NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|49274606|ref|NP_080497|]
View 

liprin-beta-1 isoform 2 [Mus musculus]

Protein Classification

SAM_liprin-beta1,2_repeat2 and SAM_liprin-beta1,2_repeat3 domain-containing protein( domain architecture ID 10175983)

protein containing domains SAM_liprin-beta1,2_repeat1, SAM_liprin-beta1,2_repeat2, and SAM_liprin-beta1,2_repeat3

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 762-833 4.68e-46

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


:

Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.16  E-value: 4.68e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 762 EVQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 833
Cdd:cd09569   1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 677-739 1.58e-37

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 134.36  E-value: 1.58e-37
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606 677 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:cd09566   1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 603-666 3.33e-33

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


:

Pssm-ID: 188962  Cd Length: 64  Bit Score: 121.95  E-value: 3.33e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49274606 603 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 666
Cdd:cd09563   1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 120-300 2.89e-11

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 67.79  E-value: 2.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    120 VSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSR-TSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFr 198
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRL- 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    199 dtEGLIQEINDLRLKVNEM-DGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVcKAKGE------GIEVLDRD 271
Cdd:TIGR02169  268 --EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-KLEAEidkllaEIEELERE 344

                          170       180
                   ....*....|....*....|....*....
gi 49274606    272 IEVQKMKKavESLMAANEEKERKIEDLRQ 300
Cdd:TIGR02169  345 IEEERKRR--DKLTEEYAELKEELEDLRA 371
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 762-833 4.68e-46

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.16  E-value: 4.68e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 762 EVQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 833
Cdd:cd09569   1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 677-739 1.58e-37

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 134.36  E-value: 1.58e-37
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606 677 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:cd09566   1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 603-666 3.33e-33

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 121.95  E-value: 3.33e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49274606 603 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 666
Cdd:cd09563   1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 679-739 2.46e-18

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 79.62  E-value: 2.46e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49274606   679 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:pfam00536   4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 605-667 6.82e-15

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.99  E-value: 6.82e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606   605 KWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 667
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 603-667 1.11e-12

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 63.85  E-value: 1.11e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606    603 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 667
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 679-739 1.43e-11

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 60.77  E-value: 1.43e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606    679 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 120-300 2.89e-11

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 67.79  E-value: 2.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    120 VSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSR-TSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFr 198
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRL- 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    199 dtEGLIQEINDLRLKVNEM-DGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVcKAKGE------GIEVLDRD 271
Cdd:TIGR02169  268 --EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-KLEAEidkllaEIEELERE 344

                          170       180
                   ....*....|....*....|....*....
gi 49274606    272 IEVQKMKKavESLMAANEEKERKIEDLRQ 300
Cdd:TIGR02169  345 IEEERKRR--DKLTEEYAELKEELEDLRA 371
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
766-833 4.95e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.95e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49274606   766 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 833
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-307 1.77e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.09  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQqELLSRTSLETQKLELMAEISNLKLKL 183
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  184 TAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMdgerlqyEKKLKSTKDELASLKEQLEEKEcEVKRLQERLvckakgE 263
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEERHELYE-EAKAKKEEL------E 375

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 49274606  264 GIEVLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 307
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-328 5.81e-09

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 60.12  E-value: 5.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    54 DLRGLLEMMETDEKEgLRCQIPDSTAEVLIEWLQNQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483 187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   134 IRDLEFCLEEHREKLNATEE--MLQQELLSRtsLETQKLELMAEISNLKLKLT-AVEKDRLDYEDRFRDTEGLIQEINDL 210
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTICQLTEEK 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   211 RLKVNEMDGERLQYEKKLKSTKDELASLKEQL--EEKECEVKRLQERLVCkakgegievldrdIEVQKMKKAVESLMAAN 288
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEELLrtEQQRLEKNEDQLKIIT-------------MELQKKSSELEEMTKFK 400

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 49274606   289 EEKERKIEDLRQCLSRYRKMQDP-------AVLAQGQDSECEGLFHS 328
Cdd:pfam05483 401 NNKEVELEELKKILAEDEKLLDEkkqfekiAEELKGKEQELIFLLQA 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-309 2.03e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 102 YQERLARLenDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKL 181
Cdd:COG1196 218 LKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 182 KLTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERL--VCK 259
Cdd:COG1196 296 ELARLEQDIARLEERRRELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleAEA 372

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 49274606 260 AKGEGIEVLDRD-IEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKMQ 309
Cdd:COG1196 373 ELAEAEEELEELaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 763-832 6.53e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.29  E-value: 6.53e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    763 VQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 832
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 762-833 4.68e-46

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.16  E-value: 4.68e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 762 EVQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 833
Cdd:cd09569   1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 677-739 1.58e-37

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 134.36  E-value: 1.58e-37
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606 677 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:cd09566   1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 603-666 3.33e-33

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 121.95  E-value: 3.33e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49274606 603 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 666
Cdd:cd09563   1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 770-831 6.39e-33

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188895  Cd Length: 62  Bit Score: 121.11  E-value: 6.39e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 770 RVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNL 831
Cdd:cd09496   1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 766-833 2.19e-31

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 117.16  E-value: 2.19e-31
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49274606 766 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 833
Cdd:cd09570   5 WTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 682-739 3.35e-20

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188894  Cd Length: 60  Bit Score: 84.89  E-value: 3.35e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 49274606 682 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 739
Cdd:cd09495   2 WVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVhLKVTSQLHHLSLKCGIHVLH 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 679-739 2.46e-18

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 79.62  E-value: 2.46e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49274606   679 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:pfam00536   4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 766-833 1.14e-17

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 78.13  E-value: 1.14e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49274606 766 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 833
Cdd:cd09568   5 WSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 605-667 6.82e-15

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.99  E-value: 6.82e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606   605 KWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 667
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 611-666 1.96e-14

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 68.41  E-value: 1.96e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 49274606 611 VCSWLAEQGLGS-YLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 666
Cdd:cd09494   2 VCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 682-736 9.38e-13

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 63.80  E-value: 9.38e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 49274606 682 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQ 736
Cdd:cd09487   1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 603-667 1.11e-12

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 63.85  E-value: 1.11e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606    603 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 667
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 677-739 2.20e-12

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 62.81  E-value: 2.20e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606 677 KLDFNWVTR-WLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 739
Cdd:cd09567   1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKhLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 679-739 1.43e-11

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 60.77  E-value: 1.43e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606    679 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 120-300 2.89e-11

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 67.79  E-value: 2.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    120 VSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSR-TSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFr 198
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRL- 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    199 dtEGLIQEINDLRLKVNEM-DGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVcKAKGE------GIEVLDRD 271
Cdd:TIGR02169  268 --EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-KLEAEidkllaEIEELERE 344

                          170       180
                   ....*....|....*....|....*....
gi 49274606    272 IEVQKMKKavESLMAANEEKERKIEDLRQ 300
Cdd:TIGR02169  345 IEEERKRR--DKLTEEYAELKEELEDLRA 371
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
766-833 4.95e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.95e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49274606   766 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 833
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-307 1.77e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.09  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQqELLSRTSLETQKLELMAEISNLKLKL 183
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  184 TAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMdgerlqyEKKLKSTKDELASLKEQLEEKEcEVKRLQERLvckakgE 263
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEERHELYE-EAKAKKEEL------E 375

