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Conserved domains on  [gi|1867163749|ref|NP_001372041|]
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polyhomeotic-like protein 2 isoform d [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 ...
 693-812 1.10e-47

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: 1.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 693 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 769
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1867163749 770 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 812
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 812-880 4.24e-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: 4.24e-45
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749 812 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 880
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 116-571 2.15e-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: 71.51  E-value: 2.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  116 SNRQGSTSGSNVSAQAPAQSSSinlaASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMAQP 195
Cdd:PHA03247  2595 SARPRAPVDDRGDPRGPAPPSP----LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL 2670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  196 GNLVQVARSLGGTVPLSPQLIFTPTATVATVQPElgtGSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALK 275
Cdd:PHA03247  2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP---PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  276 P-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqP 354
Cdd:PHA03247  2748 PaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS---P 2824

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  355 HQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPVlqAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPlqcPTA 434
Cdd:PHA03247  2825 AGPLPPPTS---------------AQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP---PVR 2884

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  435 NLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRFQHTSavilQLQPASPVPQQCVPDDWKEVAPGEKSVPETRSG-P 512
Cdd:PHA03247  2885 RLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPP----PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvP 2960

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749  513 SPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMTSGngnsASSIA 571
Cdd:PHA03247  2961 QPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSW----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 ...
 693-812 1.10e-47

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: 1.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 693 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 769
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1867163749 770 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 812
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 812-880 4.24e-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: 4.24e-45
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749 812 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 880
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 816-879 4.27e-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: 4.27e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1867163749 816 KWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKL-GPALKIYARISMLK 879
Cdd:pfam00536   2 GWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLlGHRKKILYAIQRLK 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-571 2.15e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.51  E-value: 2.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  116 SNRQGSTSGSNVSAQAPAQSSSinlaASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMAQP 195
Cdd:PHA03247  2595 SARPRAPVDDRGDPRGPAPPSP----LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL 2670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  196 GNLVQVARSLGGTVPLSPQLIFTPTATVATVQPElgtGSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALK 275
Cdd:PHA03247  2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP---PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  276 P-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqP 354
Cdd:PHA03247  2748 PaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS---P 2824

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  355 HQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPVlqAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPlqcPTA 434
Cdd:PHA03247  2825 AGPLPPPTS---------------AQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP---PVR 2884

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  435 NLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRFQHTSavilQLQPASPVPQQCVPDDWKEVAPGEKSVPETRSG-P 512
Cdd:PHA03247  2885 RLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPP----PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvP 2960

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749  513 SPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMTSGngnsASSIA 571
Cdd:PHA03247  2961 QPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSW----ASSLA 3012
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 814-881 8.20e-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: 8.20e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749  814 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNI-KLGPALKIYARISMLKDS 881
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 221-561 3.46e-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: 47.26  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 221 ATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTP-AAAASGPTPTQPVLPSLALKPTPGGSqPLPTPAQSRNTAQASPA 299
Cdd:pfam17823 111 ASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPrAAACRANASAAPRAAIAAASAPHAAS-PAPRTAASSTTAASSTT 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 300 GAKPGiadsvmephkKGDGNSSVPGSMEGRAGLSrTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQ 379
Cdd:pfam17823 190 AASSA----------PTTAASSAPATLTPARGIS-TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAA 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 380 QQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTanlhkpggSQQCHPPTPDTGPQNGHP 459
Cdd:pfam17823 259 AAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVST--------DQPVHNTAGEPTPSPSNT 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 460 EGVPHTPQRRFQHTSAVILQLQ------PASPVPqqcVPDDwKEVAPGEKSVPETRSGPSPHQQAivTAMPGGLPVPTSP 533
Cdd:pfam17823 331 TLEPNTPKSVASTNLAVVTTTKaqakepSASPVP---VLHT-SMIPEVEATSPTTQPSPLLPTQG--AAGPGILLAPEQV 404

