE---ELSALRDQLESTQIKLAGAQESmcqqvkdqrktllagiRKAAEREIQEALSQLEE 602
Cdd:COG4913 688 AALEEQLEEleaELEELEEELDELKGEIGRLEKE----------------LEQAEEELDELQDRLEA 738
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
366-563 |
1.61e-04 |
|
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: 45.71 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 366 RAMLQLKGRVSEleAELAEQQHlgRQAMddcEFLRTELDELkrQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELV 445
Cdd:COG3096 455 EEVLELEQKLSV--ADAARRQF--EKAY---ELVCKIAGEV--ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 446 Q---NHADLLRKNAEVTKQVSVARQAQVDLEREKKELAdsfARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEA 522
Cdd:COG3096 526 QrlrQQQNAERLLEEFCQRIGQQLDAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAP 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1845865226 523 KWLTQIAELEK--EQG--SLATVAA---------QREEELSALRDQLESTQIKL 563
Cdd:COG3096 603 AWLAAQDALERlrEQSgeALADSQEvtaamqqllEREREATVERDELAARKQAL 656
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
343-444 |
1.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 343 IERLYREISGLTGQLDNmkiESQRAMLQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQREDTEKAQRSLTE 422
Cdd:COG3206 293 VIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREAS--------------LQAQLAQLEARLAELPELEAELRR 355
|
90 100
....*....|....*....|..
gi 1845865226 423 IERKAQANEQRYSKLKEKYSEL 444
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEA 377
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
353-557 |
1.94e-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: 45.60 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 353 LTGQLDNMKIESQRAMLQLKG----RVSELEAELA----EQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQrslteIE 424
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDsaneRLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----LA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 425 RKAQANEQRYSKLKEKYSEL-VQNHADLlrknaevtKQVSVARQAQVDLEREKKELADSFAR-TQEQQDVLE-------- 494
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALeTWYKRDL--------ASLGVDPDVIAKLKREIRTLERKIERiAVRRQEVLRyfdwyqet 804
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845865226 495 ------NLKHELATSRQELQVLHSNLeTSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLE 557
Cdd:pfam12128 805 wlqrrpRLATQLSNIERAISELQQQL-ARLIADTK--LRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
403-599 |
1.99e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 403 LDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNH------ADLLRKNAEVTKQVSvarQAQVDL---- 472
Cdd:PRK11281 72 LDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTLDQLQ---NAQNDLaeyn 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 473 ----------EREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHsNLETSA--------QSEAKWLTQIAELEKE 534
Cdd:PRK11281 149 sqlvslqtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLL-QAEQALlnaqndlqRKSLEGNTQLQDLLQK 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845865226 535 QGSLATVAAQR-EEELSALRD-----QLESTQIKLAGAQESMcQQVKDQRKTLLagirkAAEREIQEALSQ 599
Cdd:PRK11281 228 QRDYLTARIQRlEHQLQLLQEainskRLTLSEKTVQEAQSQD-EAARIQANPLV-----AQELEINLQLSQ 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
483-591 |
2.12e-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: 44.75 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 483 FARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 562
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100
....*....|....*....|....*....
gi 1845865226 563 LAGAQESmcqqvKDQRKTLLAGIRKAAER 591
Cdd:COG4942 92 IAELRAE-----LEAQKEELAELLRALYR 115
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-483 |
2.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 334 VNKDEKDHLIERLYREISGLTGQLD-------NMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMD--DCEFLRTELD 404
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELE 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845865226 405 ELKRQREDTEKAQRSLTEiERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF 483
Cdd:COG4717 436 ELEEELEELEEELEELRE-ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
350-586 |
2.22e-04 |
|
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: 45.49 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 350 ISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQA 429
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 430 NEQRYSKLKekySELVQNHADLLRKNAEVTKQvsvarQAQVDLE-REKKELADSFARTQEQQDVLENLKHELATSRQELQ 508
Cdd:pfam15921 494 SERTVSDLT---ASLQEKERAIEATNAEITKL-----RSRVDLKlQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 509 VLHSNLETSAQ-------SEAKWLTQIAELEKEQGS----------LATVAAQREEELSALRDQLESTQIKLAGAQESMC 571
Cdd:pfam15921 566 ILRQQIENMTQlvgqhgrTAGAMQVEKAQLEKEINDrrlelqefkiLKDKKDAKIRELEARVSDLELEKVKLVNAGSERL 645
|
250
....*....|....*...