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 49274606  264 GIEVLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 307
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 610-665 1.97e-10

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 56.86  E-value: 1.97e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 49274606 610 QVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLeKELGIKHSLHRKKLQLALQ 665
Cdd:cd09487   1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-328 5.81e-09

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 60.12  E-value: 5.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    54 DLRGLLEMMETDEKEgLRCQIPDSTAEVLIEWLQNQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483 187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   134 IRDLEFCLEEHREKLNATEE--MLQQELLSRtsLETQKLELMAEISNLKLKLT-AVEKDRLDYEDRFRDTEGLIQEINDL 210
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTICQLTEEK 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   211 RLKVNEMDGERLQYEKKLKSTKDELASLKEQL--EEKECEVKRLQERLVCkakgegievldrdIEVQKMKKAVESLMAAN 288
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEELLrtEQQRLEKNEDQLKIIT-------------MELQKKSSELEEMTKFK 400

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 49274606   289 EEKERKIEDLRQCLSRYRKMQDP-------AVLAQGQDSECEGLFHS 328
Cdd:pfam05483 401 NNKEVELEELKKILAEDEKLLDEkkqfekiAEELKGKEQELIFLLQA 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-307 7.67e-09

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: 59.69  E-value: 7.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    104 ERLARLENDKESLvlQVSVLTDQVEAqgekirdlefcLEEHREKLNATEEMLQQEllsRTSLETQKLELMAEISNLKLKL 183
Cdd:TIGR02168  213 ERYKELKAELREL--ELALLVLRLEE-----------LREELEELQEELKEAEEE---LEELTAELQELEEKLEELRLEV 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    184 TAVEKDRLDYEDRFrdtegliqeiNDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLvcKAKGE 263
Cdd:TIGR02168  277 SELEEEIEELQKEL----------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL--AELEE 344

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 49274606    264 GIEVLdrDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 307
Cdd:TIGR02168  345 KLEEL--KEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-306 8.71e-09

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: 59.69  E-value: 8.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK---LNATEEMLQ---QELLSR--------TSL 165
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEaqlEELESKldelaeelAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    166 ETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQ----EINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQ 241
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    242 LEE-----KECEVKRLQERLVckAKGEGIEVLDRDIEVqkMKKAVESLMAANEEKERKIEDLRQCLSRYR 306
Cdd:TIGR02168  423 IEEllkklEEAELKELQAELE--ELEEELEELQEELER--LEEALEELREELEEAEQALDAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-300 2.27e-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: 58.14  E-value: 2.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    103 QERLARLENDKESLVLQV-------SVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAE 175
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    176 ISNLKLKLTAVEKDRLDYEDRFRDTEGLI----QEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKR 251
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLedleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 49274606    252 LQERLvcKAKGEGIEVLDRdiEVQKMKKAVESLMAANEEKERKIEDLRQ 300
Cdd:TIGR02168  892 LRSEL--EELSEELRELES--KRSELRRELEELREKLAQLELRLEGLEV 936
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-304 3.32e-08

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: 57.77  E-value: 3.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    102 YQERLARLE--------NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQ------ELLSRTSLET 167
Cdd:TIGR02169  213 YQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEQLRV 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    168 QK--LELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQ----EINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQ 241
Cdd:TIGR02169  293 KEkiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDkllaEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606    242 LEEKECEVKRLQERLvcKAKGEGIEVLDRDIEvqKMKKAVESLMAANEEKERKIEDLRQCLSR 304
Cdd:TIGR02169  373 LEEVDKEFAETRDEL--KDYREKLEKLKREIN--ELKRELDRLQEELQRLSEELADLNAAIAG 431
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-298 3.98e-08

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: 57.34  E-value: 3.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLE---FCLEEHREKLNATEEMLQQELLS--------RTSLETQKLE 171
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLKVlsrsinkiKQNLEQKQKE 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   172 LMAEISNLKlKLTAVEKDrldYEDRFRDtegLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEvkr 251
Cdd:TIGR04523 491 LKSKEKELK-KLNEEKKE---LEEKVKD---LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE--- 560

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 49274606   252 lqerlvckakgegIEVLDRDIEVQKMKKAVESLMAANEEKERKIEDL 298
Cdd:TIGR04523 561 -------------KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 678-740 5.02e-08

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 50.55  E-value: 5.02e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606 678 LDFNWV-TRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLRI 740
Cdd:cd09565   1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRThLKMVDSFHRTSLQYGILCLKR 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
131-307 1.28e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  131 GEKIRDLEFCLEEHREKLNATEEMlqQELLSrtSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDL 210
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENI--EELIK--EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  211 RLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQE-----RLVCKAKGEGIEVLDRDIEVQKMK------- 278
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLsrleeei 323

                        170       180
                 ....*....|....*....|....*....
gi 49274606  279 KAVESLMAANEEKERKIEDLRQCLSRYRK 307
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEK 352
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-309 2.03e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 102 YQERLARLenDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKL 181
Cdd:COG1196 218 LKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 182 KLTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERL--VCK 259
Cdd:COG1196 296 ELARLEQDIARLEERRRELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleAEA 372

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 49274606 260 AKGEGIEVLDRD-IEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKMQ 309
Cdd:COG1196 373 ELAEAEEELEELaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 606-667 2.04e-07

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 48.85  E-value: 2.04e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 606 WTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 667
Cdd:cd09505   5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-310 2.68e-07

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: 54.69  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    183 LTAVEKDRLDYEDRFRDT--EGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLvcKA 260
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI--KS 851

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 49274606    261 KGEGIEVLDRDI-----EVQKMKKAVESLMAANEEKERKIEDLRqclSRYRKMQD 310
Cdd:TIGR02169  852 IEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELE---AQLRELER 903
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 604-665 3.33e-07

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 48.22  E-value: 3.33e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606 604 AKWTKEQVCSWL-AEQGLGSYLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQ 665
Cdd:cd09564   2 SRWKADMVLAWLeVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIE 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-300 5.40e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 5.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 183 LTAVEKDRLDYEDRfrdTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLvckaKG 262
Cdd:COG1196 388 LLEALRAAAELAAQ---LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE----EA 460

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 49274606 263 EGIEVLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQ 300
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 683-738 6.16e-07

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 47.31  E-value: 6.16e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 49274606 683 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 738
Cdd:cd09506  10 VGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 763-832 6.53e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.29  E-value: 6.53e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    763 VQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 832
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 602-667 1.38e-06

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 46.64  E-value: 1.38e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49274606 602 PFAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 667
Cdd:cd09507   1 PVTNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 109-302 1.46e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 52.48  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    109 LENDKESLVLQVSVLTdQVEAQGE-KIRDLEFCLEEHREKLNATEEmLQQELLSRTSLETQKLE-LMAEISNLKLKLTAV 186
Cdd:pfam01576  382 LESENAELQAELRTLQ-QAKQDSEhKRKKLEGQLQELQARLSESER-QRAELAEKLSKLQSELEsVSSLLNEAEGKNIKL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    187 EKDRLDYEDRFRDTEGLIQEinDLRLKvnemdgerLQYEKKLKSTKDELASLKEQLEEKEcEVKRLQERLVCKAKgegIE 266
Cdd:pfam01576  460 SKDVSSLESQLQDTQELLQE--ETRQK--------LNLSTRLRQLEDERNSLQEQLEEEE-EAKRNVERQLSTLQ---AQ 525

