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Conserved domains on  [gi|1889930747|ref|XP_035696966|]
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polyhomeotic-like protein 3 isoform X13 [Branchiostoma floridae]

Protein Classification

polyhomeotic family protein( domain architecture ID 10176022)

polyhomeotic (Ph) family protein containing a SAM (sterile alpha motif) domain, forms a helical polymer structure via SAM domain interactions, providing a likely mechanism for extension of Polycomb group (PcG) complexes

Gene Ontology:  GO:0005515
PubMed:  15928333|11992127

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 792-860 5.67e-46

SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome.


:

Pssm-ID: 188976  Cd Length: 69  Bit Score: 158.33  E-value: 5.67e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930747 792 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 860
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 63-548 2.71e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.49  E-value: 2.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747   63 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 141
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  142 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 217
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  218 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPV-----QAVPAQQTSPKPTAPSPPITKMEAQH 292
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggpARPARPPTTAGPPAPAPPAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  293 IPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPmgaSSLGSPPPPEAKTGHVHHVHPHVQPPVQPPPPQ 372
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP---AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  373 PVQAHNPQGHAVQAAHVP--PTHIQAAHVQPTHVQPLSQPLPLalathkpvqtapplpqqpplgpsPVAQPSAVPQSASQ 450
Cdd:PHA03247  2858 PGGDVRRRPPSRSPAAKPaaPARPPVRRLARPAVSRSTESFAL-----------------------PPDQPERPPQPQAP 2914

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  451 PRPsalsvLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSpkQNGVTETQTAPQEKPAD 530
Cdd:PHA03247  2915 PPP-----QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG--RVAVPRFRVPQPAPSRE 2987

                          490
                   ....*....|....*...
gi 1889930747  531 PMKSPEPPKEDPPASRSS 548
Cdd:PHA03247  2988 APASSTPPLTGHSLSRVS 3005
 
Name Accession Description Interval E-value
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 792-860 5.67e-46

SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome.


Pssm-ID: 188976  Cd Length: 69  Bit Score: 158.33  E-value: 5.67e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930747 792 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 860
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 797-859 4.36e-12

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: 61.90  E-value: 4.36e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930747 797 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 859
Cdd:pfam00536   3 WSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 794-861 5.17e-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: 58.85  E-value: 5.17e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930747  794 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNM-KLGPALKICARINSLKQD 861
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
 63-548 2.71e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.49  E-value: 2.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747   63 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 141
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  142 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 217
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  218 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPV-----QAVPAQQTSPKPTAPSPPITKMEAQH 292
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggpARPARPPTTAGPPAPAPPAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  293 IPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPmgaSSLGSPPPPEAKTGHVHHVHPHVQPPVQPPPPQ 372
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP---AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  373 PVQAHNPQGHAVQAAHVP--PTHIQAAHVQPTHVQPLSQPLPLalathkpvqtapplpqqpplgpsPVAQPSAVPQSASQ 450
Cdd:PHA03247  2858 PGGDVRRRPPSRSPAAKPaaPARPPVRRLARPAVSRSTESFAL-----------------------PPDQPERPPQPQAP 2914

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  451 PRPsalsvLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSpkQNGVTETQTAPQEKPAD 530
Cdd:PHA03247  2915 PPP-----QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG--RVAVPRFRVPQPAPSRE 2987

                          490
                   ....*....|....*...
gi 1889930747  531 PMKSPEPPKEDPPASRSS 548
Cdd:PHA03247  2988 APASSTPPLTGHSLSRVS 3005
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 256-572 8.99e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 8.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 256 QRPHSRPTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGI 335
Cdd:pfam03154 185 SPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQ 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 336 PMGASSLGSPPPP---EAKTGHVHHVHPHVQPPVQPPPPQPVQAHNP------QGHAVQAAHVPPTHIQAAHVQPTHVQP 406
Cdd:pfam03154 265 PLPQPSLHGQMPPmphSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaaPGQSQQRIHTPPSQSQLQSQQPPREQP 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 407 LSqPLPLALATHKPVQTAPPLPQQPPLG---PSPVAQPSAVPQSASQPRPSA---LSVLPTSQP-------------SQR 467
Cdd:pfam03154 345 LP-PAPLSMPHIKPPPTTPIPQLPNPQShkhPPHLSGPSPFQMNSNLPPPPAlkpLSSLSTHHPpsahppplqlmpqSQQ 423