                         330       340
                  ....*....|....*....|....*...
gi 1867163749 534 NIQPSPAHETGQGIVHALTDLSSPGMTS 561
Cdd:pfam17823 405 ATEATAGTASAGPTPRSSGDPKTLAMAS 432
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
91-304 9.51e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 42.82  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  91 AALQQQHLSSAQLQSLAAVQQASLVSNRQGSTSGSNVSAQAPAQSSSINLAASPAAAQLlnrAQSVNSAAASGIAQQAVL 170
Cdd:COG3469     9 SPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAAS---STAATSSTTSTTATATAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 171 LGNTSSPALTASQAQMYLRAQMAQPGNLVQVARSLGGTVPLSPqliFTPTATVATVQPELGTGSPARPPTPAQVQNLTLR 250
Cdd:COG3469    86 AAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSS---TAGSTTTSGASATSSAGSTTTTTTVSGTETATGG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1867163749 251 TQQTPAaaaSGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPG 304
Cdd:COG3469   163 TTTTST---TTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLP 213
 
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 ...
 693-812 1.10e-47

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: 1.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 693 NVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQ---PTGTVPLSVTAALQLTHSQEDSSRCSDNSSY 769
Cdd:pfam16616   1 NVGCTKRVGLFHPDRSKLQKEGAEAHNRRRASKRSLSNLSKEAKKQkpsPQQSQGGSVSSPLLSQPSQEESSRCSDNSSY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1867163749 770 EEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPS 812
Cdd:pfam16616  81 EEPPSPLSAASSGSRRRRGERGLEPPDVHPRDLPGLGHHFLPS 123
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 812-880 4.24e-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: 4.24e-45
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749 812 SEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKD 880
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 814-877 1.44e-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: 1.44e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867163749 814 PTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISM 877
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 ...
 815-876 2.66e-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: 2.66e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1867163749 815 TKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARIS 876
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 ...
 814-879 3.18e-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: 3.18e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867163749 814 PTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 879
Cdd:cd09582     1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Atherin-like cd09583
SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ...
 814-878 4.39e-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: 4.39e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1867163749 814 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISML 878
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 ...
 812-879 2.49e-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: 2.49e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 812 SEPTKWNVEDVYEFIRSL--PGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 879
Cdd:cd09578     2 KDPSTWSVEDVVQFIKEAdpQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLK 71
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 816-879 4.27e-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: 4.27e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1867163749 816 KWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKL-GPALKIYARISMLK 879
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 ...
 810-879 5.42e-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: 5.42e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 810 LPSEPTKWNVEDVYEFIRSlPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 879
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 ...
 814-879 9.07e-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: 9.07e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867163749 814 PTKWNVEDVYEFIRsLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLK 879
Cdd:cd09580     1 PSTWGVKDVSQFLR-ENDCGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLK 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-571 2.15e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.51  E-value: 2.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  116 SNRQGSTSGSNVSAQAPAQSSSinlaASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMAQP 195
Cdd:PHA03247  2595 SARPRAPVDDRGDPRGPAPPSP----LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL 2670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  196 GNLVQVARSLGGTVPLSPQLIFTPTATVATVQPElgtGSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALK 275
Cdd:PHA03247  2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP---PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  276 P-TPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAqlqP 354
Cdd:PHA03247  2748 PaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS---P 2824

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  355 HQLLPQPSSkhlqpqfviqqqpqpQQQQPPPQQSRPVlqAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPlqcPTA 434
Cdd:PHA03247  2825 AGPLPPPTS---------------AQPTAPPPPPGPP--PPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP---PVR 2884

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  435 NLHKPGGSQQCHP-PTPDTGPQNGHPEGVPHTPQRRFQHTSavilQLQPASPVPQQCVPDDWKEVAPGEKSVPETRSG-P 512
Cdd:PHA03247  2885 RLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPP----PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvP 2960

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749  513 SPHQQAIVtamPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMTSGngnsASSIA 571
Cdd:PHA03247  2961 QPWLGALV---PGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSW----ASSLA 3012
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 814-881 8.20e-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: 8.20e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749  814 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNI-KLGPALKIYARISMLKDS 881
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
 184-539 9.17e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 9.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  184 AQMYLRAQMAQPGNLVQVARSLGGTVPLSPQLIFTPTATVATVQPELGTGSPARPPTPAQVQNLtlrtQQTPAAAASGPT 263
Cdd:PHA03247  2477 APVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHPRMLTWIRGL----EELASDDAGDPP 2552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  264 PTqpvLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGR-------------- 329
Cdd:PHA03247  2553 PP---LPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSplppdthapdpppp 2629

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  330 AGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVL--------------QAE 395
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVgsltsladppppppTPE 2709

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  396 PHPQLASVSPSVALQPSSEAHAMPLGPVTPALPlQCPTANLHKPGGSQQCHPPTPDTGPQNGHPEGVPHTPQRRFqhTSA 475
Cdd:PHA03247  2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL--TRP 2786

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1867163749  476 VILQLQPASP-VPQQCVPDDWKEVAPGEKSVPETRSGPSPHQQAIVTAMPGGLPVPTSPNIQPSP 539
Cdd:PHA03247  2787 AVASLSESREsLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 821-875 5.03e-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: 5.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1867163749 821 DVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARI 875
Cdd:cd09487     1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 817-881 7.36e-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: 7.36e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867163749 817 WNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIK-LGPALKIYARISMLKDS 881
Cdd:cd09505     5 WSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKMK 69
PHA03247 PHA03247
large tegument protein UL36; Provisional
 175-587 1.69e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  175 SSPALTASQAQMYLRAQMAQPGNLVQVARSLGGTVPLSPqlifTPTATVATVQP---------ELGTGSPARPPTPAQVQ 245
Cdd:PHA03247  2578 SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP----LPPDTHAPDPPppspspaanEPDPHPPPTVPPPERPR 2653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  246 NLT----------LRTQQTPAAAASGPT-PTQPVLP-------SLALKPTPGGS-QPLPTPAQSRNTAQASPAGAKPGIA 306
Cdd:PHA03247  2654 DDPapgrvsrprrARRLGRAAQASSPPQrPRRRAARptvgsltSLADPPPPPPTpEPAPHALVSATPLPPGPAAARQASP 2733

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  307 DSVMEPHKKGDGNSSVPGSMEGRAGlSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQ 386
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPATPGGPARPA-RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  387 QSRPVLQAEPHPQLASVSPSVALQPSSeahAMPLGPVTPALPLQCPTAnlhkPGGSQQCHPPTPDTGPQnghPEGVPHTP 466
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTSAQPTAP---PPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAK---PAAPARPP 2882

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  467 QRRFqhtsavilqlqPASPVPQQCVPDDWKEVAPGEKSVPETRSGPSPHQQAIVTAMPGGLPvPTSPNIQPSPAHETGQG 546
Cdd:PHA03247  2883 VRRL-----------ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP-PPPPRPQPPLAPTTDPA 2950

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1867163749  547 ivhaltdlsspgmtsgnGNSASSIAGTAPQNGENKPPQAIV 587
Cdd:PHA03247  2951 -----------------GAGEPSGAVPQPWLGALVPGRVAV 2974
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 221-561 3.46e-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: 47.26  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 221 ATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTP-AAAASGPTPTQPVLPSLALKPTPGGSqPLPTPAQSRNTAQASPA 299
Cdd:pfam17823 111 ASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPrAAACRANASAAPRAAIAAASAPHAAS-PAPRTAASSTTAASSTT 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 300 GAKPGiadsvmephkKGDGNSSVPGSMEGRAGLSrTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQ 379
Cdd:pfam17823 190 AASSA----------PTTAASSAPATLTPARGIS-TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAA 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 380 QQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTanlhkpggSQQCHPPTPDTGPQNGHP 459
Cdd:pfam17823 259 AAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVST--------DQPVHNTAGEPTPSPSNT 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 460 EGVPHTPQRRFQHTSAVILQLQ------PASPVPqqcVPDDwKEVAPGEKSVPETRSGPSPHQQAivTAMPGGLPVPTSP 533
Cdd:pfam17823 331 TLEPNTPKSVASTNLAVVTTTKaqakepSASPVP---VLHT-SMIPEVEATSPTTQPSPLLPTQG--AAGPGILLAPEQV 404

                         330       340
                  ....*....|....*....|....*...
gi 1867163749 534 NIQPSPAHETGQGIVHALTDLSSPGMTS 561
Cdd:pfam17823 405 ATEATAGTASAGPTPRSSGDPKTLAMAS 432
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 816-871 3.79e-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: 3.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1867163749 816 KWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNIKLGPALKI 871
Cdd:cd09528     2 DWTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLI 56
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 195-590 1.26e-04

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: 45.68  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 195 PGNLVqVARSLGGTVPLSPQLIFTPTATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSlal 274
Cdd:pfam05109 400 PKTLI-ITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTS--- 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 275 kPTPGGSqplptpaqsrnTAQASPAGAKPGIADSVMEPhKKGDGNSSVPGSMEGRAGLSRTVPAVAAhpliapayaqlqp 354
Cdd:pfam05109 476 -PTPAGT-----------TSGASPVTPSPSPRDNGTES-KAPDMTSPTSAVTTPTPNATSPTPAVTT------------- 529

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 355 hqllPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPH---PQLASVSPSVAL-QPSSEAHAMPLGPVTPalplQ 430
Cdd:pfam05109 530 ----PTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNatiPTLGKTSPTSAVtTPTPNATSPTVGETSP----Q 601

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 431 CPTANlHKPGGSQQChpPTPDTGPQNGhpEGVPHTPQRRFQHTSAVILQLQPASpvpqqcvpddwkevaPGEKSVPETRS 510
Cdd:pfam05109 602 ANTTN-HTLGGTSST--PVVTSPPKNA--TSAVTTGQHNITSSSTSSMSLRPSS---------------ISETLSPSTSD 661

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 511 GPSPHQQAIVTAMPGGlpvptSPNIQPSPAHETGQGIVHALTDLSSPGMT---SGNGNSASSIAGTAPQNGENKPPQAIV 587
Cdd:pfam05109 662 NSTSHMPLLTSAHPTG-----GENITQVTPASTSTHHVSTSSPAPRPGTTsqaSGPGNSSTSTKPGEVNVTKGTPPKNAT 736


                  ...
gi 1867163749 588 KPQ 590
Cdd:pfam05109 737 SPQ 739
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 814-879 2.61e-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: 2.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163749 814 PTKWNVEDVYEFIRSLpGCQEIAEEFRAQE-IDGQALLLLKEDHLMS-AMNIK-LGPALKIYARISMLK 879
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 ...
 817-879 8.16e-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: 8.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867163749 817 WNVEDVYEFIRSLpGCQEIAEEFRAQEIDGQALLLLKEDHLMSaMNI-KLGPALKIYARISMLK 879
Cdd:cd09534     1 WDEEFVEEWLNEL-NCGQYLDIFEKNLITGDLLLELDKEALKE-LGItKVGDRIRLLRAIKSLR 62
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
91-304 9.51e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 42.82  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  91 AALQQQHLSSAQLQSLAAVQQASLVSNRQGSTSGSNVSAQAPAQSSSINLAASPAAAQLlnrAQSVNSAAASGIAQQAVL 170
Cdd:COG3469     9 SPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAAS---STAATSSTTSTTATATAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 171 LGNTSSPALTASQAQMYLRAQMAQPGNLVQVARSLGGTVPLSPqliFTPTATVATVQPELGTGSPARPPTPAQVQNLTLR 250
Cdd:COG3469    86 AAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSS---TAGSTTTSGASATSSAGSTTTTTTVSGTETATGG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1867163749 251 TQQTPAaaaSGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPG 304
Cdd:COG3469   163 TTTTST---TTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLP 213
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 817-879 9.60e-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: 9.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867163749 817 WNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLmSAMNIK-LGPALKIYARISMLK 879
Cdd:cd09535     3 WSPEQVAEWLLSAGFDDSVCEKFRENEITGDILLELDLEDL-KELDIGsFGKRFKLWNEIKSLR 65
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 235-489 1.13e-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: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 235 PARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPV------------LPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAK 302
Cdd:pfam09770 107 PAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVrtgyekykepepIPDLQVDASLWGVAPKKAAAPAPAPQPAAQPASL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 303 PGIADSVMEPHKkgdgnssVPGSMegRAGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSkHLQPQFVIQQQPQPQQQQ 382
Cdd:pfam09770 187 PAPSRKMMSLEE-------VEAAM--RAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPP-QIQQQQQPQQQPQQPQQH 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 383 PPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPtaNLHKPGGSQQCHPPTPDTGPQNGHPEgv 462
Cdd:pfam09770 257 PGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNP--NRLSAARVGYPQNPQPGVQPAPAHQA-- 332