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 49274606    267 VLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCL 302
Cdd:pfam01576  526 LSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 683-735 1.58e-06

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 46.15  E-value: 1.58e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 49274606 683 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAI 735
Cdd:cd09533   2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
679-739 1.77e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.11  E-value: 1.77e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606   679 DFNWVTRWLDDIGLPQYKTQFDEGRVDG-RMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:pfam07647   5 SLESVADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 133-308 1.97e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.92  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 133 KIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDR------FRDTEGLIQE 206
Cdd:COG1579  18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 207 INDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLvckakgegievldrDIEVQKMKKAVESLMA 286
Cdd:COG1579  98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL--------------DEELAELEAELEELEA 163

                       170       180
                ....*....|....*....|...
gi 49274606 287 ANEEKERKI-EDLrqcLSRYRKM 308
Cdd:COG1579 164 EREELAAKIpPEL---LALYERI 183
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 105-300 3.07e-06

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 50.19  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   105 RLARLENDKESLVLQVSVLTDQveaqgEKIRDLEFCLEEHREKLNATEE--MLQQELLSRTSLETQK--LELMAEISNLK 180
Cdd:pfam15905 130 QLLELTRVNELLKAKFSEDGTQ-----KKMSSLSMELMKLRNKLEAKMKevMAKQEGMEGKLQVTQKnlEHSKGKVAQLE 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   181 LKLTAVEKDRLDYEDrfrDTEGLIQEINDLRLKVNEMDGERL---QYEKKLKSTKDELASLKEQLEEKECEVKRLQERLV 257
Cdd:pfam15905 205 EKLVSTEKEKIEEKS---ETEKLLEYITELSCVSEQVEKYKLdiaQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLN 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 49274606   258 --CKAKGEGIEVLDRDIEVQK--MKKAVESLMAANEEKERKIEDLRQ 300
Cdd:pfam15905 282 ekCKLLESEKEELLREYEEKEqtLNAELEELKEKLTLEEQEHQKLQQ 328
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 103-321 4.31e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 4.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNAteemLQQELLSRTSLETQKLELMAEIsnlkLK 182
Cdd:COG3883  22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK----LQAEIAEAEAEIEERREELGER----AR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 183 LTAVEKDRLDYEDRF---RDTEGLIQEINDLRlKVNEMDGERLQyekKLKSTKDELASLKEQLEEKECEVKRLQERLVCK 259
Cdd:COG3883  94 ALYRSGGSVSYLDVLlgsESFSDFLDRLSALS-KIADADADLLE---ELKADKAELEAKKAELEAKLAELEALKAELEAA 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 260 AKgegievldrdiEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKMQDPAVLAQGQDSE 321
Cdd:COG3883 170 KA-----------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 155-300 4.84e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.77  E-value: 4.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 155 LQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDGERLQYEKKLKSTKD- 233
Cdd:COG1579  12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLGNVRNn 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606 234 --------ELASLKEQLEEKECEVKRLQERLvcKAKGEGIEVLDRDIEvqKMKKAVESLMAANEEKERKIEDLRQ 300
Cdd:COG1579  89 keyealqkEIESLKRRISDLEDEILELMERI--EELEEELAELEAELA--ELEAELEEKKAELDEELAELEAELE 159
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-312 5.38e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.76  E-value: 5.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942   3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 195 DRFRDtegLIQEINDLRLKVNEMDGE-------------------------------RLQYEK-----------KLKSTK 232
Cdd:COG4942  83 AELAE---LEKEIAELRAELEAQKEElaellralyrlgrqpplalllspedfldavrRLQYLKylaparreqaeELRADL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 233 DELASLKEQLEEKECEVKRLQERLVCKAKGEGIEVLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKMQDPA 312
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
141-307 6.22e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 6.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 141 LEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEdrfrdtegLIQEINDLRLKVNEMDgE 220
Cdd:COG4717  76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--------LYQELEALEAELAELP-E 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 221 RLQyekKLKSTKDELASLKEQLEEKECEVKRLQERLVCKAKGEGIEVLDrdiEVQKMKKAVESLMAANEEKERKIEDLRQ 300
Cdd:COG4717 147 RLE---ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQE 220


                ....*..
gi 49274606 301 CLSRYRK 307
Cdd:COG4717 221 ELEELEE 227
Filament pfam00038
Intermediate filament protein;
125-256 6.48e-06

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 49.15  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   125 DQVEAQGEKIRDLEFCLEEHREKLNAT----EEMLQQEL--LSRT--SLETQKLELMAEISNLKLkltAVEKDRLDYEDR 196
Cdd:pfam00038  18 DKVRFLEQQNKLLETKISELRQKKGAEpsrlYSLYEKEIedLRRQldTLTVERARLQLELDNLRL---AAEDFRQKYEDE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   197 FRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEkecEVKRLQERL 256
Cdd:pfam00038  95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEE---EVRELQAQV 151
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
103-256 7.90e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 7.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 103 QERLARLENDKESLVLQVSVLTDQVEAQG--EKIRDLEFCLEEHREKLnateEMLQQELLSRTSLETQKLELMAEISNLK 180
Cdd:COG4717 101 EEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQ 176

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49274606 181 LKLTAvEKDRLDYEDRfrdtegliQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLE--EKECEVKRLQERL 256
Cdd:COG4717 177 EELEE-LLEQLSLATE--------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERL 245
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
100-300 8.40e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 8.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 100 DVYQERlaRLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK--LNATEEMLQQELLSRTSLETQKLELMAEIS 177
Cdd:COG3206 159 EAYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELA 236

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 178 NLKLKLTAVEKDRLDYEDRFRDTEGlIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLV 257
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 49274606 258 CKAKGEGIEVLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQ 300
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLER 358
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 603-667 1.24e-05

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 44.09  E-value: 1.24e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49274606 603 FAKWTKEQVCSWLaEQGLGS---YLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 667
Cdd:cd09562   1 FALWNGPTVVAWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
103-297 1.46e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQellsrtsLETQKLELMAEISNLKLK 182
Cdd:COG4372  30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-------LNEQLQAAQAELAQAQEE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 183 LTAVEKDrldYEDRFRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVCKAKG 262
Cdd:COG4372 103 LESLQEE---AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179

                       170       180       190
                ....*....|....*....|....*....|....*
gi 49274606 263 EGIEVLDRDIEVQKMKKAVESLMAANEEKERKIED 297
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 89-300 1.52e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.95  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    89 QMTNghLPGNGDVYQERLARLENDKESLVLQvsvlTDQVEAQGEKIR----DLEFCLEEHREKLNATEEMLQQELLSRTS 164
Cdd:pfam05483 395 EMTK--FKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKgkeqELIFLLQAREKEIHDLEIQLTAIKTSEEH 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   165 LETQKLELMAEISNLKLK---LTAvEKDRLDYEDRfrdteGLIQEINDLRLKVN----EMDGERLQYEKKLKST------ 231
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKnieLTA-HCDKLLLENK-----ELTQEASDMTLELKkhqeDIINCKKQEERMLKQIenleek 542

