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Conserved domains on  [gi|119627863|gb|EAX07458|]
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polyhomeotic-like 2 (Drosophila), isoform CRA_b [Homo sapiens]

Protein Classification

PHC2_SAM_assoc and SAM_Ph1,2,3 domain-containing protein( domain architecture ID 11244362)

PHC2_SAM_assoc and SAM_Ph1,2,3 domain-containing protein

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 ...
 671-790 9.38e-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: 9.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  671 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 747
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119627863  748 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 790
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 790-858 4.01e-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: 4.01e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627863 790 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 858
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 131-549 2.56e-12

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.12  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  131 APAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMLIFTPTATVATVQPElgt 210
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP--- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  211 GSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKP-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVME 289
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT 2784

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  290 PHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqPHQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPV 369
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS---PAGPLPPPTS---------------AQPTAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  370 lqAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPlqcPTANLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRF 448
Cdd:PHA03247 2847 --PPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP---PVRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQP 2921

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  449 QHTSavilQLQPASPVPQQCVPDDWKEVAPGEKSVPETRSG-PSPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVH 527
Cdd:PHA03247 2922 QPPP----PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvPQPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTP 2994

                         410       420
                  ....*....|....*....|..
gi 119627863  528 ALTDLSSPGMTSGngnsASSIA 549
Cdd:PHA03247 2995 PLTGHSLSRVSSW----ASSLA 3012
 
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 ...
 671-790 9.38e-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: 9.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  671 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 747
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119627863  748 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 790
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 790-858 4.01e-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: 4.01e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627863 790 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 858
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 794-857 4.16e-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: 4.16e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119627863  794 KWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKL-GPALKIYARISMLK 857
Cdd:pfam00536   2 GWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLlGHRKKILYAIQRLK 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
 131-549 2.56e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.12  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  131 APAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMLIFTPTATVATVQPElgt 210
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP--- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  211 GSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKP-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVME 289
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT 2784

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  290 PHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqPHQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPV 369
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS---PAGPLPPPTS---------------AQPTAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  370 lqAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPlqcPTANLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRF 448
Cdd:PHA03247 2847 --PPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP---PVRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQP 2921

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  449 QHTSavilQLQPASPVPQQCVPDDWKEVAPGEKSVPETRSG-PSPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVH 527
Cdd:PHA03247 2922 QPPP----PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvPQPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTP 2994

                         410       420
                  ....*....|....*....|..
gi 119627863  528 ALTDLSSPGMTSGngnsASSIA 549
Cdd:PHA03247 2995 PLTGHSLSRVSSW----ASSLA 3012
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 792-859 7.99e-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: 7.99e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627863   792 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNI-KLGPALKIYARISMLKDS 859
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 199-539 2.35e-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: 48.03  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  199 ATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTP-AAAASGPTPTQPVLPSLALKPTPGGSqPLPTPAQSRNTAQASPA 277
Cdd:pfam17823 111 ASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPrAAACRANASAAPRAAIAAASAPHAAS-PAPRTAASSTTAASSTT 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  278 GAKPGiadsvmephkKGDGNSSVPGSMEGRAGLSrTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQ 357
Cdd:pfam17823 190 AASSA----------PTTAASSAPATLTPARGIS-TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAA 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  358 QQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTanlhkpggSQQCHPPTPDTGPQNGHP 437
Cdd:pfam17823 259 AAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVST--------DQPVHNTAGEPTPSPSNT 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  438 EGVPHTPQRRFQHTSAVILQLQ------PASPVPqqcVPDDwKEVAPGEKSVPETRSGPSPHQQAivTAMPGGLPVPTSP 511
Cdd:pfam17823 331 TLEPNTPKSVASTNLAVVTTTKaqakepSASPVP---VLHT-SMIPEVEATSPTTQPSPLLPTQG--AAGPGILLAPEQV 404

                         330       340
                  ....*....|....*....|....*...
gi 119627863  512 NIQPSPAHETGQGIVHALTDLSSPGMTS 539
Cdd:pfam17823 405 ATEATAGTASAGPTPRSSGDPKTLAMAS 432
 