gi 1845865226 572 QQVKD---QRKTLLAGIR 586
Cdd:pfam15921 646 RAVKDikqERDQLLNEVK 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
337-601 |
2.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 337 DEKDHLIERLYREISgltgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGR------------------------QA 392
Cdd:PRK03918 448 EHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaeqlkeleeklkkynleeleKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 393 MDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKQVSVARQAQVDL 472
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVEELEERLKELEPF 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 473 EREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLEtsaqsEAKwlTQIAELEKEQGslatvaaqrEEELSAL 552
Cdd:PRK03918 601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-----ELR--KELEELEKKYS---------EEEYEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1845865226 553 RDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAER--EIQEALSQLE 601
Cdd:PRK03918 665 REEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEEleEREKAKKELE 714
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
347-557 |
2.76e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 347 YREISGLTGQLDNMKIESQRAMLQL---KGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEi 423
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKE- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 424 erkaqanEQRYskLKEKYSELVqnhADLLRKNAEVTKQVSVARQAQVDL---------------EREKKELADSF-ARTQ 487
Cdd:pfam00038 132 -------ELAF--LKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLtsalaeiraqyeeiaAKNREEAEEWYqSKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 488 EQQ-------DVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEkEQGSLATVAAQR-----EEELSALRDQ 555
Cdd:pfam00038 200 ELQqaaarngDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETE-ERYELQLADYQEliselEAELQETRQE 278
|
..
gi 1845865226 556 LE 557
Cdd:pfam00038 279 MA 280
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
399-601 |
3.23e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 399 LRTELDELKRQREDTEKAQRSLTEIERKAQANEQRY-----SKLKEKyselvqnhaDLLRKNAEVTKQVSVARQAqvdlE 473
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKEIERLEWRQqtevlSPEEEK---------ELVEKIKELEKELEKAKKA----L 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 474 REKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLetsaqseAKWLTQIAELEKEQGSLATVAAQREEELSALR 553
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM-------IELYKEADELRKEADELHKEIVEAQEKADELH 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1845865226 554 DQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLE 601
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
399-516 |
4.45e-04 |
|
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: 41.09 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 399 LRTELDELKRQREDTEKAQRSLTEiERKAQAneQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLERE--- 475
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQE-DLEKQA--EIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAEaes 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1845865226 476 -KKELADSFARTQEQQDVLENLKHELATSRQELQ----VLHSNLET 516
Cdd:pfam07926 83 aKAELEESEESWEEQKKELEKELSELEKRIEDLNeqnkLLHDQLES 128
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-602 |
5.23e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 361 KIESQRAMLQLKgRVSELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYS-KLKE 439
Cdd:PTZ00121 1559 KAEEKKKAEEAK-KAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeEEKK 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 440 KYSELVQNHADLLRKNAEVTK--QVSVARQAQV--DLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLE 515
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKaeEENKIKAAEEakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 516 TSAQSEakwltQIAELEKEQGSLATVAAQREEElsalrDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQE 595
Cdd:PTZ00121 1714 EKKKAE-----ELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
....*..
gi 1845865226 596 ALSQLEE 602
Cdd:PTZ00121 1784 ELDEEDE 1790
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
360-508 |
6.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 360 MKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQR-EDTEKAQ--RSLTEIERKAQANEQRYSK 436
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAeEDKKKAEeaKKAEEDEKKAAEALKKEAE 1699
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845865226 437 LKEKYSELVQNHADLLRKNAEVTKQVSV----ARQAQVDLEREKKElADSFARTQEQQDVLENLKHELATSRQELQ 508
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKK-AEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
368-590 |
7.30e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 368 MLQLKGRVSELEAELAEQQHLGRQAMDdceflrtELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEkyselvqn 447
Cdd:PRK10929 111 ILQVSSQLLEKSRQAQQEQDRAREISD-------SLSQLPQQQTE---ARRQLNEIERRLQTLGTPNTPLAQ-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 448 hADLLRKNAEvtkqvSVARQAQVDlEREKKELadSFARTQEqqdvLENLKHELATSRQE-----LQVLHSNLETSAQSEA 522
Cdd:PRK10929 173 -AQLTALQAE-----SAALKALVD-ELELAQL--SANNRQE----LARLRSELAKKRSQqldayLQALRNQLNSQRQREA 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845865226 523 -KWLTQIAELEKEQGSLATVAA---QREEELSALRDQlESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE 590
Cdd:PRK10929 240 eRALESTELLAEQSGDLPKSIVaqfKINRELSQALNQ-QAQRMDLIASQQRQAASQTLQVRQALNTLREQSQ 310
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
361-556 |
7.90e-04 |
|
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: 42.22 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 361 KIESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQredtekaqrsLTEIERKAQANEQRYSKLKEK 440
Cdd:COG1579 14 ELDSELD--RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----------IKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 441 YSElVQNHADLlrknAEVTKQVSVARQAQVDLEREKKELADsfaRTQEQQDVLENLKHELATSRQELQVLHSNLEtsaqs 520
Cdd:COG1579 82 LGN-VRNNKEY----EALQKEIESLKRRISDLEDEILELME---RIEELEEELAELEAELAELEAELEEKKAELD----- 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1845865226 521 eakwlTQIAELEKEqgsLATVAAQREEELSALRDQL 556
Cdd:COG1579 149 -----EELAELEAE---LEELEAEREELAAKIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
405-602 |
8.33e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 405 ELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFA 484
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 485 RTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLA 564
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
170 180 190
....*....|....*....|....*....|....*...