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606   232 ----KDELASLKEQLEEKECEVKRLQERLVCKAKGEGIEVLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQ 300
Cdd:pfam05483 543 emnlRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 109-298 1.88e-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: 48.48  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   109 LENDKESLVLqvSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEisnLKLKLTAVEK 188
Cdd:TIGR04523 300 LNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEK 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   189 DRLDYEDRFRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKstkdelaSLKEQLEEKECEVKRLQErLVCKAKGEgIEVL 268
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK-------KLQQEKELLEKEIERLKE-TIIKNNSE-IKDL 445

                         170       180       190
                  ....*....|....*....|....*....|
gi 49274606   269 DRDIEVqkMKKAVESLMAANEEKERKIEDL 298
Cdd:TIGR04523 446 TNQDSV--KELIIKNLDNTRESLETQLKVL 473
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-239 2.46e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKLNATEEMLQQEL----LSRTSLETQKLELMAE 175
Cdd:COG4913  291 ELLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDRLEQLEREIerleRELEERERRRARLEAL 367

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606  176 ISNLKLKLTAVEKDRLDYEDRFRDT-EGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLK 239
Cdd:COG4913  368 LAALGLPLPASAEEFAALRAEAAALlEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 606-667 2.82e-05

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 43.06  E-value: 2.82e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 606 WTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 667
Cdd:cd09501   4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVEL 65
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-320 3.07e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  103 QERLARLENdkeslvlQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQqelLSRTSLETQKLElmAEISNLKLK 182
Cdd:COG4913  609 RAKLAALEA-------ELAELEEELAEAEERLEALEAELDALQERREALQRLAE---YSWDEIDVASAE--REIAELEAE 676

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  183 LTAVEKDRLDYEdrfrdteGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVCKAKG 262
Cdd:COG4913  677 LERLDASSDDLA-------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606  263 EGIE----VLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKmQDPAVLAQGQDS 320
Cdd:COG4913  750 LLEErfaaALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR-EWPAETADLDAD 810
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
97-300 3.17e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   97 GNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEI 176
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  177 SNLKLKLTAVEKDRLDYEDRFRDTEGLIQE------------------INDLRLKVNEMDGERLQYEKKLKSTKDELASL 238
Cdd:PRK02224 422 DELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA 501

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606  239 kEQLEEKECEVKRLQER--LVCKAKGEGIEVLDRDIE-VQKMKKAVESLMAANEEKERKIEDLRQ 300
Cdd:PRK02224 502 -EDLVEAEDRIERLEERreDLEELIAERRETIEEKRErAEELRERAAELEAEAEEKREAAAEAEE 565
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-256 3.18e-05

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: 48.13  E-value: 3.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606    183 LTAVEKDRLDYEdrfRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKST-KDELASLKEQLEEKECEVKRLQERL 256
Cdd:TIGR02168  903 LRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRL 974
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 103-318 3.74e-05

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: 47.64  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 103 QERLARLENDKESLVLQVSVLTDQVeAQGEKIRDLEFCLEEHREKLNATEEmlqqellsRTSLETQKLELMAEISNLKLK 182
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKI-AEYTKSIDIKKATESLEEQLAAAEA--------EQELEESKRETETGIQNLTAE 344

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 183 LtavekdrldyEDRFRDTEGLIQEIN-DLRLKVNEMDGERLqyEKKLKSTKDELASLKEQLEEKECEVKRlQERLVCKAK 261
Cdd:COG5185 345 I----------EQGQESLTENLEAIKeEIENIVGEVELSKS--SEELDSFKDTIESTKESLDEIPQNQRG-YAQEILATL 411

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 49274606 262 GEGIEVLDRDIEvqKMKKAVESLMAANEEKERKIEDLRQCLSRYRKMQDPAVLAQGQ 318
Cdd:COG5185 412 EDTLKAADRQIE--ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLE 466
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
606-667 4.00e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 42.26  E-value: 4.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606   606 WTKEQVCSWLAEQGLGSYLSS-GKHWIISGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 667
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNfRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 680-738 4.16e-05

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188929  Cd Length: 67  Bit Score: 42.31  E-value: 4.16e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606 680 FNW----VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 738
Cdd:cd09530   1 LSWdtedVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
127-300 6.31e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 6.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 127 VEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQE 206
Cdd:COG4372  26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 207 IND----LRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLvcKAKGEGIEVLDRDIEVQKMKKAVE 282
Cdd:COG4372 106 LQEeaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL--ESLQEELAALEQELQALSEAEAEQ 183

                       170
                ....*....|....*...
gi 49274606 283 SLMAANEEKERKIEDLRQ 300
Cdd:COG4372 184 ALDELLKEANRNAEKEEE 201
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-298 6.47e-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: 46.94  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   103 QERLARLENDKESLVLQVSVLTDQveaqgekIRDLEFCLEeHREKLNateEMLQQELlsrTSLETQKLELMAEISNLKlk 182
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQ-------INDLESKIQ-NQEKLN---QQKDEQI---KKLQQEKELLEKEIERLK-- 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   183 ltaveKDRLDYEDRFRDtegLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKR-LQERLVCKAK 261
Cdd:TIGR04523 433 -----ETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkEKELKKLNEE 504

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 49274606   262 GEGIE--VLDRDIEVQKMKKAVESLMAANEEKERKIEDL 298
Cdd:TIGR04523 505 KKELEekVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-255 7.60e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  103 QERLARLENDKESLVLQVSVLTDQVEAqgekirdlefcLEEHREKLNATEEMLQQELLSRTSLETQKLElmAEISNLKLK 182
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELER-----------LEARLDALREELDELEAQIRGNGGDRLEQLE--REIERLERE 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  183 LTAVEKDRLDYEDRFR--------DTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQE 254
Cdd:COG4913  354 LEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433


                 .
gi 49274606  255 R 255
Cdd:COG4913  434 R 434
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-307 1.09e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  141 LEEHREKLNATEEMLQQELLSRTSLETQKlELMAEISNLKLKLTA-----VEKDRLDYE---DRFRDTEGLIQEINDLRL 212
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLKKynleeLEKKAEEYEklkEKLIKLKGEIKSLKKELE 549

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  213 KVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECE-VKRLQERL--VCKAKGEGIEVLDRDIEVQKMKKAVESLMAANE 289
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLkeLEPFYNEYLELKDAEKELEREEKELKKLEEELD 629

                        170
                 ....*....|....*...
gi 49274606  290 EKERKIEDLRQCLSRYRK 307
Cdd:PRK03918 630 KAFEELAETEKRLEELRK 647
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 102-300 1.16e-04

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: 46.17  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQEL--LSR------------TSLET 167
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqLSEkqkeleqnnkkiKELEK 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   168 QKLELMAEISNLK----------LK--LTAVEKDRLDYEDRFRDTEGLI----QEINDLRLKVNEMDGERLQYEKKLKST 231
Cdd:TIGR04523 289 QLNQLKSEISDLNnqkeqdwnkeLKseLKNQEKKLEEIQNQISQNNKIIsqlnEQISQLKKELTNSESENSEKQRELEEK 368

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49274606   232 KDELASLKEQLEEKECEVKRLQERlvckakgegIEVLDRDIEVQKMKKA-----VESLMAANEEKERKIEDLRQ 300
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQ---------INDLESKIQNQEKLNQqkdeqIKKLQQEKELLEKEIERLKE 433
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 105-156 1.27e-04

Protein of unknown function DUF16; The function of this protein is unknown. It appears to only occur in Mycoplasma pneumoniae. The crystal structure revealed that this domain is composed of two separated homotrimeric coiled-coils.