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 468 QIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVP-SPKQNGVTETQTAPQEKPADPMKSPEPPKEDPPASr 546
Cdd:pfam03154 424 LPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSS- 502

                         330       340
                  ....*....|....*....|....*.
gi 1889930747 547 SSDLPLALNKPQPEKQQPQRAVVKPQ 572
Cdd:pfam03154 503 SGPVPAAVSCPLPPVQIKEEALDEAE 528
 
Name Accession Description Interval E-value
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 792-860 5.67e-46

SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome.


Pssm-ID: 188976  Cd Length: 69  Bit Score: 158.33  E-value: 5.67e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930747 792 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 860
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 794-857 1.32e-34

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.


Pssm-ID: 188908  Cd Length: 64  Bit Score: 126.05  E-value: 1.32e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889930747 794 PARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINS 857
Cdd:cd09509     1 PSKWSVDDVAQFIKSLDGCAEYAEVFREQEIDGQALLLLTEDDLLKGMGLKLGPALKIYNHIVK 64
SAM_Samd7,11 cd09579
SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a ...
 796-855 1.86e-21

SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a protein-protein interaction domain. Phylogenetic analysis suggests that proteins of this subfamily are most closely related to SAM-Ph1,2,3 subfamily of Polycomb group. They are predicted transcriptional repressors in photoreceptor cells and pinealocytes of vertebrates. SAM domain containing protein 11 is also known as Mr-s (major retinal SAM) protein. In mouse, it is predominantly expressed in developing retinal photoreceptors and in adult pineal gland. The SAM domain is involved in homooligomerization of whole proteins (it was shown based on immunoprecipitation assay and mutagenesis), however its repression activity is not due to SAM/SAM interactions but to the C-terminal region.


Pssm-ID: 188978  Cd Length: 68  Bit Score: 88.66  E-value: 1.86e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 796 RWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARI 855
Cdd:cd09579     3 KWTVDDVCSFIGSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQV 62
SAM_Scm-like-3MBT3,4 cd09582
SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 794-859 1.90e-20

SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-3MBT3,4 (Sex comb on midleg, Malignant brain tumor) subfamily proteins (also known as L3mbtl3,4 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are predicted transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain three MBT repeats and Zn finger domain. Murine L3mbtl3 protein of this subfamily is essential for maturation of myeloid progenitor cells during differentiation. Human L3mbtl4 is a potential tumor suppressor gene in breast cancer, while deregulation of L3MBTL3 is associated with neuroblastoma.


Pssm-ID: 188981  Cd Length: 66  Bit Score: 85.79  E-value: 1.90e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930747 794 PARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 859
Cdd:cd09582     1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Scm cd09578
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ...
 793-860 8.93e-20

SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex comb on midleg) subfamily of Polycomb group is a protein-protein interaction domain. Proteins of this subfamily are transcriptional repressors associated with PRC1 complex. This group includes invertebrate Scm protein and chordate Scm homolog 1 and Scm-like 1, 2, 3 proteins. Most have a SAM domain, two MBT repeats, and a DUF3588 domain, except Scm-like 4 proteins which do not have MBT repeats. Originally the Scm protein was described in Drosophila as a regulator required for proper spatial expression of homeotic genes. It plays a major role during early embryogenesis. SAM domains of Scm proteins can interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with SAM domains of Ph (polyhomeotic) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Mammalian Scmh1 protein is known be indispensible member of PRC1 complex; it plays a regulatory role for the complex during meiotic prophase of male sperm cells, and is particularly involved in regulation of chromatin modification at the XY chromatin domain of the pachytene spermatocytes.