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 ...
 671-790 9.38e-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: 9.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  671 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 747
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119627863  748 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 790
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 790-858 4.01e-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: 4.01e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627863 790 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 858
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 792-855 1.40e-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: 1.40e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119627863 792 PTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISM 855
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 ...
 793-854 2.59e-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: 2.59e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119627863 793 TKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARIS 854
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 ...
 792-857 3.10e-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: 3.10e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119627863 792 PTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 857
Cdd:cd09582    1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Atherin-like cd09583
SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ...
 792-856 4.27e-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: 4.27e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119627863 792 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISML 856
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 ...
 790-857 2.43e-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: 2.43e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 790 SEPTKWNVEDVYEFIRSL--PGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 857
Cdd:cd09578    2 KDPSTWSVEDVVQFIKEAdpQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLK 71
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 794-857 4.16e-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: 4.16e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119627863  794 KWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKL-GPALKIYARISMLK 857
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 ...
 788-857 5.28e-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: 5.28e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 788 LPSEPTKWNVEDVYEFIRSlPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 857
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 ...
 792-857 8.83e-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: 8.83e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119627863 792 PTKWNVEDVYEFIRsLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 857
Cdd:cd09580    1 PSTWGVKDVSQFLR-ENDCGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLK 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 131-549 2.56e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.12  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  131 APAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMLIFTPTATVATVQPElgt 210
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP--- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  211 GSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKP-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVME 289
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT 2784

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  290 PHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqPHQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPV 369
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS---PAGPLPPPTS---------------AQPTAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  370 lqAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPlqcPTANLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRF 448
Cdd:PHA03247 2847 --PPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP---PVRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQP 2921

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  449 QHTSavilQLQPASPVPQQCVPDDWKEVAPGEKSVPETRSG-PSPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVH 527
Cdd:PHA03247 2922 QPPP----PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvPQPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTP 2994

                         410       420
                  ....*....|....*....|..
gi 119627863  528 ALTDLSSPGMTSGngnsASSIA 549
Cdd:PHA03247 2995 PLTGHSLSRVSSW----ASSLA 3012
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 792-859 7.99e-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: 7.99e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627863   792 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNI-KLGPALKIYARISMLKDS 859
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 799-853 4.90e-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: 4.90e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119627863 799 DVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARI 853
Cdd:cd09487    1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
PHA03247 PHA03247
large tegument protein UL36; Provisional
 196-517 2.63e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  196 TPTATVATVQPELGTGSPARPPTPAQVQNLtlrtQQTPAAAASGPTPTqpvLPSLALKPTPGGSQPLPTPAQSRNTAQAS 275
Cdd:PHA03247 2511 APSRLAPAILPDEPVGEPVHPRMLTWIRGL----EELASDDAGDPPPP---LPPAAPPAAPDRSVPPPRPAPRPSEPAVT 2583

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  276 PAGAKPGIADSVMEPHKKGDGNSSVPGSMEGR--------------AGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSS 341
Cdd:PHA03247 2584 SRARRPDAPPQSARPRAPVDDRGDPRGPAPPSplppdthapdppppSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR 2663

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  342 KHLQPQFVIQQQPQPQQQQPPPQQSRPVL--------------QAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPl 407
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPRRRAARPTVgsltsladppppppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP- 2742

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  408 QCPTANLHKPGGSQQCHPPTPDTGPQNGHPEGVPHTPQRRFqhTSAVILQLQPASP-VPQQCVPDDWKEVAPGEKSVPET 486
Cdd:PHA03247 2743 AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL--TRPAVASLSESREsLPSPWDPADPPAAVLAPAAALPP 2820

                         330       340       350
                  ....*....|....*....|....*....|.
gi 119627863  487 RSGPSPHQQAIVTAMPGGLPVPTSPNIQPSP 517
Cdd:PHA03247 2821 AASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 795-859 7.17e-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: 7.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119627863 795 WNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIK-LGPALKIYARISMLKDS 859
Cdd:cd09505    5 WSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKMK 69
PHA03247 PHA03247
large tegument protein UL36; Provisional
 213-565 1.55e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  213 PARPPTPAQVQNLTLRTQQTPAAAASGPT--PTQPVLP-------SLALKPTPGGS-QPLPTPAQSRNTAQASPAGAKPG 282
Cdd:PHA03247 2652 PRDDPAPGRVSRPRRARRLGRAAQASSPPqrPRRRAARptvgsltSLADPPPPPPTpEPAPHALVSATPLPPGPAAARQA 2731