Pssm-ID: 396208 [Multi-domain]  Cd Length: 95  Bit Score: 41.74  E-value: 1.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 49274606   105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQ 156
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 602-658 1.43e-04

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 41.10  E-value: 1.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 602 PFAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLeKELGI-----KHSLHRK 658
Cdd:cd09512   3 PVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKL-KALGItsssdRSLLKKK 63
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 103-272 1.46e-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: 44.53  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQellSRTSLETQKLElmAEISNLKLK 182
Cdd:COG1579  30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---VRNNKEYEALQ--KEIESLKRR 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 183 LTAVEKDRLDYEDRFRDTEGLIQEIND-LRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEV----KRLQERLV 257
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIppelLALYERIR 184

                       170
                ....*....|....*
gi 49274606 258 CKAKGEGIEVLDRDI 272
Cdd:COG1579 185 KRKNGLAVVPVEGGA 199
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 49-347 2.11e-04

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: 45.34  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606     49 LHLVEDLRGLLEMmETDEKEGLRCQipdstAEVLIEWLQNQMTNGHLPGNGDVYQERLARLENDKESLVLQV-------- 120
Cdd:TIGR00618  590 QNITVRLQDLTEK-LSEAEDMLACE-----QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervreh 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    121 SVLTDQVEAQGEKIRDLEFCLEEHR-EKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRD 199
Cdd:TIGR00618  664 ALSIRVLPKELLASRQLALQKMQSEkEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    200 TEGLIQEINDLRLKVNEMDGER--------LQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVCKAK-GEGIevldR 270
Cdd:TIGR00618  744 SLKELMHQARTVLKARTEAHFNnneevtaaLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPsDEDI----L 819

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    271 DIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRY---RKMQDPAVLAQGQDSECEG-LFHSSSISTLLDAQGFSDLERS 346
Cdd:TIGR00618  820 NLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYeecSKQLAQLTQEQAKIIQLSDkLNGINQIKIQFDGDALIKFLHE 899


                   .
gi 49274606    347 T 347
Cdd:TIGR00618  900 I 900
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 606-662 2.44e-04

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 40.39  E-value: 2.44e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49274606 606 WTKEQVCSWLAEQ-GLGSYLSSGKHWIISGQTLLQ-ASQQD--LEKELGIKHSLHRKKLQL 662
Cdd:cd09504   5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALPRlAVNNPsfLTSVLGIKDPIHRQKLSL 65
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 103-313 2.55e-04

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: 44.73  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMlqQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:pfam05557  51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA--REVISCLKNELSELRRQIQRAELELQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   183 LTAVEKDRLdyedrfrdtegliQEINDL-RLKVNEMDGERLQYEKKLKSTKDELASLKE------QLEEKECEVKRLQER 255
Cdd:pfam05557 129 STNSELEEL-------------QERLDLlKAKASEAEQLRQNLEKQQSSLAEAEQRIKElefeiqSQEQDSEIVKNSKSE 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 49274606   256 LvckakgEGIEVLDRDIEVQK-MKKAVESLMAANEEKERKIEDLRQCLSRYRKMQDPAV 313
Cdd:pfam05557 196 L------ARIPELEKELERLReHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAA 248
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-308 2.59e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  104 ERLARLENDKESLVLQVSVLTDQVEAQgEKIRDLEFCLEEHREKL-NATEEMLQQELLSrtsLETQKLELMAEISNLKLK 182
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLtGLTPEKLEKELEE---LEKAKEEIEEEISKITAR 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  183 LTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDGERL--QYEKKLKSTKDELASLKEQLEEKECEVKRLQerlvcka 260
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELleEYTAELKRIEKELKEIEEKERKLRKELRELE------- 486

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 49274606  261 kgegiEVLDRDIEVQKMKKAVESLMAANEE-KERKIEDLRQCLSRYRKM 308
Cdd:PRK03918 487 -----KVLKKESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKL 530
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 84-303 2.60e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.50  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    84 EWLQNQMtNGHLPGNGDVYQERLA---RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELL 160
Cdd:pfam07888  30 ELLQNRL-EECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   161 SRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKV----NEMDGERLQYEKKLKSTKDELA 236
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrKEEEAERKQLQAKLQQTEEELR 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49274606   237 SL-------KEQLEEKECEVKRLQERlVCKAKGEGIEVLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLS 303
Cdd:pfam07888 189 SLskefqelRNSLAQRDTQVLQLQDT-ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS 261
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 104-298 2.90e-04

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: 45.06  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleEHREKLNATEEMLQQELlsrTSLETQKLELMAEISNLKLKL 183
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK----EQIKSIEKEIENLNGKK---EELEEELEELEAALRDLESRL 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    184 TAVEKDRLDyedrfrdtegLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVCKAKGE 263
Cdd:TIGR02169  885 GDLKKERDE----------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 49274606    264 GIEVldrdiEVQKMKKAVESL----MAANEEKERKIEDL 298
Cdd:TIGR02169  955 DVQA-----ELQRVEEEIRALepvnMLAIQEYEEVLKRL 988
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
102-316 2.98e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQelLSRTSLETQKLELMAEISnlkl 181
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALLAEAG---- 380

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 182 klTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDGERLQYEKKL--KSTKDELASLKEQLEEKECEVKRLQERLVcK 259
Cdd:COG4717 381 --VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREELA-E 457

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49274606 260 AKGEgIEVLDRDIEVQKMKKAVESLMAANEEKERKI-------EDLRQCLSRYRKMQDPAVLAQ 316
Cdd:COG4717 458 LEAE-LEQLEEDGELAELLQELEELKAELRELAEEWaalklalELLEEAREEYREERLPPVLER 520
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 683-740 3.37e-04

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 39.87  E-value: 3.37e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 49274606 683 VTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRI 740
Cdd:cd09547   6 VSDWLDSIKMGQYKNNFmAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 680-739 3.74e-04

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 39.99  E-value: 3.74e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49274606 680 FNWVTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:cd09552   6 FSTVDEWLDAIKMGQYKESFaNAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMR 66
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 103-298 3.89e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.40  E-value: 3.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    103 QERLARLENDKESLVLQVSVLTDQVEA--------QGEK------IRDLE---FCLEEHREKLNATEEMLQQELLSRTSL 165
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqklQLEKvtteakIKKLEediLLLEDQNSKLSKERKLLEERISEFTSN 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    166 ETQKLELMAEISNLKLKLTAVEKdrlDYEDRFRDTEGLIQEINDLRLKvneMDGERLQYEKKLKSTKDELASLKEQLEEK 245
Cdd:pfam01576  168 LAEEEEKAKSLSKLKNKHEAMIS---DLEERLKKEEKGRQELEKAKRK---LEGESTDLQEQIAELQAQIAELRAQLAKK 241