Pssm-ID: 188977  Cd Length: 72  Bit Score: 84.01  E-value: 8.93e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 793 NPARWSVEEVWEFIRSLPGCS--DFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 860
Cdd:cd09578     3 DPSTWSVEDVVQFIKEADPQAlaPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72
SAM_Scm-like-4MBT1,2 cd09581
SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 793-860 2.84e-14

SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT1,2 (Sex comb on midleg, Malignant Brain Tumor) subfamily proteins (also known as Sfmbt1,2 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain four MBT repeats and DUF5388 domain. The MBT repeats of the human sfmbt1 protein are responsible for association with the nuclear matrix and for selective binding of H3 histone N-terminal tails, while the exact function of the SAM domain is unclear.


Pssm-ID: 188980  Cd Length: 85  Bit Score: 68.63  E-value: 2.84e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930747 793 NPARWSVEEVWEFIRSlPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 860
Cdd:cd09581    11 NPLFWSVDDVVRFIKS-TDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIERVKV 77
SAM_Scm-like-4MBT cd09580
SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 794-859 3.61e-14

SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT (Sex comb on midleg like, Malignant Brain Tumor) subfamily proteins of the polycomb group is a putative protein-protein interaction domain. Additionally to the SAM domain, most of the proteins of this subfamily have 4 MBT repeats. In Drosophila SAM-Scm-like-4MBT protein (known as dSfmbt) is a member of Pho repressive complex (PhoRC). Additionally to dSfmbt, the PhoRC complex includes Pho or Pho-like proteins. This complex is responsible for HOX (Homeobox) gene silencing: Pho or Pho-like proteins bind DNA and dSmbt binds methylated histones. dSmbt can interact with mono- and di-methylated histones H3 and H4 (however this activity has been shown for the MBT repeats, while exact function of the SAM domain is unclear). Besides interaction with histones, dSmbt can interact with Scm (a member of PRC complex), but this interaction also seems to be SAM domain independent.


Pssm-ID: 188979  Cd Length: 67  Bit Score: 67.78  E-value: 3.61e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930747 794 PARWSVEEVWEFIRsLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 859
Cdd:cd09580     1 PSTWGVKDVSQFLR-ENDCGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLK 65
SAM_Atherin-like cd09583
SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ...
 794-860 5.42e-14

SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin and Atherin-like subfamily proteins is a putative protein-protein and/or protein-lipid interaction domain. In addition to the C-terminal SAM domain, the majority of proteins belonging to this group also have PHD (or Zn finger) domain. As potential members of the polycomb group, these proteins may be involved in regulation of some key regulatory genes during development. Atherin can be recruited by Ruk/CIN85 kinase-binding proteins via its SH3 domains thus participating in the signal transferring kinase cascades. Also, atherin was found associated with low density lipids (LDL) in atherosclerotic lesions in human. It was suggested that atherin plays an essential role in atherogenesis via immobilization of LDL in the arterial wall. SAM domains of atherins are predicted to form polymers. Inhibition of polymer formation could be a potential antiatherosclerotic therapy.


Pssm-ID: 188982  Cd Length: 69  Bit Score: 67.30  E-value: 5.42e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889930747 794 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 860
Cdd:cd09583     1 PSNWSVEDVVQYFKTA-GFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQ 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 797-859 4.36e-12

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: 61.90  E-value: 4.36e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930747 797 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 859
Cdd:pfam00536   3 WSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 794-861 5.17e-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: 58.85  E-value: 5.17e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930747  794 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNM-KLGPALKICARINSLKQD 861
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
 63-548 2.71e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.49  E-value: 2.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747   63 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 141
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  142 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 217
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  218 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPV-----QAVPAQQTSPKPTAPSPPITKMEAQH 292
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggpARPARPPTTAGPPAPAPPAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  293 IPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPmgaSSLGSPPPPEAKTGHVHHVHPHVQPPVQPPPPQ 372
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP---AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  373 PVQAHNPQGHAVQAAHVP--PTHIQAAHVQPTHVQPLSQPLPLalathkpvqtapplpqqpplgpsPVAQPSAVPQSASQ 450
Cdd:PHA03247  2858 PGGDVRRRPPSRSPAAKPaaPARPPVRRLARPAVSRSTESFAL-----------------------PPDQPERPPQPQAP 2914

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  451 PRPsalsvLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSpkQNGVTETQTAPQEKPAD 530
Cdd:PHA03247  2915 PPP-----QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG--RVAVPRFRVPQPAPSRE 2987

                          490
                   ....*....|....*...
gi 1889930747  531 PMKSPEPPKEDPPASRSS 548
Cdd:PHA03247  2988 APASSTPPLTGHSLSRVS 3005
PHA03247 PHA03247
large tegument protein UL36; Provisional
 201-591 5.90e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 60.34  E-value: 5.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  201 PSLPKPAADQQKTTlcRPPAPKPEGyhPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQAVPAQQ---TSPK 277
Cdd:PHA03247  2557 PAAPPAAPDRSVPP--PRPAPRPSE--PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDpppPSPS 2632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  278 PTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPMGA-SSLGSPPPPEaktghVH 356
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSlTSLADPPPPP-----PT 2707

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  357 HVHPHVQPPVQPPPPQPVQAHNPQGHAVQAAHVPPTHIQAAHVQPTHVQPLSQPLPLALATHKPvqtAPPLPQQPPLGPS 436
Cdd:PHA03247  2708 PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAP---PAAPAAGPPRRLT 2784

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  437 PVAQPSAVPQSASQPRPSAlsvlptsqPSQRQIPTPGPQSRLTPPPAQPQRpqsLPPPVSTSAVVSQQAPPRVPSPKQ-- 514
Cdd:PHA03247  2785 RPAVASLSESRESLPSPWD--------PADPPAAVLAPAAALPPAASPAGP---LPPPTSAQPTAPPPPPGPPPPSLPlg 2853

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  515 -----NGVTETQTAPQEKPADPMKSPEPPKED---PPASRSSDlPLALNKPQPEKQQPQRAVVKPQILTHLIDGFIIQEG 586
Cdd:PHA03247  2854 gsvapGGDVRRRPPSRSPAAKPAAPARPPVRRlarPAVSRSTE-SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932


                   ....*
gi 1889930747  587 PQPFP 591
Cdd:PHA03247  2933 PPPPP 2937
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
443-570 1.17e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 52.09  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 443 AVPQSASQPRPSAlSVLPTSQPSQRQIPTPGPQsrltpppaqpqrpqslPPPVSTSAVVSQQAPPRVPSPKQngVTETQT 522
Cdd:PRK14971  382 VFTQPAAAPQPSA-AAAASPSPSQSSAAAQPSA----------------PQSATQPAGTPPTVSVDPPAAVP--VNPPST 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1889930747 523 APQEKPADPMKSPEPPkedpPASRSSDLPLALNKPQPEKQQPQRAVVK 570
Cdd:PRK14971  443 APQAVRPAQFKEEKKI----PVSKVSSLGPSTLRPIQEKAEQATGNIK 486
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 797-860 2.65e-06

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: 45.77  E-value: 2.65e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930747 797 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMK-LGPALKICARINSLKQ 860
Cdd:cd09505     5 WSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKM 68
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 801-856 6.12e-06

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: 44.15  E-value: 6.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930747 801 EVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARIN 856
Cdd:cd09487     1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
797-859 8.38e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.18  E-value: 8.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930747 797 WSVEEVWEFIRSLpGCSDFADEFRSQEIDG-QALMLLKEDHLMsAMNM-KLGPALKICARINSLK 859
Cdd:pfam07647   4 WSLESVADWLRSI-GLEQYTDNFRDQGITGaELLLRLTLEDLK-RLGItSVGHRRKILKKIQELK 66
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 797-859 2.25e-05

SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L subfamily is a putative protein-protein interaction domain. SAM is a widespread domain in signaling proteins. Samd9 is a tumor suppressor gene. It is involved in death signaling of malignant glioblastoma. Samd9 suppression blocks cancer cell death induced by HVJ-E or IFN-beta treatment. Deleterious mutations in Samd9 lead to normophosphatemic familial tumoral calcinosis, a cutaneous disorder characterized by cutaneous calcification or ossification.


Pssm-ID: 188927  Cd Length: 64  Bit Score: 42.79  E-value: 2.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930747 797 WSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSaMNMKLGPALKICARINSLK 859
Cdd:cd09528     3 WTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLIIHSFNELN 64
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
411-565 7.91e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 46.31  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 411 LPLALATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALsvlpTSQPSQrqiptpgpqsrltpppaqpqrpqs 490
Cdd:PRK14971  362 LTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSA----AAQPSA------------------------ 413

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930747 491 lPPPVSTSAVVSQQAPPRVPSPKQngVTETQTAPQEKPADPMKSPEPPkedPPASRSSDLPLALNKPQPEKQQPQ 565
Cdd:PRK14971  414 -PQSATQPAGTPPTVSVDPPAAVP--VNPPSTAPQAVRPAQFKEEKKI---PVSKVSSLGPSTLRPIQEKAEQAT 482
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 256-572 8.99e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 8.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 256 QRPHSRPTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGI 335
Cdd:pfam03154 185 SPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQ 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 336 PMGASSLGSPPPP---EAKTGHVHHVHPHVQPPVQPPPPQPVQAHNP------QGHAVQAAHVPPTHIQAAHVQPTHVQP 406
Cdd:pfam03154 265 PLPQPSLHGQMPPmphSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaaPGQSQQRIHTPPSQSQLQSQQPPREQP 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 407 LSqPLPLALATHKPVQTAPPLPQQPPLG---PSPVAQPSAVPQSASQPRPSA---LSVLPTSQP-------------SQR 467
Cdd:pfam03154 345 LP-PAPLSMPHIKPPPTTPIPQLPNPQShkhPPHLSGPSPFQMNSNLPPPPAlkpLSSLSTHHPpsahppplqlmpqSQQ 423

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 468 QIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVP-SPKQNGVTETQTAPQEKPADPMKSPEPPKEDPPASr 546
Cdd:pfam03154 424 LPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSS- 502

                         330       340
                  ....*....|....*....|....*.
gi 1889930747 547 SSDLPLALNKPQPEKQQPQRAVVKPQ 572
Cdd:pfam03154 503 SGPVPAAVSCPLPPVQIKEEALDEAE 528
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 794-861 5.27e-04

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: 39.16  E-value: 5.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889930747 794 PARWSVEEVWEFIRSLpGCSDFADEFRSQE-IDGQALMLLKEDHLMS-AMNMK-LGPALKICARINSLKQD 861
Cdd:cd09515     1 VHEWTCEDVAKWLKKE-GFSKYVDLLCNKHrIDGKVLLSLTEEDLRSpPLEIKvLGDIKRLWLAIRKLQRQ 70
PHA03378 PHA03378
EBNA-3B; Provisional
 385-562 5.59e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 385 QAAHVPPTHIQAAHVQPTHVQplSQPLPLALATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQP-------RPSALS 457
Cdd:PHA03378  653 QPPQVEITPYKPTWTQIGHIP--YQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPaaatgraRPPAAA 730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 458 VLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRV-PSPKQNgvtetqtaPQEKPAdpmksPE 536
Cdd:PHA03378  731 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQApPAPQQR--------PRGAPT-----PQ 797

                         170       180
                  ....*....|....*....|....*.
gi 1889930747 537 PPKEDPPASRSSDLPLALNKPQPEKQ 562
Cdd:PHA03378  798 PPPQAGPTSMQLMPRAAPGQQGPTKQ 823
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 336-554 7.04e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 336 PMGASSLGSPPPPEAKTGHVHHVHPHVQPPVQPPPPQPVQAhnPQGHAVQAAHVPPTHIQAAHvqptHVQPLSQPLPLAL 415
Cdd:PRK07764  592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA--AAAPAEASAAPAPGVAAPEH----HPKHVAVPDASDG 665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 416 ATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPP-- 493
Cdd:PRK07764  666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPep 745