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  283 IADSVMEPHKKGDGNSSVPGSMEGRAGlSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPP 362
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGPARPA-RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  363 PQQSRPVLQAEPHPQLASVSPSVALQPSSeahAMPLGPVTPALPLQCPTAnlhkPGGSQQCHPPTPDTGPQnghPEGVPH 442
Cdd:PHA03247 2811 VLAPAAALPPAASPAGPLPPPTSAQPTAP---PPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAK---PAAPAR 2880

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  443 TPQRRFqhtsavilqlqPASPVPQQCVPDDWKEVAPGEKSVPETRSGPSPHQQAIVTAMPGGLPvPTSPNIQPSPAHETG 522
Cdd:PHA03247 2881 PPVRRL-----------ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP-PPPPRPQPPLAPTTD 2948

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 119627863  523 QGivhaltdlsspgmtsgnGNSASSIAGTAPQNGENKPPQAIV 565
Cdd:PHA03247 2949 PA-----------------GAGEPSGAVPQPWLGALVPGRVAV 2974
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 199-539 2.35e-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: 48.03  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  199 ATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTP-AAAASGPTPTQPVLPSLALKPTPGGSqPLPTPAQSRNTAQASPA 277
Cdd:pfam17823 111 ASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPrAAACRANASAAPRAAIAAASAPHAAS-PAPRTAASSTTAASSTT 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  278 GAKPGiadsvmephkKGDGNSSVPGSMEGRAGLSrTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQ 357
Cdd:pfam17823 190 AASSA----------PTTAASSAPATLTPARGIS-TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAA 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  358 QQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTanlhkpggSQQCHPPTPDTGPQNGHP 437
Cdd:pfam17823 259 AAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVST--------DQPVHNTAGEPTPSPSNT 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  438 EGVPHTPQRRFQHTSAVILQLQ------PASPVPqqcVPDDwKEVAPGEKSVPETRSGPSPHQQAivTAMPGGLPVPTSP 511
Cdd:pfam17823 331 TLEPNTPKSVASTNLAVVTTTKaqakepSASPVP---VLHT-SMIPEVEATSPTTQPSPLLPTQG--AAGPGILLAPEQV 404

                         330       340
                  ....*....|....*....|....*...
gi 119627863  512 NIQPSPAHETGQGIVHALTDLSSPGMTS 539
Cdd:pfam17823 405 ATEATAGTASAGPTPRSSGDPKTLAMAS 432
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 794-849 3.69e-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: 3.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119627863 794 KWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKLGPALKI 849
Cdd:cd09528    2 DWTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLI 56
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 158-568 9.25e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.06  E-value: 9.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  158 SAAASGIAQQAVLLGNTSSPALTASQAqmylraqmLIFTPTATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTPAAAA 237
Cdd:pfam05109 392 TVSGLGTAPKTLIITRTATNATTTTHK--------VIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPAS 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  238 SGPTPTQPVLPSlalkPTPGGSqplptpaqsrnTAQASPAGAKPGIADSVMEPhKKGDGNSSVPGSMEGRAGLSRTVPAV 317
Cdd:pfam05109 464 TGPTVSTADVTS----PTPAGT-----------TSGASPVTPSPSPRDNGTES-KAPDMTSPTSAVTTPTPNATSPTPAV 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  318 AAhpliapayaqlqphqllPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPH---PQLASVSPSVAL-QPSSEA 393
Cdd:pfam05109 528 TT-----------------PTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNatiPTLGKTSPTSAVtTPTPNA 590

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  394 HAMPLGPVTPalplQCPTANlHKPGGSQQChpPTPDTGPQNGhpEGVPHTPQRRFQHTSAVILQLQPASpvpqqcvpddw 473
Cdd:pfam05109 591 TSPTVGETSP----QANTTN-HTLGGTSST--PVVTSPPKNA--TSAVTTGQHNITSSSTSSMSLRPSS----------- 650