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 49274606    246 ECEVKRLQERL--VCKAKGEGIEVLdRDIEVQ--KMKKAVESLMAANEEKERKIEDL 298
Cdd:pfam01576  242 EEELQAALARLeeETAQKNNALKKI-RELEAQisELQEDLESERAARNKAEKQRRDL 297
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 103-345 4.13e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.40  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    103 QERLARLENDKESlvlqVSVLTDQVEAQGEKIRDLEFCLEEHrekLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:pfam01576  432 AEKLSKLQSELES----VSSLLNEAEGKNIKLSKDVSSLESQ---LQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQ 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    183 LTAVEKDRLDYEdrfRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQerlvcKAKG 262
Cdd:pfam01576  505 LEEEEEAKRNVE---RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE-----KTKN 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    263 E-GIEVLDRDIEVQKMKKAVESLmaanEEKERKIEDL----RQCLSRYRKMQDPAVlAQGQDSECEGLFHSSSISTLLDA 337
Cdd:pfam01576  577 RlQQELDDLLVDLDHQRQLVSNL----EKKQKKFDQMlaeeKAISARYAEERDRAE-AEAREKETRALSLARALEEALEA 651


                   ....*...
gi 49274606    338 QgfSDLER 345
Cdd:pfam01576  652 K--EELER 657
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
104-300 5.35e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  104 ERLARLENDKESLVLQVSVLTdQVEAQGEKIR----DLEFcLEEHREKLNATEEMLQQELLSR--TSLETQKLELMAEIS 177
Cdd:COG4913  235 DDLERAHEALEDAREQIELLE-PIRELAERYAaareRLAE-LEYLRAALRLWFAQRRLELLEAelEELRAELARLEAELE 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  178 NLKLKLTAVEKDRLDYEDRFRDTEG-----LIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRL 252
Cdd:COG4913  313 RLEARLDALREELDELEAQIRGNGGdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 49274606  253 QERLvcKAKGEGIEVLDRDIEVQKMKkavesLMAANEEKERKIEDLRQ 300
Cdd:COG4913  393 LEAL--EEELEALEEALAEAEAALRD-----LRRELRELEAEIASLER 433
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 141-321 5.80e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 5.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    141 LEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKD---RLDYE-DRFR----DTEGLIQEINDLRL 212
Cdd:pfam01576   31 LEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHElesRLEEEeERSQqlqnEKKKMQQHIQDLEE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    213 KVNEMDGER--LQYEK-----KLKSTKDELASLKEQLEEKECEVKRLQERLvCKAKGEGIEVLDRDIEVQKMKKAVESLM 285
Cdd:pfam01576  111 QLDEEEAARqkLQLEKvtteaKIKKLEEDILLLEDQNSKLSKERKLLEERI-SEFTSNLAEEEEKAKSLSKLKNKHEAMI 189

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 49274606    286 AANEEKERKIEDLRQCLSRY-RKMQDPAVLAQGQDSE 321
Cdd:pfam01576  190 SDLEERLKKEEKGRQELEKAkRKLEGESTDLQEQIAE 226
SAM_Samd3 cd09526
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...
 606-650 6.62e-04

SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. Exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188925  Cd Length: 66  Bit Score: 38.88  E-value: 6.62e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 49274606 606 WTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQ---QDLEKELG 650
Cdd:cd09526   4 WSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDrmvQQLVKKIG 51
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 206-343 7.14e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 7.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 206 EINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQErlvckakgegievldrdievqKMKKAVESLM 285
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---------------------EIDKLQAEIA 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 49274606 286 AANEEKERKIEDLRQclsRYRKMQdpavlAQGQDSeceglfhsSSISTLLDAQGFSDL 343
Cdd:COG3883  76 EAEAEIEERREELGE---RARALY-----RSGGSV--------SYLDVLLGSESFSDF 117
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 166-307 8.13e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 8.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 166 ETQKLELMAEISNLKLKLTAVEKdrldyedrfrdtegliqEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEK 245
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQA-----------------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 246 ECEVKRLQERLVCKAK--------GEGIEVL----------------------DRDI--EVQKMKKAVESLMAANEEKER 293
Cdd:COG3883  78 EAEIEERREELGERARalyrsggsVSYLDVLlgsesfsdfldrlsalskiadaDADLleELKADKAELEAKKAELEAKLA 157

                       170
                ....*....|....
gi 49274606 294 KIEDLRQCLSRYRK 307
Cdd:COG3883 158 ELEALKAELEAAKA 171
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 103-300 1.05e-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: 42.89  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLklk 182
Cdd:pfam10174 309 QTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDL--- 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   183 ltaveKDRLDYEDrfRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKS-------TKDELASLKEQLEEKECEVKRLQER 255
Cdd:pfam10174 386 -----KDMLDVKE--RKINVLQKKIENLQEQLRDKDKQLAGLKERVKSlqtdssnTDTALTTLEEALSEKERIIERLKEQ 458

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 49274606   256 --LVCKAKGEGIEVLDRdiEVQKMKKAVESLMAANEEKERKIEDLRQ 300
Cdd:pfam10174 459 reREDRERLEELESLKK--ENKDLKEKVSALQPELTEKESSLIDLKE 503
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 141-256 1.18e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 39.49  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   141 LEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKlkltAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDGE 220
Cdd:pfam18595   4 LAEEKEELAELERKARELQAKIDALQVVEKDLRSCIKLLE----EIEAELAKLEEAKKKLKELRDALEEKEIELRELERR 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 49274606   221 RLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERL 256
Cdd:pfam18595  80 EERLQRQLENAQEKLERLREQAEEKREAAQARLEEL 115
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 680-738 1.20e-03

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 37.98  E-value: 1.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 680 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 738
Cdd:cd09488   2 FRSVGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 103-306 1.31e-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: 42.50  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLqqellsrTSLETQKLELMAEISNLKLK 182
Cdd:pfam10174 365 TKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQL-------AGLKERVKSLQTDSSNTDTA 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   183 LTAVEKDRLDYEdrfRDTEGLIQEIN-DLRLKVNEMDgerlQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVCKA- 260
Cdd:pfam10174 438 LTTLEEALSEKE---RIIERLKEQRErEDRERLEELE----SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLAs 510

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49274606   261 ----KGEGIEVLDRDIEVQK---------MKKAVESLMAA--NEEKERKIEDLRQCLSRYR 306
Cdd:pfam10174 511 sglkKDSKLKSLEIAVEQKKeecsklenqLKKAHNAEEAVrtNPEINDRIRLLEQEVARYK 571
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 604-652 1.34e-03

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.