gi 1845865226 565 gaqESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 602
Cdd:PTZ00121 1447 ---DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
336-602 |
8.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 336 KDEKDHLIERLYREISGLTGQLDnmKIESQRAMLQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQREDTEK 415
Cdd:COG4717 97 LEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAE--------------LPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 416 AQRSLTEIERKAQANEQRYSKLKEKYS--------ELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQ 487
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 488 EQQDVLENL-----------------------------------------------KHELATSRQELQVLHSNLETSAQS 520
Cdd:COG4717 241 LEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 521 EAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAgaqesmCQQVKDQRKTLLAGIRKAAEREIQEALSQL 600
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ------LEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
..
gi 1845865226 601 EE 602
Cdd:COG4717 395 EE 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
372-602 |
1.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 372 KGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDT-----------EKAQRSLTEIERKAQANEQRYSKLKEK 440
Cdd:PTZ00121 1301 KKKADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAkkaaeaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 441 YSELvQNHADLLRKNAEVTKQVSVARQAQVDLER--EKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSA 518
Cdd:PTZ00121 1380 ADAA-KKKAEEKKKADEAKKKAEEDKKKADELKKaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 519 QSEAKWLTQIA----ELEK--EQGSLATVAAQREEELSALRDQLESTQIKLAGAQESmcQQVKDQRKTllAGIRKAAERE 592
Cdd:PTZ00121 1459 AEEAKKKAEEAkkadEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA--KKAEEAKKA--DEAKKAEEAK 1534
|
250
....*....|
gi 1845865226 593 IQEALSQLEE 602
Cdd:PTZ00121 1535 KADEAKKAEE 1544
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
352-598 |
1.11e-03 |
|
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: 42.90 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 352 GLTGQLDNMKIESQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDtekAQRSLteieRKAQAN 430
Cdd:pfam12128 582 GVKLDLKRIDVPEWAASEEeLRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETF---ARTAL----KNARLD 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 431 EQRYSklkekyselVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELAdsfartQEQQDVLENLKHELATSRQELQvl 510
Cdd:pfam12128 655 LRRLF---------DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD------KKHQAWLEEQKEQKREARTEKQ-- 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 511 hsnletsaqseAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES---TQIKLAGAQESMCQQVKDQRKTLLAGIRK 587
Cdd:pfam12128 718 -----------AYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETwykRDLASLGVDPDVIAKLKREIRTLERKIER 786
|
250
....*....|.