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930747 494 --PVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEKPADPMKSPEPPKEDPPASRSSDLPLAL 554
Cdd:PRK07764  746 ddPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMEL 808
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 93-562 7.59e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  93 STSPKKTDSstvDKTKSQSSHPVPQAIAIGQPSSAKAVPVQYSPTKQTAPEPPVSKLEAHSSLHLLASHAHHASSRSPTH 172
Cdd:pfam03154 131 SSDPKDIDQ---DNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVP 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 173 DRGISAMSPPFRHSVQWPNG----NRKGSDGLPSLPKPAADQQKTTLCRPPAPKPEGYHPYMGSRGQDTTSPTTPTTVPs 248
Cdd:pfam03154 208 PQGSPATSQPPNQTQSTAAPhtliQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGP- 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 249 ptflqhSQRPHSRPTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPvpvvprpplhnRPATTPPSPTFQQRLPTSP 328
Cdd:pfam03154 287 ------SHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPS-----------QSQLQSQQPPREQPLPPAP 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 329 TVQSMGIPMGASSLGSPPPPEAKtghvhhvhphvqppvqpppPQPVQAHNPQGHAVQAAHVPPTHIQAAHVQPTHVQPLS 408
Cdd:pfam03154 350 LSMPHIKPPPTTPIPQLPNPQSH-------------------KHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSA 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 409 QPLPLALATHkpvqtapplpqqPPLGPSPVAQPSAVPQSASQPrPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRP 488
Cdd:pfam03154 411 HPPPLQLMPQ------------SQQLPPPPAQPPVLTQSQSLP-PPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITP 477

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930747 489 QSLPPPVSTSAVVSQQAPPRVPS----PKQNGVTETQTAPQEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQ 562
Cdd:pfam03154 478 PSGPPTSTSSAMPGIQPPSSASVsssgPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSHASQ 555
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 797-846 8.94e-04

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: 38.44  E-value: 8.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889930747 797 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLG 846
Cdd:cd09501     4 WSVADVQTWLKQI-GFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSG 52
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 797-859 1.05e-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: 37.96  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930747 797 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 859
Cdd:cd09534     1 WDEEFVEEWLNEL-NCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR 62
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
401-571 1.28e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 401 PTHVQPLSQPLPlALATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLP------------TSQPSQRQ 468
Cdd:PRK12323  376 TAAAAPVAQPAP-AAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAaarqasargpggAPAPAPAP 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 469 IPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTE------TQTAPQEKPADPMKSPEPPKEDP 542
Cdd:PRK12323  455 AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEfaspapAQPDAAPAGWVAESIPDPATADP 534

                         170       180
                  ....*....|....*....|....*....
gi 1889930747 543 PASRSSDLPLALNKPQPEKQQPQRAVVKP 571
Cdd:PRK12323  535 DDAFETLAPAPAAAPAPRAAAATEPVVAP 563
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 262-572 3.96e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 262 PTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPMGASS 341
Cdd:PRK07764  419 AAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 342 LGSPPPPEAKTGHVHHVHPHVQPPVQPPPPQPVQAHNPQghaVQAAHVPPTHIQAAHVQPTHVQPLSQP-----LPLALA 416
Cdd:PRK07764  499 APAAPAGADDAATLRERWPEILAAVPKRSRKTWAILLPE---ATVLGVRGDTLVLGFSTGGLARRFASPgnaevLVTALA 575

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 417 -----THKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSL 491
Cdd:PRK07764  576 eelggDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPK 655

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 492 PPPVSTSAVVSQQAPPRVPSPKQngvtETQTAPQEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQRAVVKP 571
Cdd:PRK07764  656 HVAVPDASDGGDGWPAKAGGAAP----AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAP 731


                  .
gi 1889930747 572 Q 572
Cdd:PRK07764  732 S 732
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
388-515 4.15e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 40.91  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 388 HVPPTHIQAaHVQPTHVQPLSQPLPLALATHKPVQTaPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQR 467
Cdd:PRK14971  369 ASGGRGPKQ-HIKPVFTQPAAAPQPSAAAAASPSPS-QSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTAPQA 446

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1889930747 468 QIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQN 515
Cdd:PRK14971  447 VRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAPTGTQK 494
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 381-518 4.70e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 381 GHAVQAAHVPPTHIQAAHVQPTHVQPLSQPLPLALATHKPvqtapplpqqpplgpSPVAQPSAVPQSASQPRPSALSVLP 460
Cdd:PRK07764  386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP---------------AAAPQPAPAPAPAPAPPSPAGNAPA 450