Pssm-ID: 188910  Cd Length: 69  Bit Score: 38.04  E-value: 1.34e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 49274606 604 AKWTKEQVCSWLaeQGLGS----YLSSGKHWIISGQTLLQASQQDLEkELGIK 652
Cdd:cd09511   2 AKWSPKQVTDWL--KGLDDclqqYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
53-309 1.52e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   53 EDLRGLLEMMETDEKEglrcqiPDSTAEvLIEWLQNQmtNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQV----- 127
Cdd:PRK03918 217 PELREELEKLEKEVKE------LEELKE-EIEELEKE--LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkelke 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  128 -EAQGEKIRDLEFCLEEHREKLNATEEmlqqeLLSRTSLETQKLE-LMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQ 205
Cdd:PRK03918 288 lKEKAEEYIKLSEFYEEYLDELREIEK-----RLSRLEEEINGIEeRIKELEEKEERLEELKKKLKELEKRLEELEERHE 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  206 EINDLRLKVNEMDG----------------------ERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQerlvcKAKGE 263
Cdd:PRK03918 363 LYEEAKAKKEELERlkkrltgltpeklekeleelekAKEEIEEEISKITARIGELKKEIKELKKAIEELK-----KAKGK 437

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 49274606  264 ----GIEvLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKMQ 309
Cdd:PRK03918 438 cpvcGRE-LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-255 1.55e-03

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: 42.36  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNAteemlqqellsrtsLETQKLELMAEISNLKL 181
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--------------LEEEKEDKALEIKKQEW 455

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49274606    182 KLTAVEKDRLDYEDRFRDTEGLIQEINdlrlkvnemdgerlqyekklkstkDELASLKEQLEEKECEVKRLQER 255
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVE------------------------KELSKLQRELAEAEAQARASEER 505
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 602-667 1.70e-03

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 37.68  E-value: 1.70e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49274606 602 PFAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 667
Cdd:cd09506   1 PVHEWTVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDL-TELGVTRVGHRMNIERALKKL 65
PRK01156 PRK01156
chromosome segregation protein; Provisional
 109-309 2.08e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  109 LENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEE---MLQQELLSRTSLETQKLELMAEISNLKLKLTA 185
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDdynNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  186 VEKDRLDYEDRfrdTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQ-------ERLVC 258
Cdd:PRK01156 268 ELEKNNYYKEL---EERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSvlqkdynDYIKK 344

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 49274606  259 KAKGEGIEVLDRDIEVQKMK-----KAVESLMAANEEKERKIEDLRQCLSRYRKMQ 309
Cdd:PRK01156 345 KSRYDDLNNQILELEGYEMDynsylKSIESLKKKIEEYSKNIERMSAFISEILKIQ 400
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 762-814 2.14e-03

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.70  E-value: 2.14e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 49274606 762 EVQQWTNHRVMEWL-RSVDLAEYAPNLRGSGVHGGLMvlePRFNVETMAQLLNI 814
Cdd:cd09504   1 EVHNWTVEDTVEWLvNSVELPQYVEAFKENGVDGSAL---PRLAVNNPSFLTSV 51
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-307 2.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  104 ERLARLEN--DKESLVLQVSVLTDQVEAQGEK-----IRDLEFCLEEHRE------KLNATEEMLQQELLSRTSLETQKL 170
Cdd:PRK03918 480 KELRELEKvlKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKlkekliKLKGEIKSLKKELEKLEELKKKLA 559

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  171 ELMAEISNLKLKLTAVEK--DRLDYEDrFRDTEGLIQEIND-----LRLKVNEMDGERLqyEKKLKSTKDELASLKEQLE 243
Cdd:PRK03918 560 ELEKKLDELEEELAELLKelEELGFES-VEELEERLKELEPfyneyLELKDAEKELERE--EKELKKLEEELDKAFEELA 636

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606  244 EKECEVKRLQERLVCKAKG------EGI--EVLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 307
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKyseeeyEELreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
SAM_BAR cd09513
SAM domain of BAR subfamily; SAM (sterile alpha motif) domain of BAR (Bifunctional Apoptosis ...
 604-665 2.39e-03

SAM domain of BAR subfamily; SAM (sterile alpha motif) domain of BAR (Bifunctional Apoptosis Regulator) subfamily is a protein-protein interaction domain. In addition to the SAM domain, this type of regulator has a RING finger domain. Proteins of this subfamily are involved in the apoptosis signal network. Their overexpression in human neuronal cells significantly protects cells from a broad range of cell death stimuli. SAM domain can interact with Caspase8, Bcl-2 and Bcl-X resulting in suppression of Bax-induced cell death.


Pssm-ID: 188912  Cd Length: 71  Bit Score: 37.47  E-value: 2.39e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49274606 604 AKWTKEQVCSWLAEQGLGSYLSSGKHWI--ISGQTLLQASQQDLEKE-LGIKHSLHRKKLQLALQ 665
Cdd:cd09513   2 SKWTPEEVVLWLEQLGPWASLYRERFLSenVNGRLLLTLTEEELSKPpFNIENSLHRRAILTELE 66
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 606-667 2.48e-03

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 37.19  E-value: 2.48e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49274606 606 WTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 667
Cdd:cd09534   1 WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEAL-KELGITKVGDRIRLLRAIKSL 61
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 43-334 2.49e-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: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606     43 MGSLRALHLVEDLRGLLEMMETDEKEGLRCQIPDSTAEvliewLQNQMTNGHLPGngdVYQERLARLENDkeslVLQVSV 122
Cdd:TIGR00618  475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-----PNPARQDIDNPG---PLTRRMQRGEQT----YAQLET 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    123 LTDQVEAQGEKIRdlefcleEHREKLNATEEMLQQELLSRTSLETqklELMAEISNLkLKLTAVEKDRLDYEDRFRDTEG 202
Cdd:TIGR00618  543 SEEDVYHQLTSER-------KQRASLKEQMQEIQQSFSILTQCDN---RSKEDIPNL-QNITVRLQDLTEKLSEAEDMLA 611

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    203 LIQ---------EINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVCKakgegievldRDIE 273
Cdd:TIGR00618  612 CEQhallrklqpEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS----------RQLA 681

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49274606    274 VQKMKKAVESLMAANEEKERKIEDLRQC------LSRYRKMQDPAVLAQGQDSECEGLFHSSSISTL 334
Cdd:TIGR00618  682 LQKMQSEKEQLTYWKEMLAQCQTLLRELethieeYDREFNEIENASSSLGSDLAAREDALNQSLKEL 748
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-298 2.72e-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: 41.54  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLnateEMLQQELLSRTS-----------LETQKLE 171
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL----EQKQKELKSKEKelkklneekkeLEEKVKD 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   172 LMAEISNLKLKLTAVEKDRLDYEDRFRDTE--------------------GLIQEINDLRLKVNEMDGERLQYEKKLKST 231
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEdelnkddfelkkenlekeidEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49274606   232 KDELASLKEQLEEKECEVKRLQERL-VCKAKGEGIEVLDRDI---------EVQKMKKAVESLMAANEEKERKIEDL 298
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELeKAKKENEKLSSIIKNIkskknklkqEVKQIKETIKEIRNKWPEIIKKIKES 671
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 187-305 2.90e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 40.29  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   187 EKDRLDyedrfRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEekecEVKRLQERLVckakgegiE 266
Cdd:pfam11932  35 KIDKWD-----DEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIE----EIERTERELV--------P 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 49274606   267 VLDRDIEvqKMKKAVESLMAAN-EEKERKIEDLRQCLSRY 305
Cdd:pfam11932  98 LMLKMLD--RLEQFVALDLPFLlEERQARLARLRELMDDA 135
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
77-308 3.18e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 3.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  77 STAEVLIEwlqnqMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLnateEMLQ 156
Cdd:COG2433 377 SIEEALEE-----LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI----ERLE 447

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 157 QELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDGERLqyeKKLKS-TKDEL 235
Cdd:COG2433 448 RELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPV---KVVEKfTKEAI 524

