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Conserved domains on  [gi|199560064|ref|NP_001013187|]
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polyhomeotic-like protein 2 [Rattus norvegicus]

Protein Classification

polyhomeotic family protein( domain architecture ID 13557891)

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

Gene Ontology:  GO:0005515
PubMed:  15928333|11992127

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHC2_SAM_assoc pfam16616
Unstructured region on Polyhomeotic-like protein 1 and 2; PHC2_SAM_assoc is a natively ...
 662-781 1.03e-46

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: 162.44  E-value: 1.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  662 NVGCTKRVGLFHSDRSKLQKAGTTTHNRRRASKASLPTLTKDTKKQ---PSGTVPLSVTAALQLAHSQEDSSRCSDNSSY 738
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 199560064  739 EEPLSPISASSSTSRRRQGQRDLELSDMHMRDLVGMGHHFLPS 781
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 781-849 3.90e-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: 3.90e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199560064 781 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 849
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 141-559 2.51e-06

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.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.46  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  141 AASPAAAQLINRAQSVNSA---TASGL--AQQAVLLGNTSSPALTASQAqmylraqmLIFTPTATVATVQPELGTGSPAR 215
Cdd:pfam05109 370 SGTPSGCENISGAFASNRTfdiTVSGLgtAPKTLIITRTATNATTTTHK--------VIFSKAPESTTTSPTLNTTGFAA 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  216 PPTPAQVQNLTlrtqQTPAAAAAAAASGPAPTQPVLPSLALKPTPSSSQPLPPTPQGRtvvqgspvgakpsvtDNVTEPL 295
Cdd:pfam05109 442 PNTTTGLPSST----HVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPR---------------DNGTESK 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  296 KTDGNSNMEARPGPD-RATVPTVAthqLTAPAYTQLQPHQLLPQPSSKHPQPQFVAQQQPQPPRPTPQVQSQPQLAAVSP 374
Cdd:pfam05109 503 APDMTSPTSAVTTPTpNATSPTPA---VTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSP 579

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  375 SLAL-QPSPEGHAMPLGPVTQalplQCSTAHVHKPGSSQQCHLPTPDSGSQNGHPEGvshapQRRFQHTSAVILQLQPAS 453
Cdd:pfam05109 580 TSAVtTPTPNATSPTVGETSP----QANTTNHTLGGTSSTPVVTSPPKNATSAVTTG-----QHNITSSSTSSMSLRPSS 650

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  454 pvpqqcapddwkevvPAEKSVPVTRPGLSPHQQAIITAIPGGlpgpkSPNIQQCPAHETGQGIVHALTDLSSPGMT---S 530
Cdd:pfam05109 651 ---------------ISETLSPSTSDNSTSHMPLLTSAHPTG-----GENITQVTPASTSTHHVSTSSPAPRPGTTsqaS 710

                         410       420
                  ....*....|....*....|....*....
gi 199560064  531 GNGNSASSITGTAPQNGENKPPQAIVKPQ 559
Cdd:pfam05109 711 GPGNSSTSTKPGEVNVTKGTPPKNATSPQ 739
 
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 ...
 662-781 1.03e-46

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: 162.44  E-value: 1.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  662 NVGCTKRVGLFHSDRSKLQKAGTTTHNRRRASKASLPTLTKDTKKQ---PSGTVPLSVTAALQLAHSQEDSSRCSDNSSY 738
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 199560064  739 EEPLSPISASSSTSRRRQGQRDLELSDMHMRDLVGMGHHFLPS 781
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 781-849 3.90e-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: 3.90e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199560064 781 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 849
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 785-848 4.12e-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: 4.12e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 199560064  785 KWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKL-GPALKIYARISMLK 848
Cdd:pfam00536   2 GWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLlGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 783-850 7.90e-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: 7.90e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199560064   783 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNI-KLGPALKIYARISMLKDS 850
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 141-559 2.51e-06

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: 51.46  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  141 AASPAAAQLINRAQSVNSA---TASGL--AQQAVLLGNTSSPALTASQAqmylraqmLIFTPTATVATVQPELGTGSPAR 215
Cdd:pfam05109 370 SGTPSGCENISGAFASNRTfdiTVSGLgtAPKTLIITRTATNATTTTHK--------VIFSKAPESTTTSPTLNTTGFAA 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  216 PPTPAQVQNLTlrtqQTPAAAAAAAASGPAPTQPVLPSLALKPTPSSSQPLPPTPQGRtvvqgspvgakpsvtDNVTEPL 295
Cdd:pfam05109 442 PNTTTGLPSST----HVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPR---------------DNGTESK 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  296 KTDGNSNMEARPGPD-RATVPTVAthqLTAPAYTQLQPHQLLPQPSSKHPQPQFVAQQQPQPPRPTPQVQSQPQLAAVSP 374
Cdd:pfam05109 503 APDMTSPTSAVTTPTpNATSPTPA---VTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSP 579

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  375 SLAL-QPSPEGHAMPLGPVTQalplQCSTAHVHKPGSSQQCHLPTPDSGSQNGHPEGvshapQRRFQHTSAVILQLQPAS 453
Cdd:pfam05109 580 TSAVtTPTPNATSPTVGETSP----QANTTNHTLGGTSSTPVVTSPPKNATSAVTTG-----QHNITSSSTSSMSLRPSS 650

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  454 pvpqqcapddwkevvPAEKSVPVTRPGLSPHQQAIITAIPGGlpgpkSPNIQQCPAHETGQGIVHALTDLSSPGMT---S 530
Cdd:pfam05109 651 ---------------ISETLSPSTSDNSTSHMPLLTSAHPTG-----GENITQVTPASTSTHHVSTSSPAPRPGTTsqaS 710

                         410       420
                  ....*....|....*....|....*....
gi 199560064  531 GNGNSASSITGTAPQNGENKPPQAIVKPQ 559
Cdd:pfam05109 711 GPGNSSTSTKPGEVNVTKGTPPKNATSPQ 739
PHA03247 PHA03247
large tegument protein UL36; Provisional
 197-530 8.34e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  197 PTATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTPAAAAAAAASGP-APTQPVLPSlALKPTPSSSQPLP----PTPQ 271
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqRPRRRAARP-TVGSLTSLADPPPppptPEPA 2711

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  272 GRTVVQGSPVGAKPSVTDNVTEPLK-------------TDGNSNMEARP----GPDRATVPTV----ATHQLTAPAYTQL 330
Cdd:PHA03247 2712 PHALVSATPLPPGPAAARQASPALPaapappavpagpaTPGGPARPARPpttaGPPAPAPPAApaagPPRRLTRPAVASL 2791

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  331 QPH-QLLPQPSSKHPQPQFVAQQQPQPPRPTPQVQSQPQLAAVSPSLALQPSP--------EGHAMPLGPVTQALPLQCS 401
Cdd:PHA03247 2792 SESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGppppslplGGSVAPGGDVRRRPPSRSP 2871

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  402 TAHVHKPGSSQQCHLPTPDSGSQNGHPEGVSHAPQRRFQHTSAVILQLQPASPVPQQCAPDDWKEVVPAEKSVPVTRPGL 481
Cdd:PHA03247 2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG 2951

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 199560064  482 SPHQQAIITA------IPGGLPGPKSPNIQQCPAHETGQGIVHALTDLSSPGMTS 530
Cdd:PHA03247 2952 AGEPSGAVPQpwlgalVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006
 
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 ...
 662-781 1.03e-46

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: 162.44  E-value: 1.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  662 NVGCTKRVGLFHSDRSKLQKAGTTTHNRRRASKASLPTLTKDTKKQ---PSGTVPLSVTAALQLAHSQEDSSRCSDNSSY 738
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 199560064  739 EEPLSPISASSSTSRRRQGQRDLELSDMHMRDLVGMGHHFLPS 781
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 781-849 3.90e-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: 3.90e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199560064 781 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 849
Cdd:cd09577    1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 783-846 1.38e-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: 1.38e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 199560064 783 PTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISM 846
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 ...
 784-845 2.56e-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: 2.56e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 199560064 784 TKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARIS 845
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 ...
 783-848 3.07e-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: 3.07e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 199560064 783 PTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 848
Cdd:cd09582    1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Atherin-like cd09583
SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ...
 783-847 4.23e-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: 4.23e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 199560064 783 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISML 847
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 ...
 781-848 2.40e-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: 2.40e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064 781 SEPTKWNVEDVYEFIRSL--PGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 848
Cdd:cd09578    2 KDPSTWSVEDVVQFIKEAdpQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLK 71
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 785-848 4.12e-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: 4.12e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 199560064  785 KWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKL-GPALKIYARISMLK 848
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 ...
 779-848 7.56e-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: 67.47  E-value: 7.56e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064 779 LPSEPTKWNVEDVYEFIRSlPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 848
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 ...
 783-848 8.74e-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: 8.74e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 199560064 783 PTKWNVEDVYEFIRsLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 848
Cdd:cd09580    1 PSTWGVKDVSQFLR-ENDCGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLK 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 783-850 7.90e-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: 7.90e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199560064   783 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNI-KLGPALKIYARISMLKDS 850
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 790-844 4.85e-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: 4.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 199560064 790 DVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARI 844
Cdd:cd09487    1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 141-559 2.51e-06

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: 51.46  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  141 AASPAAAQLINRAQSVNSA---TASGL--AQQAVLLGNTSSPALTASQAqmylraqmLIFTPTATVATVQPELGTGSPAR 215
Cdd:pfam05109 370 SGTPSGCENISGAFASNRTfdiTVSGLgtAPKTLIITRTATNATTTTHK--------VIFSKAPESTTTSPTLNTTGFAA 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  216 PPTPAQVQNLTlrtqQTPAAAAAAAASGPAPTQPVLPSLALKPTPSSSQPLPPTPQGRtvvqgspvgakpsvtDNVTEPL 295
Cdd:pfam05109 442 PNTTTGLPSST----HVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPR---------------DNGTESK 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  296 KTDGNSNMEARPGPD-RATVPTVAthqLTAPAYTQLQPHQLLPQPSSKHPQPQFVAQQQPQPPRPTPQVQSQPQLAAVSP 374
Cdd:pfam05109 503 APDMTSPTSAVTTPTpNATSPTPA---VTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSP 579

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  375 SLAL-QPSPEGHAMPLGPVTQalplQCSTAHVHKPGSSQQCHLPTPDSGSQNGHPEGvshapQRRFQHTSAVILQLQPAS 453
Cdd:pfam05109 580 TSAVtTPTPNATSPTVGETSP----QANTTNHTLGGTSSTPVVTSPPKNATSAVTTG-----QHNITSSSTSSMSLRPSS 650

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  454 pvpqqcapddwkevvPAEKSVPVTRPGLSPHQQAIITAIPGGlpgpkSPNIQQCPAHETGQGIVHALTDLSSPGMT---S 530
Cdd:pfam05109 651 ---------------ISETLSPSTSDNSTSHMPLLTSAHPTG-----GENITQVTPASTSTHHVSTSSPAPRPGTTsqaS 710

                         410       420
                  ....*....|....*....|....*....
gi 199560064  531 GNGNSASSITGTAPQNGENKPPQAIVKPQ 559
Cdd:pfam05109 711 GPGNSSTSTKPGEVNVTKGTPPKNATSPQ 739
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 786-850 7.09e-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: 7.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 199560064 786 WNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIK-LGPALKIYARISMLKDS 850
Cdd:cd09505    5 WSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKMK 69
PHA03247 PHA03247
large tegument protein UL36; Provisional
 197-530 8.34e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  197 PTATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTPAAAAAAAASGP-APTQPVLPSlALKPTPSSSQPLP----PTPQ 271
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqRPRRRAARP-TVGSLTSLADPPPppptPEPA 2711

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  272 GRTVVQGSPVGAKPSVTDNVTEPLK-------------TDGNSNMEARP----GPDRATVPTV----ATHQLTAPAYTQL 330
Cdd:PHA03247 2712 PHALVSATPLPPGPAAARQASPALPaapappavpagpaTPGGPARPARPpttaGPPAPAPPAApaagPPRRLTRPAVASL 2791

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  331 QPH-QLLPQPSSKHPQPQFVAQQQPQPPRPTPQVQSQPQLAAVSPSLALQPSP--------EGHAMPLGPVTQALPLQCS 401
Cdd:PHA03247 2792 SESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGppppslplGGSVAPGGDVRRRPPSRSP 2871

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  402 TAHVHKPGSSQQCHLPTPDSGSQNGHPEGVSHAPQRRFQHTSAVILQLQPASPVPQQCAPDDWKEVVPAEKSVPVTRPGL 481
Cdd:PHA03247 2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG 2951

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 199560064  482 SPHQQAIITA------IPGGLPGPKSPNIQQCPAHETGQGIVHALTDLSSPGMTS 530
Cdd:PHA03247 2952 AGEPSGAVPQpwlgalVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 785-840 3.65e-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: 3.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 199560064 785 KWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKLGPALKI 840
Cdd:cd09528    2 DWTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLI 56
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 783-848 2.51e-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: 2.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199560064 783 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQE-IDGQALLLLKEDHLMS-AMNIK-LGPALKIYARISMLK 848
Cdd:cd09515    1 VHEWTCEDVAKWLKKE-GFSKYVDLLCNKHrIDGKVLLSLTEEDLRSpPLEIKvLGDIKRLWLAIRKLQ 68
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
191-382 7.47e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 7.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064 191 QMLIFTPTATVATVQPELGTGSPARP-PTPAqvqnltlrtqqtPAAAAAAAASGPAPTQPVLPSLALKPTPSSSQPLPPT 269
Cdd:PRK07003 354 RMLAFEPAVTGGGAPGGGVPARVAGAvPAPG------------ARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAAT 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064 270 PQGRTVVQGSPVGAKPSVTDNVTEPLKTDGNSNMEARPGP---DRATVPTVATHQLTAPAYTQLQPHQLLPQPSSKHPQP 346
Cdd:PRK07003 422 RAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSrcdERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSA 501

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 199560064 347 QFVAQQQPQPPRPTPQVQSQPQLAAVSPSLALQPSP 382
Cdd:PRK07003 502 ATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTP 537
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 786-848 7.87e-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: 7.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 199560064 786 WNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNI-KLGPALKIYARISMLK 848
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 ...
 786-848 9.26e-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: 9.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 199560064 786 WNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLmSAMNIK-LGPALKIYARISMLK 848
Cdd:cd09535    3 WSPEQVAEWLLSAGFDDSVCEKFRENEITGDILLELDLEDL-KELDIGsFGKRFKLWNEIKSLR 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 213-507 2.96e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  213 PARPPTPAQvqnltlrTQQTPAAAAAAAASGPAPTQPVLPSLALKPTPSS-----SQPLPPTPQGRTvvqgSPVGAKPSV 287
Cdd:PHA03247 2595 SARPRAPVD-------DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEpdphpPPTVPPPERPRD----DPAPGRVSR 2663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  288 TDNVTEPLKTDGNSNMEARPGPdRATVPTVAThqLTAPAytqlQPHQLLPQPSSKHPQPQFVAQQQPQPPRPTPQVQSQP 367
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPRR-RAARPTVGS--LTSLA----DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALP 2736

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199560064  368 qLAAVSPslalqPSPEGHAMPLGPVTQALPlqcstahvhkpgssqqchlPTPDSGSQNGHPEGVSHAPQRRFQHTSAVIL 447
Cdd:PHA03247 2737 -AAPAPP-----AVPAGPATPGGPARPARP-------------------PTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 199560064  448 QLQ-PASPVPQQCAPDDWKEVVPAEKSVPVTRP-GLSPHQQAIITAIPGGLPGPKSPNIQQC 507
Cdd:PHA03247 2792 SESrESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
 
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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