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  474 kevaPGEKSVPETRSGPSPHQQAIVTAMPGGlpvptSPNIQPSPAHETGQGIVHALTDLSSPGMT---SGNGNSASSIAG 550
Cdd:pfam05109 651 ----ISETLSPSTSDNSTSHMPLLTSAHPTG-----GENITQVTPASTSTHHVSTSSPAPRPGTTsqaSGPGNSSTSTKP 721

                         410
                  ....*....|....*...
gi 119627863  551 TAPQNGENKPPQAIVKPQ 568
Cdd:pfam05109 722 GEVNVTKGTPPKNATSPQ 739
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 792-857 2.54e-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: 2.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627863 792 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQE-IDGQALLLLKEDHLMS-AMNIK-LGPALKIYARISMLK 857
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 ...
 795-857 7.96e-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: 7.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119627863 795 WNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNI-KLGPALKIYARISMLK 857
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 ...
 795-857 9.36e-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: 9.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119627863 795 WNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLmSAMNIK-LGPALKIYARISMLK 857
Cdd:cd09535    3 WSPEQVAEWLLSAGFDDSVCEKFRENEITGDILLELDLEDL-KELDIGsFGKRFKLWNEIKSLR 65
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 213-467 1.09e-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: 42.72  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  213 PARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPV------------LPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAK 280
Cdd:pfam09770 107 PAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVrtgyekykepepIPDLQVDASLWGVAPKKAAAPAPAPQPAAQPASL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  281 PGIADSVMEPHKkgdgnssVPGSMegRAGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSkHLQPQFVIQQQPQPQQQQ 360
Cdd:pfam09770 187 PAPSRKMMSLEE-------VEAAM--RAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPP-QIQQQQQPQQQPQQPQQH 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  361 PPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPtaNLHKPGGSQQCHPPTPDTGPQNGHPEgv 440
Cdd:pfam09770 257 PGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNP--NRLSAARVGYPQNPQPGVQPAPAHQA-- 332

                         250       260
                  ....*....|....*....|....*..
gi 119627863  441 pHTPQRRFQHTSAVILQLQPASPVPQQ 467
Cdd:pfam09770 333 -HRQQGSFGRQAPIITHPQQLAQLSEE 358
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 375-526 1.28e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  375 HPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTANLHKPGGSQQCHP----PTPDTGPQnghPEGVPHTPQRRFQH 450
Cdd:PRK10263  314 APITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPgpqtGEPVIAPA---PEGYPQQSQYAQPA 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  451 TSAVILQLQPASPVPQQCVPDDWKEV-APGEKSVPETRSG---PSPHQQAIVTAMPgGLPVPTSPNIQPSPAHETGQGIV 526
Cdd:PRK10263  391 VQYNEPLQQPVQPQQPYYAPAAEQPAqQPYYAPAPEQPAQqpyYAPAPEQPVAGNA-WQAEEQQSTFAPQSTYQTEQTYQ 469
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 139-546 1.88e-03

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: 42.06  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  139 NLAASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMLIFTPTATVATVQPElgtGSPARPPT 218
Cdd:pfam03154 141 NRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQ---GSPATSQP 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  219 PAQVQNltlrTQQTPAAAASGPTPTQPVLPSlalkPTPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNS 298
Cdd:pfam03154 218 PNQTQS----TAAPHTLIQQTPTLHPQRLPS----PHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHM 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  299 SVPGSMEGRAGLSRTvpAVAAHPLIAPAYAQLQPHQLLPQPSSKhlqpqfviqqQPQPQQQQPPPQQSRPVLQAEPHPQL 378
Cdd:pfam03154 290 QHPVPPQPFPLTPQS--SQSQVPPGPSPAAPGQSQQRIHTPPSQ----------SQLQSQQPPREQPLPPAPLSMPHIKP 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  379 ASVSPsVALQPSSEAHAMP---LGPVTPALPLQCPTANLHKPGGSQQCHPPTpdtgpqNGHPEGVPHTPQRrfqhtsavi 455
Cdd:pfam03154 358 PPTTP-IPQLPNPQSHKHPphlSGPSPFQMNSNLPPPPALKPLSSLSTHHPP------SAHPPPLQLMPQS--------- 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  456 lQLQPASPVPQQCVPDDWKEVAPGEKSVPETRSGPSPHQQAIVTA--MPGGLPVPTSPNIQPSPAHETGQGIVHALTDLS 533
Cdd:pfam03154 422 -QQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHpfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASV 500

                         410
                  ....*....|...
gi 119627863  534 SPGMTSGNGNSAS 546
Cdd:pfam03154 501 SSSGPVPAAVSCP 513
PRK10856 PRK10856
cytoskeleton protein RodZ;
133-276 3.55e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.39  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 133 AQSSSINLAASPAAAQLlnraqsvnsaaaSGIAQQAVLLGNTSSPALTASQAqmylraqmliftPTATVATVQPELGTGS 212
Cdd:PRK10856 138 AQQEEITTMADQSSAEL------------SQNSGQSVPLDTSTTTDPATTPA------------PAAPVDTTPTNSQTPA 193

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119627863 213 PARPPTPAQVQnltlrtQQTPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASP 276
Cdd:PRK10856 194 VATAPAPAVDP------QQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQAGVSTPAADP 251
PRK10118 PRK10118
flagellar hook length control protein FliK;
67-273 7.26e-03

flagellar hook length control protein FliK;


Pssm-ID: 236652 [Multi-domain]  Cd Length: 408  Bit Score: 39.85  E-value: 7.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863  67 QPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVSNRQGSTSGSNVSAQAPAQSSSInLAASPAA 146
Cdd:PRK10118  75 VSDKLADLLAQQANLLIPVDETLPVITDEQSLSSPLTPALKTSALAALSKNAQKDEKADDLSDEDLASLSAL-FAMLPGQ 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 147 AQLLNRAQSvnSAAASGIAQQAVLLGNTSSPALTASQAqmyLRAQMLIFTPTATVAT-VQPELGTGSPARPPTP--AQVQ 223
Cdd:PRK10118 154 DNTTPVADA--PSTVLPAEKPTLLTKDMPSAPQDETHT---LSSDEHEKGLTSAQLTtAQPDDAPGTPAQPLTPlaAEAQ 228

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119627863 224 NLTLRTQQ-TPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQ 273
Cdd:PRK10118 229 AKAEVISTpSPVTAAASPTITPHQTQPLPTAAAPVLSAPLGSHEWQQSLSQ 279
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
142-383 7.41e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 7.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 142 ASPAAAQLLNRAQSVNSAAASGIAQQAvllgnTSSPALTASQAqmylraqmliftptATVATVQPELGTGSPARPPTPAQ 221
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPAAAAPA-----PAAPPAAPAAA--------------PAAAAAARAVAAAPARRSPAPEA 432

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 222 VQNLTLRTQQTPAAAaSGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPgiADSVMEPHKKGDGNSSVP 301
Cdd:PRK12323 433 LAAARQASARGPGGA-PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAP--ADDDPPPWEELPPEFASP 509

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 302 GSMEGRAGLSRTVPAVAAHPLIAPAYAQLQPhqLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPHPQLASV 381
Cdd:PRK12323 510 APAQPDAAPAGWVAESIPDPATADPDDAFET--LAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAAR 587


                 ..
gi 119627863 382 SP 383
Cdd:PRK12323 588 LP 589
PRK11901 PRK11901
hypothetical protein; Reviewed
 120-278 7.57e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 39.28  E-value: 7.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 120 GSTSGSNVSAQAPAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAV------------LLGNTSSpALTASQAQMY 187
Cdd:PRK11901  83 GSSSLSSGNQSSPSAANNTSDGHDASGVKNTAPPQDISAPPISPTPTQAAppqtpngqqrieLPGNISD-ALSQQQGQVN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627863 188 LRAQMLIF------TPTATVATVQPELGTGSPARPPTPAqvqnltlrtqqtPAAAASGPTPTQPVLPSLALKPTPggsQP 261
Cdd:PRK11901 162 AASQNAQGntstlpTAPATVAPSKGAKVPATAETHPTPP------------QKPATKKPAVNHHKTATVAVPPAT---SG 226

                        170
                 ....*....|....*...
gi 119627863 262 LPTPAQSRNTA-QASPAG 278
Cdd:PRK11901 227 KPKSGAASARAlSSAPAS 244
 
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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