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 236 ASLKEQLEEKECEV----------KRLQERLVCK------------------AKGEGIEVLD-RDIEVQKM-------KK 279
Cdd:COG2433 525 RRLEEEYGLKEGDVvylrdasgagRSTAELLAEAgpravivpgelseaadevLFEEGIPVLPaEDVTIQEVddlavvdEE 604

                       250       260       270
                ....*....|....*....|....*....|....*
gi 49274606 280 AVESLMAANEE------KERKIEDLRQCLSRYRKM 308
Cdd:COG2433 605 ELEAAIEDWEEraeerrREKKAEMLERLISEYRAE 639
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 604-667 3.19e-03

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 37.23  E-value: 3.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49274606 604 AKWTKEQVCSWLAEQGLGSY--LSSGKHwIISGQTLLQASQQDL-EKELGIKHSLHRKKLQLALQAL 667
Cdd:cd09515   2 HEWTCEDVAKWLKKEGFSKYvdLLCNKH-RIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIRKL 67
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 683-739 3.43e-03

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 36.91  E-value: 3.43e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 49274606 683 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 739
Cdd:cd09505  10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELK 67
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 203-310 4.92e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 4.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 203 LIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLvckAKGEG----------IEVLDRDI 272
Cdd:COG1579  22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---KKYEEqlgnvrnnkeYEALQKEI 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 49274606 273 EVQKMKKAV--ESLMAANEEKERKIEDLRQCLSRYRKMQD 310
Cdd:COG1579  99 ESLKRRISDleDEILELMERIEELEEELAELEAELAELEA 138
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 680-727 4.98e-03

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 36.54  E-value: 4.98e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49274606 680 FNW----VTRWL-DDIGLPQYKTQFDEGRVDGRML--------HYMTVDdllsLKVVSVLH 727
Cdd:cd09504   3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALprlavnnpSFLTSV----LGIKDPIH 59
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
100-312 5.46e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 5.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFC---LEEHREKLNATEEMLQQELLSrtsLETQKlELMAEI 176
Cdd:COG1340  67 DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLS---PEEEK-ELVEKI 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 177 SNLKLKLTAVEKdRLDYEDRFRDTEGLIQEI----NDLRLKVNEMDGERLQYekklkstKDELASLKEQLEEKECEVKRL 252
Cdd:COG1340 143 KELEKELEKAKK-ALEKNEKLKELRAELKELrkeaEEIHKKIKELAEEAQEL-------HEEMIELYKEADELRKEADEL 214

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606 253 QErlvckakgegievldrdiEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKMQDPA 312
Cdd:COG1340 215 HK------------------EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 680-739 5.84e-03

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 36.38  E-value: 5.84e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49274606 680 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 739
Cdd:cd09549   7 FGSVGEWLEALDLCRYKDNFAAaGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
46 PHA02562
endonuclease subunit; Provisional
 41-257 6.13e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   41 PFMGsLRALH---LVEDLR--GLLEMMETDEKE---GLRCQIpdSTAEVLIEWLQNQ--MTNGHLPGNGDVYQERLARLE 110
Cdd:PHA02562 143 PFMQ-LSAPArrkLVEDLLdiSVLSEMDKLNKDkirELNQQI--QTLDMKIDHIQQQikTYNKNIEEQRKKNGENIARKQ 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  111 NDKESLV-------LQVSVLTDQVEA---QGE-------KIRDLEFCLEEHREKLNATEEMLQQELLSRTSleTQKL--- 170
Cdd:PHA02562 220 NKYDELVeeaktikAEIEELTDELLNlvmDIEdpsaalnKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTC--TQQIseg 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  171 -ELMAEI----SNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEK 245
Cdd:PHA02562 298 pDRITKIkdklKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377

                        250
                 ....*....|..
gi 49274606  246 ECEVKRLQERLV 257
Cdd:PHA02562 378 AEELAKLQDELD 389
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 103-306 6.99e-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: 40.34  E-value: 6.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    103 QERLARLENDKESL--VLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLN-------------ATEEMLQQELLSRTSLET 167
Cdd:TIGR00618  239 QQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahikAVTQIEQQAQRIHTELQS 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606    168 QklelMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDGERLQYEKKLKSTKD--ELASLKEQLEEK 245
Cdd:TIGR00618  319 K----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihTLQQQKTTLTQK 394

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49274606    246 E---CEVKRLQERLVCKAKGEGIE---------VLDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYR 306
Cdd:TIGR00618  395 LqslCKELDILQREQATIDTRTSAfrdlqgqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
PRK01156 PRK01156
chromosome segregation protein; Provisional
 108-310 7.96e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  108 RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEM--LQQELLSRTSLETQKLELMAEISNLKLKLTA 185
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYddLNNQILELEGYEMDYNSYLKSIESLKKKIEE 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  186 VEKDRLDYEDRFRDTEGlIQEIN--DLRLKVNEMDGERLQYEKKLKSTKDELASLKEQLEEKECEVKRLQERLVCKAKG- 262
Cdd:PRK01156 382 YSKNIERMSAFISEILK-IQEIDpdAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGt 460

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49274606  263 ----EGIEVLDRD-------IEvQKMKKAVESLMAANEEKERKI--------EDLRQCLSRYRKMQD 310
Cdd:PRK01156 461 tlgeEKSNHIINHynekksrLE-EKIREIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNKIES 526
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 102-254 8.44e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 39.30  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEF-CLEEHREKLNAteemlqqellSRTSLETQKLELMAEISNLK 180
Cdd:pfam15294  98 FEEREFTSSNKKPNFELNKPKLEPLNEGGGSALLHMEIeRLKEENEKLKE----------RLKTLESQATQALDEKSKLE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606   181 LKLTAVEKDRLDYEDRFRDTegliQEINDLRLKVNEM--DGERLQYEKK---------LKSTKDELASLKEQLE--EKEC 247
Cdd:pfam15294 168 KALKDLQKEQGAKKDVKSNL----KEISDLEEKMAALksDLEKTLNASTalqksleedLASTKHELLKVQEQLEmaEKEL 243


                  ....*..
gi 49274606   248 EvKRLQE 254
Cdd:pfam15294 244 E-KKFQQ 249
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-307 9.58e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 9.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  102 YQER-------LARLENDKESLVLQVSvltDQVEAQGEKirDLEFCLEEHREKLNATEEMLQQellsrtsLETQKLELMA 174
Cdd:PRK02224 167 YRERasdarlgVERVLSDQRGSLDQLK---AQIEEKEEK--DLHERLNGLESELAELDEEIER-------YEEQREQARE 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49274606  175 EISNLKLKLTAvekdrldYEDRFRDTEGLIQEINDLRLKVNEMDGERlqyekklKSTKDELASLKEQLEEKECEVKRLQE 254
Cdd:PRK02224 235 TRDEADEVLEE-------HEERREELETLEAEIEDLRETIAETERER-------EELAEEVRDLRERLEELEEERDDLLA 300

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 49274606  255 RLvckakgegiEVLDRDIEVqkMKKAVESLMAANEEKERKIEDLRQCLSRYRK 307
Cdd:PRK02224 301 EA---------GLDDADAEA--VEARREELEDRDEELRDRLEECRVAAQAHNE 342
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH