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Conserved domains on  [gi|120660112|gb|AAI30631|]
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PHC2 protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHC2_SAM_assoc pfam16616
Unstructured region on Polyhomeotic-like protein 1 and 2; PHC2_SAM_assoc is a natively ...
 642-761 7.44e-48

Unstructured region on Polyhomeotic-like protein 1 and 2; PHC2_SAM_assoc is a natively unstructured region on Polyhomeotic-like proteins 1 and 2, that lies immediately upstream of the SAM domain, pfam00536. The function is not known.


:

Pssm-ID: 465202  Cd Length: 123  Bit Score: 165.52  E-value: 7.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  642 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 718
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 120660112  719 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 761
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 761-829 3.66e-45

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: 156.02  E-value: 3.66e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120660112 761 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 829
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 193-520 1.58e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.34  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  193 VQNLTLRTQQTPAAAASGPTPTQPVLPSLALKP-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSV 271
Cdd:PHA03247 2716 VSATPLPPGPAAARQASPALPAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESR 2795

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  272 PGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqPHQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPVlqAEPHPQLAS 351
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAAS---PAGPLPPPTS---------------AQPTAPPPPPGPP--PPSLPLGGS 2855

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  352 VSPSVALQPSSEAHAMPLGPVTPALPlqcPTANLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRFQHTSavilQLQ 430
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSPAAKPAAPARP---PVRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPP----PPQ 2928

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  431 PASPVPQQCVPDDWKEMAPGEKSVPETRSG-PSPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMT 509
Cdd:PHA03247 2929 PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvPQPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVS 3005

                         330
                  ....*....|.
gi 120660112  510 SGngnsASSIA 520
Cdd:PHA03247 3006 SW----ASSLA 3012
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 39-224 7.79e-03

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


The actual alignment was detected with superfamily member cd22539:

Pssm-ID: 425404  Cd Length: 433  Bit Score: 39.50  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  39 RPTGPQISVYSGiPDRQTVQVIQQALHRQPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVSNR 118
Cdd:cd22539   88 RVATAGYVVVAA-PNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASGQLQIIPGTNQQIITTNR 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 119 QGS---TSGSNVSAQA-PAQSSSINLAASPAAAQLLNRAQ----------SVNSAAASGIAQQAVLLGNTSSPALTASQA 184
Cdd:cd22539  167 SGSgniITMPNLLQQAvPIQGLGLANNVLPGQTQFVANVPvalngnitllPVSSVTASFFTNANSYSTTTTTSNMGQQQQ 246

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 120660112 185 QMYLRAQMVQNLTlRTQQTPAAAASGPTPTQPVLPSLALK 224
Cdd:cd22539  247 QILIQPQLVQGGQ-TIQALQAASLPGQTFTTQTISQEALQ 285
 
Name Accession Description Interval E-value
PHC2_SAM_assoc pfam16616
Unstructured region on Polyhomeotic-like protein 1 and 2; PHC2_SAM_assoc is a natively ...
 642-761 7.44e-48

Unstructured region on Polyhomeotic-like protein 1 and 2; PHC2_SAM_assoc is a natively unstructured region on Polyhomeotic-like proteins 1 and 2, that lies immediately upstream of the SAM domain, pfam00536. The function is not known.


Pssm-ID: 465202  Cd Length: 123  Bit Score: 165.52  E-value: 7.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  642 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 718
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 120660112  719 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 761
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 761-829 3.66e-45

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: 156.02  E-value: 3.66e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120660112 761 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 829
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 765-828 4.02e-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: 70.38  E-value: 4.02e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 120660112  765 KWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKL-GPALKIYARISMLK 828
Cdd:pfam00536   2 GWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLlGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 763-830 7.71e-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: 58.46  E-value: 7.71e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120660112   763 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNI-KLGPALKIYARISMLKDS 830
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
 193-520 1.58e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.34  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  193 VQNLTLRTQQTPAAAASGPTPTQPVLPSLALKP-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSV 271
Cdd:PHA03247 2716 VSATPLPPGPAAARQASPALPAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESR 2795

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  272 PGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqPHQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPVlqAEPHPQLAS 351
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAAS---PAGPLPPPTS---------------AQPTAPPPPPGPP--PPSLPLGGS 2855

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  352 VSPSVALQPSSEAHAMPLGPVTPALPlqcPTANLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRFQHTSavilQLQ 430
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSPAAKPAAPARP---PVRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPP----PPQ 2928

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  431 PASPVPQQCVPDDWKEMAPGEKSVPETRSG-PSPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMT 509
Cdd:PHA03247 2929 PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvPQPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVS 3005

                         330
                  ....*....|.
gi 120660112  510 SGngnsASSIA 520
Cdd:PHA03247 3006 SW----ASSLA 3012
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 173-510 5.33e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 46.49  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  173 NTSSPAL---TASQAQMYLRAQMVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASP-- 247
Cdd:pfam17823  96 DLSEPATregAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPap 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  248 ---AGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSrTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQ 324
Cdd:pfam17823 176 rtaASSTTAASSTTAASSAPTTAASSAPATLTPARGIS-TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALA 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  325 PQPQQQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTanlhkpggSQQCHPPTPDTGPQ 404
Cdd:pfam17823 255 TLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVST--------DQPVHNTAGEPTPS 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  405 NGHPEGVPHTPQRRFQHTSAVILQLQPASPVPQQC-VPDDWKEMAPG-EKSVPETRSGPSPHQQAivTAMPGGLPVPTSP 482
Cdd:pfam17823 327 PSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASpVPVLHTSMIPEvEATSPTTQPSPLLPTQG--AAGPGILLAPEQV 404

                         330       340
                  ....*....|....*....|....*...
gi 120660112  483 NIQPSPAHETGQGIVHALTDLSSPGMTS 510
Cdd:pfam17823 405 ATEATAGTASAGPTPRSSGDPKTLAMAS 432
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 39-224 7.79e-03

N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 has been shown to interact with a variety of proteins including myogenin, SMAD3, SUMO1, SF1, TAL1, and UBC. Some 12,000 SP1 binding sites are found in the human genome. SP1 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLF bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1.


Pssm-ID: 411775  Cd Length: 433  Bit Score: 39.50  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  39 RPTGPQISVYSGiPDRQTVQVIQQALHRQPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVSNR 118
Cdd:cd22539   88 RVATAGYVVVAA-PNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASGQLQIIPGTNQQIITTNR 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 119 QGS---TSGSNVSAQA-PAQSSSINLAASPAAAQLLNRAQ----------SVNSAAASGIAQQAVLLGNTSSPALTASQA 184
Cdd:cd22539  167 SGSgniITMPNLLQQAvPIQGLGLANNVLPGQTQFVANVPvalngnitllPVSSVTASFFTNANSYSTTTTTSNMGQQQQ 246

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 120660112 185 QMYLRAQMVQNLTlRTQQTPAAAASGPTPTQPVLPSLALK 224
Cdd:cd22539  247 QILIQPQLVQGGQ-TIQALQAASLPGQTFTTQTISQEALQ 285
 
Name Accession Description Interval E-value
PHC2_SAM_assoc pfam16616
Unstructured region on Polyhomeotic-like protein 1 and 2; PHC2_SAM_assoc is a natively ...
 642-761 7.44e-48

Unstructured region on Polyhomeotic-like protein 1 and 2; PHC2_SAM_assoc is a natively unstructured region on Polyhomeotic-like proteins 1 and 2, that lies immediately upstream of the SAM domain, pfam00536. The function is not known.


Pssm-ID: 465202  Cd Length: 123  Bit Score: 165.52  E-value: 7.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  642 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 718
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 120660112  719 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 761
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 761-829 3.66e-45

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: 156.02  E-value: 3.66e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120660112 761 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 829
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 763-826 1.34e-35

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: 128.75  E-value: 1.34e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120660112 763 PTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISM 826
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 ...
 764-825 2.50e-23

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: 94.05  E-value: 2.50e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 120660112 764 TKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARIS 825
Cdd:cd09579    2 RKWTVDDVCSFIGSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQVA 63
SAM_Scm-like-3MBT3,4 cd09582
SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 763-828 3.00e-23

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: 93.49  E-value: 3.00e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120660112 763 PTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 828
Cdd:cd09582    1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Atherin-like cd09583
SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ...
 763-827 4.13e-19

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: 81.93  E-value: 4.13e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 120660112 763 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISML 827
Cdd:cd09583    1 PSNWSVEDVVQYFKTA-GFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKL 64
SAM_Scm cd09578
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ...
 761-828 2.34e-16

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: 74.38  E-value: 2.34e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 761 SEPTKWNVEDVYEFIRSL--PGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 828
Cdd:cd09578    2 KDPSTWSVEDVVQFIKEAdpQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLK 71
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 765-828 4.02e-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: 70.38  E-value: 4.02e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 120660112  765 KWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKL-GPALKIYARISMLK 828
Cdd:pfam00536   2 GWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLlGHRKKILYAIQRLK 64
SAM_Scm-like-4MBT1,2 cd09581
SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 759-828 5.35e-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: 67.86  E-value: 5.35e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 759 LPSEPTKWNVEDVYEFIRSlPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 828
Cdd:cd09581    8 LDSNPLFWSVDDVVRFIKS-TDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIERVK 76
SAM_Scm-like-4MBT cd09580
SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 763-828 8.53e-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: 66.62  E-value: 8.53e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120660112 763 PTKWNVEDVYEFIRsLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 828
Cdd:cd09580    1 PSTWGVKDVSQFLR-ENDCGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLK 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 763-830 7.71e-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: 58.46  E-value: 7.71e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120660112   763 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNI-KLGPALKIYARISMLKDS 830
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
 193-520 1.58e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.34  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  193 VQNLTLRTQQTPAAAASGPTPTQPVLPSLALKP-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSV 271
Cdd:PHA03247 2716 VSATPLPPGPAAARQASPALPAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESR 2795

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  272 PGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqPHQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPVlqAEPHPQLAS 351
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAAS---PAGPLPPPTS---------------AQPTAPPPPPGPP--PPSLPLGGS 2855

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  352 VSPSVALQPSSEAHAMPLGPVTPALPlqcPTANLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRFQHTSavilQLQ 430
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSPAAKPAAPARP---PVRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPP----PPQ 2928

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  431 PASPVPQQCVPDDWKEMAPGEKSVPETRSG-PSPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMT 509
Cdd:PHA03247 2929 PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvPQPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVS 3005

                         330
                  ....*....|.
gi 120660112  510 SGngnsASSIA 520
Cdd:PHA03247 3006 SW----ASSLA 3012
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 770-824 4.73e-07

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: 47.23  E-value: 4.73e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 120660112 770 DVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARI 824
Cdd:cd09487    1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 766-830 6.92e-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: 44.62  E-value: 6.92e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 120660112 766 WNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIK-LGPALKIYARISMLKDS 830
Cdd:cd09505    5 WSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKMK 69
PHA03247 PHA03247
large tegument protein UL36; Provisional
 208-488 2.00e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  208 ASGPTPTqpvLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGR--------- 278
Cdd:PHA03247 2548 AGDPPPP---LPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSplppdthap 2624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  279 -----AGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVL------------ 341
Cdd:PHA03247 2625 dppppSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVgsltsladpppp 2704

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  342 --QAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPlQCPTANLHKPGGSQQCHPPTPDTGPQNGHPEGVPHTPQRRF 419
Cdd:PHA03247 2705 ppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL 2783

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  420 qhTSAVILQLQPASP-VPQQCVPDDWKEMAPGEKSVPETRSGPSPHQQAIVTAMPGGLPVPTSPNIQPSP 488
Cdd:PHA03247 2784 --TRPAVASLSESREsLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 765-820 3.57e-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: 42.40  E-value: 3.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 120660112 765 KWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKLGPALKI 820
Cdd:cd09528    2 DWTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLI 56
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 173-510 5.33e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 46.49  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  173 NTSSPAL---TASQAQMYLRAQMVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASP-- 247
Cdd:pfam17823  96 DLSEPATregAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPap 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  248 ---AGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSrTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQ 324
Cdd:pfam17823 176 rtaASSTTAASSTTAASSAPTTAASSAPATLTPARGIS-TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALA 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  325 PQPQQQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTanlhkpggSQQCHPPTPDTGPQ 404
Cdd:pfam17823 255 TLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVST--------DQPVHNTAGEPTPS 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  405 NGHPEGVPHTPQRRFQHTSAVILQLQPASPVPQQC-VPDDWKEMAPG-EKSVPETRSGPSPHQQAivTAMPGGLPVPTSP 482
Cdd:pfam17823 327 PSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASpVPVLHTSMIPEvEATSPTTQPSPLLPTQG--AAGPGILLAPEQV 404

                         330       340
                  ....*....|....*....|....*...
gi 120660112  483 NIQPSPAHETGQGIVHALTDLSSPGMTS 510
Cdd:pfam17823 405 ATEATAGTASAGPTPRSSGDPKTLAMAS 432
PHA03247 PHA03247
large tegument protein UL36; Provisional
 200-536 1.12e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  200 TQQTPAAAASGPT--PTQPVLP-------SLALKPTPGGS-QPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNS 269
Cdd:PHA03247 2668 RRLGRAAQASSPPqrPRRRAARptvgsltSLADPPPPPPTpEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  270 SV-PGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPHPQ 348
Cdd:PHA03247 2748 PAtPGGPARPARPPTTAGPPAPAPPAAPAAG---PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  349 LASVSPSVALQPSseAHAMPLGPVTPALPLQCPTAnlhkPGGSQQCHPPTPDTGPQnghPEGVPHTPQRRFqhtsavilq 428
Cdd:PHA03247 2825 AGPLPPPTSAQPT--APPPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAK---PAAPARPPVRRL--------- 2886

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  429 lqPASPVPQQCVPDDWKEMAPGEKSVPETRSGPSPHQQAIVTAMPGGLPvPTSPNIQPSPAHETGQGivhaltdlsspgm 508
Cdd:PHA03247 2887 --ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP-PPPPRPQPPLAPTTDPA------------- 2950

                         330       340
                  ....*....|....*....|....*...
gi 120660112  509 tsgnGNSASSIAGTAPQNGENKPPQAIV 536
Cdd:PHA03247 2951 ----GAGEPSGAVPQPWLGALVPGRVAV 2974
PHA03247 PHA03247
large tegument protein UL36; Provisional
 131-408 1.86e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  131 APAQSSSINLAASPAAAQLLNRAQSVNSAAASgiaqqavllgntSSPALTASQAQMYLRAQMVQNLTLRTQQTPAAAASG 210
Cdd:PHA03247 2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAP------------APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  211 PTPTQPVLPSLALKPTPGGSQPLPTPAQSrntAQASPAGAKPGIADSVMEphkkgdGNSSVPGSMEGRAGLSR---TVPA 287
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAASPAGPLPPPTSA---QPTAPPPPPGPPPPSLPL------GGSVAPGGDVRRRPPSRspaAKPA 2876

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  288 VAAHP----LIAPAYAQLQPHQLLPQPSSKHLQP-------QFVIQQQPQPQQQQPPPQQSRPVLQAEPHPQLASVSpsv 356
Cdd:PHA03247 2877 APARPpvrrLARPAVSRSTESFALPPDQPERPPQpqappppQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG--- 2953

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 120660112  357 alQPSSEAHAMPLGPVTPAlplQCPTANLHKPGGSQQCHPPTPDTGPQNGHP 408
Cdd:PHA03247 2954 --EPSGAVPQPWLGALVPG---RVAVPRFRVPQPAPSREAPASSTPPLTGHS 3000
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 763-828 2.45e-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: 39.93  E-value: 2.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 120660112 763 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQE-IDGQALLLLKEDHLMS-AMNIK-LGPALKIYARISMLK 828
Cdd:cd09515    1 VHEWTCEDVAKWLKKE-GFSKYVDLLCNKHrIDGKVLLSLTEEDLRSpPLEIKvLGDIKRLWLAIRKLQ 68
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 766-828 7.68e-04

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: 38.34  E-value: 7.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120660112 766 WNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNI-KLGPALKIYARISMLK 828
Cdd:cd09534    1 WDEEFVEEWLNEL-NCGQYLDIFEKNLITGDLLLELDKEALKE-LGItKVGDRIRLLRAIKSLR 62
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 766-828 9.03e-04

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 38.31  E-value: 9.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120660112 766 WNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLmSAMNIK-LGPALKIYARISMLK 828
Cdd:cd09535    3 WSPEQVAEWLLSAGFDDSVCEKFRENEITGDILLELDLEDL-KELDIGsFGKRFKLWNEIKSLR 65
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 346-497 1.02e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  346 HPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTANLHKPGGSQQCHP----PTPDTGPQnghPEGVPHTPQRRFQH 421
Cdd:PRK10263  314 APITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPgpqtGEPVIAPA---PEGYPQQSQYAQPA 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  422 TSAVILQLQPASPVPQQCVPDDWKE-MAPGEKSVPETRSG---PSPHQQAIVTAMPgGLPVPTSPNIQPSPAHETGQGIV 497
Cdd:PRK10263  391 VQYNEPLQQPVQPQQPYYAPAAEQPaQQPYYAPAPEQPAQqpyYAPAPEQPVAGNA-WQAEEQQSTFAPQSTYQTEQTYQ 469
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 98-534 1.40e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  98 LSSAQLQSLAAVQQASLVSNRQGSTSGSNVSAQAPAQSSSInlAASPAAAQLLNRAQSVNSAAASGIAQQAvllgntSSP 177
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAA--APAAAPAPAAAAPAAAAAPAPAAAPQPA------PAP 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 178 AlTASQAQMYLRAQMVQNLTLRTQQTPAAAASGPTPTQPVlpslalkPTPGGSQPLPTPAQSRNTAQASPAGAKPGIAds 257
Cdd:PRK07764 436 A-PAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAP-------EPTAAPAPAPPAAPAPAAAPAAPAAPAAPAG-- 505

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 258 vmephkkGDGNSSVPGSM-EGRAGLSRTVPAVAAHPLIAPAYAQLQPHQLL---PQPSSKHLQPQFVIQQQPQPQQQQPP 333
Cdd:PRK07764 506 -------ADDAATLRERWpEILAAVPKRSRKTWAILLPEATVLGVRGDTLVlgfSTGGLARRFASPGNAEVLVTALAEEL 578

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 334 PQQSRPVLQAEPHPQLASVSPSVALQPSS--EAHAMPLGPVTPALPLQCPTANLHKPGGSQQCHPPTPDTGPQNGHPEGV 411
Cdd:PRK07764 579 GGDWQVEAVVGPAPGAAGGEGPPAPASSGppEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVA 658

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 412 PHTPQRRFQHTSAVILQLQPASPVPQQcvpddwkemAPGEKSVPETRSGPSPHQQAIVTAMPGglPVPTSPNIQPSPAHE 491
Cdd:PRK07764 659 VPDASDGGDGWPAKAGGAAPAAPPPAP---------APAAPAAPAGAAPAQPAPAPAATPPAG--QADDPAAQPPQAAQG 727

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 120660112 492 TGQGiVHALTDLSSPGMTSGNGNSASSIAGTAPQNGENKPPQA 534
Cdd:PRK07764 728 ASAP-SPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAA 769
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 200-438 2.71e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.56  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  200 TQQTPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQS-------------------------RNTAQASPAGAKPGI 254
Cdd:pfam09770 103 NRQQPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTgyekykepepipdlqvdaslwgvapKKAAAPAPAPQPAAQ 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  255 ADSVMEPHKKGDGNSSVPGSMegRAGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSkHLQPQFVIQQQPQPQQQQPPP 334
Cdd:pfam09770 183 PASLPAPSRKMMSLEEVEAAM--RAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPP-QIQQQQQPQQQPQQPQQHPGQ 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  335 QQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPtaNLHKPGGSQQCHPPTPDTGPQNGHPEgvpHT 414
Cdd:pfam09770 260 GHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNP--NRLSAARVGYPQNPQPGVQPAPAHQA---HR 334

                         250       260
                  ....*....|....*....|....
gi 120660112  415 PQRRFQHTSAVILQLQPASPVPQQ 438
Cdd:pfam09770 335 QQGSFGRQAPIITHPQQLAQLSEE 358
SP1_N cd22539
N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins ...
 39-224 7.79e-03

N-terminal domain of transcription factor Specificity Protein (SP) 1; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 has been shown to interact with a variety of proteins including myogenin, SMAD3, SUMO1, SF1, TAL1, and UBC. Some 12,000 SP1 binding sites are found in the human genome. SP1 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLF bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1.


Pssm-ID: 411775  Cd Length: 433  Bit Score: 39.50  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112  39 RPTGPQISVYSGiPDRQTVQVIQQALHRQPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVSNR 118
Cdd:cd22539   88 RVATAGYVVVAA-PNLQNQQVLTSLPGVMPNIQYQVIPQFQTVDGQQLQFATTQAQVQQDASGQLQIIPGTNQQIITTNR 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120660112 119 QGS---TSGSNVSAQA-PAQSSSINLAASPAAAQLLNRAQ----------SVNSAAASGIAQQAVLLGNTSSPALTASQA 184
Cdd:cd22539  167 SGSgniITMPNLLQQAvPIQGLGLANNVLPGQTQFVANVPvalngnitllPVSSVTASFFTNANSYSTTTTTSNMGQQQQ 246

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 120660112 185 QMYLRAQMVQNLTlRTQQTPAAAASGPTPTQPVLPSLALK 224
Cdd:cd22539  247 QILIQPQLVQGGQ-TIQALQAASLPGQTFTTQTISQEALQ 285
 
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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