gi 1845865226 588 AAEREiQEALS 598
Cdd:pfam12128 787 IAVRR-QEVLR 796
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
340-558 |
1.27e-03 |
|
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: 43.02 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 340 DHLIERlyreISGLTGQLDNMKiESQRAMLQLKGRVSELEAELA-----EQQHlgrqamddcEFLRTELDELKRQREDTE 414
Cdd:COG3096 889 ETLADR----LEELREELDAAQ-EAQAFIQQHGKALAQLEPLVAvlqsdPEQF---------EQLQADYLQAKEQQRRLK 954
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 415 KAQRSLTE-IERKAQANEQRYSKLKEKYSELV-QNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDV 492
Cdd:COG3096 955 QQIFALSEvVQRRPHFSYEDAVGLLGENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQT 1034
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845865226 493 LENLKHEL------------ATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 558
Cdd:COG3096 1035 LQELEQELeelgvqadaeaeERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
399-599 |
1.47e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 399 LRTELDELKRQRE----------DTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR---KNAEVTKQ---- 461
Cdd:PRK11281 41 VQAQLDALNKQKLleaedklvqqDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkdDNDEETREtlst 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 462 VSVAR------QAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNL-ETSAQSEAKWLTQIAELEKE 534
Cdd:PRK11281 121 LSLRQlesrlaQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLkGGKVGGKALRPSQRVLLQAE 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845865226 535 QGSLATVAAQREEEL---SALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 599
Cdd:PRK11281 201 QALLNAQNDLQRKSLegnTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQ 268
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
399-577 |
1.57e-03 |
|
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: 42.31 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 399 LRTELDELKRQREDTEKAQ-RSLTEIERKaqanEQRYSKLKEKYSELvqnhadllrknaevTKQVSvarqaqvDLEREKK 477
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIdKFLTEIKKK----EKELEKLNNKYNDL--------------KKQKE-------ELENELN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 478 ELADSfartqeqqdvLENLKHELATSRQELQVLH---SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRD 554
Cdd:TIGR04523 177 LLEKE----------KLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
170 180
....*....|....*....|...
gi 1845865226 555 QLESTQIKLAGAQESMcQQVKDQ 577
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQ-NKIKKQ 268
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
471-568 |
1.83e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 471 DLEREKKELADSFA----RTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQRE 546
Cdd:PRK09039 57 RLNSQIAELADLLSlerqGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL 136
|
90 100
....*....|....*....|..
gi 1845865226 547 EELSALRDQLESTQIKLAGAQE 568
Cdd:PRK09039 137 AQVELLNQQIAALRRQLAALEA 158
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
362-516 |
1.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 362 IESQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIE---------------- 424
Cdd:PRK02224 532 IEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRtllaaiadaedeierl 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 425 ---RKAQA--NEQRYSKLKEK---YSELVQNHADLLRKNAEVTKQVSVARQAQVD-----LEREKKELADSFARTQEQQD 491
Cdd:PRK02224 612 rekREALAelNDERRERLAEKrerKRELEAEFDEARIEEAREDKERAEEYLEQVEekldeLREERDDLQAEIGAVENELE 691
|
170 180
....*....|....*....|....*...
gi 1845865226 492 VLENLKHE---LATSRQELQVLHSNLET 516
Cdd:PRK02224 692 ELEELRERreaLENRVEALEALYDEAEE 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-602 |
1.85e-03 |
|
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: 42.35 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 427 AQANEQRySKLKEKYSeLVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQE 506
Cdd:TIGR02168 632 DNALELA-KKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 507 LQVLHSNLETSAQSEAKWLT----QIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLL 582
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-AEAEAEIEELE 788
|
170 180
....*....|....*....|..
gi 1845865226 583 AGIRKAAER--EIQEALSQLEE 602
Cdd:TIGR02168 789 AQIEQLKEElkALREALDELRA 810
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
407-535 |
1.98e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 407 KRQREDTEKAQRSLTEIERKAQA-NEQRYSKLKEKYSELVQNH-ADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfa 484
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAiKKEALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLELL----- 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1845865226 485 rtQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQ 535
Cdd:PRK12704 106 --EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE 154
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
412-602 |
2.21e-03 |
|
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: 41.94 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 412 DTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLlrknaevtkqVSVARQAQVDLErekkELADSFARTQEQQD 491
Cdd:pfam05667 227 NSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEA----------TSGASRSAQDLA----ELLSSFSGSSTTDT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 492 VLenLKHELATSRQELQvlhsnLETSAQSEAKWLTQIAELEKEqgslatVAAQREEELSALRDQLESTQIKLagaqesmc 571
Cdd:pfam05667 293 GL--TKGSRFTHTEKLQ-----FTNEAPAATSSPPTKVETEEE------LQQQREEELEELQEQLEDLESSI-------- 351
|
170 180 190
....*....|....*....|....*....|...
gi 1845865226 572 QQVKDQRKTLLAGIRKAAE--REIQEALSQLEE 602
Cdd:pfam05667 352 QELEKEIKKLESSIKQVEEelEELKEQNEELEK 384
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
350-602 |
2.68e-03 |
|
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: 41.88 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 350 ISGLTGqLDNMKIESQRAMLQLKGRVSELEAELAEQQHLgrqaMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQA 429
Cdd:TIGR00618 169 LMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLL----TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 430 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvarqAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQV 509
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 510 LHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEelsaLRDQLEstqiklagaQESMCQQVKDQRKTLLAGIRKAA 589
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH----IRDAHE---------VATSIREISCQQHTLTQHIHTLQ 385
|
250
....*....|...
gi 1845865226 590 erEIQEALSQLEE 602
Cdd:TIGR00618 386 --QQKTTLTQKLQ 396
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
337-597 |
2.78e-03 |
|
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: 41.73 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 337 DEKDHLIERLYREISGLTGQLDNM----------------KIES--------QRAMLQLKGRVSELEAE----------- 381
Cdd:pfam10174 362 NKKTKQLQDLTEEKSTLAGEIRDLkdmldvkerkinvlqkKIENlqeqlrdkDKQLAGLKERVKSLQTDssntdtalttl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 382 ---LAEQQHL-----------GRQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKeKYSELV 445
Cdd:pfam10174 442 eeaLSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSalQPELTEKESSLIDLKEHASSLASSGLK-KDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 446 QNHADLLRKNAEVTKQVSVARQAQ------------VD----LEREKKELADSFARTQEQQDVL-------ENLKH---- 498
Cdd:pfam10174 521 SLEIAVEQKKEECSKLENQLKKAHnaeeavrtnpeiNDrirlLEQEVARYKEESGKAQAEVERLlgilrevENEKNdkdk 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 499 -----ELATSRQ--ELQVLHSNLETSAQSE-AKWLTQIAELEKEQGSLATVAAQR--EEELSAL---RDQLESTQIKLAG 565
Cdd:pfam10174 601 kiaelESLTLRQmkEQNKKVANIKHGQQEMkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSS 680
|
330 340 350
....*....|....*....|....*....|....*.
gi 1845865226 566 AQESMCQqvKDQRKTLLAGIRKAAEREI----QEAL 597
Cdd:pfam10174 681 TQQSLAE--KDGHLTNLRAERRKQLEEIlemkQEAL 714
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
343-606 |
3.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 343 IERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAelAEQQhlgrqamddcefLRTELDELKRQREDTEKAQRSLTE 422
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ--LEEE------------LEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 423 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELAT 502
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 503 SRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLL 582
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260
....*....|....*....|....
gi 1845865226 583 AGIRKAAEREIQEALSQLEEPTLI 606
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALE 289
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
402-563 |
4.27e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 402 ELDELKRQREDTEKAQRSLtEIERKAQANEQRYSKLKEKYSEL---VQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE 478
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL-DLDEAEEKNEEIQERIDQLYDILereVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 479 LADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQ--SE-----AKWLTQIAELEKEQGSLA-TVAAQREEELS 550
Cdd:PRK04778 336 VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIaySElqeelEEILKQLEEIEKEQEKLSeMLQGLRKDELE 415
|
170
....*....|...
gi 1845865226 551 AlRDQLESTQIKL 563
Cdd:PRK04778 416 A-REKLERYRNKL 427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-596 |
4.55e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 361 KIESQRAMLQLKGRVSEL----EAELAEQQHLGRQAMDDCEFLRTE----LDELKRQrEDTEKAQRsLTEIERKAQANEQ 432
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEAKKAEekkkADELKKA-EELKKAEE-KKKAEEAKKAEED 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 433 RYSKLKEkyselvqnhadllrknAEVTKQVSVARQAQVD--LEREKKELADSFARTQEQQDVLENLKHElatsrQELQVL 510
Cdd:PTZ00121 1576 KNMALRK----------------AEEAKKAEEARIEEVMklYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKK 1634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 511 HSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTllAGIRKAAE 590
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA--EELKKKEA 1712
|
....*.