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930747 461 TSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVT 518
Cdd:PRK07764  451 GGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADD 508
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 391-551 5.00e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  391 PTHIQAAHVQPTHVQPLSQPLPLALATHKP-VQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQRQi 469
Cdd:PRK10263   381 PQQSQYAQPAVQYNEPLQQPVQPQQPYYAPaAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQ- 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  470 PTPGPQSRL---TPPPAQPQRPQSLPPPVSTS--AVVSQQAPPRVPSPKQNGVTETQTAPQEKPA-------DPMKSPEP 537
Cdd:PRK10263   460 STYQTEQTYqqpAAQEPLYQQPQPVEQQPVVEpePVVEETKPARPPLYYFEEVEEKRAREREQLAawyqpipEPVKEPEP 539

                          170
                   ....*....|....
gi 1889930747  538 PKEDPPASRSSDLP 551
Cdd:PRK10263   540 IKSSLKAPSVAAVP 553
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 811-860 6.45e-03

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188916  Cd Length: 66  Bit Score: 36.16  E-value: 6.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889930747 811 GCSDFADEFRSQEIDGQALMLLKEDHLMSaMNMKLGPALKICARINSLKQ 860
Cdd:cd09517    13 HLEEYLPVFEREKIDLEALMLLTDEDLQS-LKLPLGPRRKLLNAIAKRKQ 61
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 438-564 6.79e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747  438 VAQPSAVPQSASQPRPSALSV-LPTSQPSQRQIPTPGPQsrlTPPPAQPQRPQSLPP-PVSTSAVVSQQAPPRVPSPKQN 515
Cdd:PRK10263   329 ATQSWAAPVEPVTQTPPVASVdVPPAQPTVAWQPVPGPQ---TGEPVIAPAPEGYPQqSQYAQPAVQYNEPLQQPVQPQQ 405

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1889930747  516 GVTETQTAPQEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQP 564
Cdd:PRK10263   406 PYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQS 454
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 436-560 6.89e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.08  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 436 SPVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSrltppPAQPQRPQSLPPPVSTSAVVSQQ-APPRVPSPKQ 514
Cdd:PRK14951  372 AAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAAS-----APAAPPAAAPPAPVAAPAAAAPAaAPAAAPAAVA 446

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1889930747 515 NGVTETQTAPQEKPADPMK-SPEPPKEDPPASRSSDLPLALNKPQPE 560
Cdd:PRK14951  447 LAPAPPAQAAPETVAIPVRvAPEPAVASAAPAPAAAPAAARLTPTEE 493
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 391-525 6.97e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 40.10  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 391 PTHIQAAHVQPTHVQPLSQPLPlalATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSAlSVLPTSQPSQRQIP 470
Cdd:PHA03269   23 NTNIPIPELHTSAATQKPDPAP---APHQAASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDP-APAPHQAASRAPDP 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1889930747 471 TPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNgvteTQTAPQ 525
Cdd:PHA03269   99 AVAPQLAAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKPDPAAH----TQHSPP 149
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 445-568 8.17e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.70  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 445 PQSASQPRPSALSVLPTSQPSQRQIPTPGPQSrltpppaqPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAP 524
Cdd:PRK14951  366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQA--------AAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAA 437

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1889930747 525 QEKPadPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQRAV 568
Cdd:PRK14951  438 PAAA--PAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAP 479
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
 436-565 9.03e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 39.69  E-value: 9.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930747 436 SPVAQPSAVPQSASQPRP---SALSVLPTSQPSQRQIPTPG---------PQSRLTPPPAQPQRPQSLPPPVSTSA-VVS 502
Cdd:PRK08691  379 SPSAQTAEKETAAKKPQPrpeAETAQTPVQTASAAAMPSEGktagpvsnqENNDVPPWEDAPDEAQTAAGTAQTSAkSIQ 458

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930747 503 QQAPPRVPSPKQNGVTETQTAPQEKPADPMKSPEPPKEDP---PASRSSDLPLALNKPQPEKQQPQ 565
Cdd:PRK08691  459 TASEAETPPENQVSKNKAADNETDAPLSEVPSENPIQATPndeAVETETFAHEAPAEPFYGYGFPD 524
 
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.
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