gi 1845865226 591 REIQEA 596
Cdd:PTZ00121 1713 EEKKKA 1718
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
338-563 |
6.50e-03 |
|
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: 40.49 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 338 EKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEaELAEQQHLGRQAMDDCEFLRTELDelKRQREDTEKAQ 417
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQLRQNLE--KQQSSLAEAEQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 418 RsLTEIERKAQANEQRYSKLKEKYSELVQ--NHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLEN 495
Cdd:pfam05557 171 R-IKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAAT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 496 LKHELATSRQELQ-----------------VLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 558
Cdd:pfam05557 250 LELEKEKLEQELQswvklaqdtglnlrspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED 329
|
....*
gi 1845865226 559 TQIKL 563
Cdd:pfam05557 330 LNKKL 334
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
401-553 |
6.88e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 401 TELDELKRQ-----------REDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQvsvarqaq 469
Cdd:PRK09039 53 SALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE-------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 470 vdLEREKKELADsfARTQeqqdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELekeqGSLATVA-AQREEE 548
Cdd:PRK09039 125 --LDSEKQVSAR--ALAQ-----VELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL----GRRLNVAlAQRVQE 191
|
....*
gi 1845865226 549 LSALR 553
Cdd:PRK09039 192 LNRYR 196
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
467-603 |
7.05e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 467 QAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETsaqseakwltQIAELEkeqgslatvaaqrE 546
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEE----------KKEKLQ-------------E 562
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1845865226 547 EELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEEP 603
Cdd:PRK00409 563 EEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKA 619
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
480-598 |
7.05e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 480 ADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQgslatvaAQREEELSALRDQLEST 559
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQ-------QELEAQLEQLQEKAAET 210
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1845865226 560 QiklagaqesmcQQVKDQRKTLlagIRKAAER-EIQEALS 598
Cdd:PRK11448 211 S-----------QERKQKRKEI---TDQAAKRlELSEEET 236
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
403-602 |
7.14e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.21 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 403 LDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvarQAQVDLEREKKELADS 482
Cdd:pfam12795 29 LDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLSLEELEQRLL----QTSAQLQELQNQLAQL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 483 FARTQEQQDVLENLKHELATSRQELQVLHSNLE-TSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSA--LRDQLEST 559
Cdd:pfam12795 105 NSQLIELQTRPERAQQQLSEARQRLQQIRNRLNgPAPPGEPLSEAQRWALQAELAALKAQIDMLEQELLSnnNRQDLLKA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1845865226 560 QIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 602
Cdd:pfam12795 185 RRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
370-591 |
7.30e-03 |
|
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: 40.27 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 370 QLKGRVSELEAELAEQQHLGRQAMDdceflrTELDELKRQREDTEKAQRSL--------TEIERKAQANEQRYSKLKEKY 441
Cdd:pfam15964 364 ELERQKERLEKELASQQEKRAQEKE------ALRKEMKKEREELGATMLALsqnvaqleAQVEKVTREKNSLVSQLEEAQ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 442 SELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDV-LENLKHELATSRQELQVLHSNlETSAQS 520
Cdd:pfam15964 438 KQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQeIEKLGLELSESKQRLEQAQQD-AARARE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 521 EAKWLTQ----------IAELEK---------EQGSLATVAAQREEELS-------ALRDQLESTQIKLAGAQESMCQQV 574
Cdd:pfam15964 517 ECLKLTEllgesehqlhLTRLEKesiqqsfsnEAKAQALQAQQREQELTqkmqqmeAQHDKTVNEQYSLLTSQNTFIAKL 596
|
250
....*....|....*..
gi 1845865226 575 KDQRKTLLAGIRKAAER 591
Cdd:pfam15964 597 KEECCTLAKKLEEITQK 613
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
405-602 |
7.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 405 ELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFA 484
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 485 RTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIaELEKEQGSLATVAAQREEELSALRDQLESTQIKLA 564
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*...
gi 1845865226 565 GAqESMCQQVKDQRKTllagirkaaEREIQEALSQLEE 602
Cdd:PRK03918 332 EL-EEKEERLEELKKK---------LKELEKRLEELEE 359
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
367-492 |
7.96e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 367 AMLQLKGRVSELEAELAEQ------QHLGRQAmddcefLRTELDELKRQREDTEKAQRSLTEIERK-AQANEQRYSKLKE 439
Cdd:COG3206 264 VIQQLRAQLAELEAELAELsarytpNHPDVIA------LRAQIAALRAQLQQEAQRILASLEAELEaLQAREASLQAQLA 337
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1845865226 440 KYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKEladsfARTQEQQDV 492
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE-----ARLAEALTV 385
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
353-536 |
8.00e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 353 LTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQR-------SLTEIER 425
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845865226 426 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFART---QEQQDVLENLKH 498
Cdd:PLN02939 279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEAnvsKFSSYKVELLQQ 358
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1845865226 499 ELATSRQELQV----LHSNLETSAQSEAKWLTQIAELEKEQG 536
Cdd:PLN02939 359 KLKLLEERLQAsdheIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| |