                         250       260
                  ....*....|....*....|....*..
gi 1867163749 463 pHTPQRRFQHTSAVILQLQPASPVPQQ 489
Cdd:pfam09770 333 -HRQQGSFGRQAPIITHPQQLAQLSEE 358
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 397-548 1.27e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  397 HPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTANLHKPGGSQQCHP----PTPDTGPQnghPEGVPHTPQRRFQH 472
Cdd:PRK10263   314 APITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPgpqtGEPVIAPA---PEGYPQQSQYAQPA 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749  473 TSAVILQLQPASPVPQQCVPDDWKEV-APGEKSVPETRSG---PSPHQQAIVTAMPgGLPVPTSPNIQPSPAHETGQGIV 548
Cdd:PRK10263   391 VQYNEPLQQPVQPQQPYYAPAAEQPAqQPYYAPAPEQPAQqpyYAPAPEQPVAGNA-WQAEEQQSTFAPQSTYQTEQTYQ 469
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
120-303 1.68e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 120 GSTSGSNVSAQAP-AQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAVllgntsSPALTASQAQMYLRAQMAQPGNL 198
Cdd:PRK07003  365 GGAPGGGVPARVAgAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAA------AAAAATRAEAPPAAPAPPATADR 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 199 VQVARSLGGTVPLSPQLIFTPTATVATVQPELGTgSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKPTP 278
Cdd:PRK07003  439 GDDAADGDAPVPAKANARASADSRCDERDAQPPA-DSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS 517

                         170       180
                  ....*....|....*....|....*
gi 1867163749 279 GGSQPLPTPAQSRNTAQASPAGAKP 303
Cdd:PRK07003  518 REDAPAAAAPPAPEARPPTPAAAAP 542
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 107-428 1.74e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 107 AAVQQASLVSNRQGSTSGSNVSAQAPAQSSSINLAASPAAA------QLLNRAQSVNSAAASGIAQQAVLLGNTSsPALT 180
Cdd:PRK07764  471 AAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATlrerwpEILAAVPKRSRKTWAILLPEATVLGVRG-DTLV 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 181 ASQAQMYLRAQMAQPGN---LVQ-VARSLGGTvplspqliFTPTATVATvQPELGTGSPARPPTPAqvqnltLRTQQTPA 256
Cdd:PRK07764  550 LGFSTGGLARRFASPGNaevLVTaLAEELGGD--------WQVEAVVGP-APGAAGGEGPPAPASS------GPPEEAAR 614

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 257 AAASGPTPTQPVlpslalkPTPGGSQPLPTPAQSRNTAQASPAGAKPgiADSVMEPHKKGDGNSSVPGSMEGRAGLSRTV 336
Cdd:PRK07764  615 PAAPAAPAAPAA-------PAPAGAAAAPAEASAAPAPGVAAPEHHP--KHVAVPDASDGGDGWPAKAGGAAPAAPPPAP 685

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 337 PAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPHPQlasvsPSVALQPSSEAH 416
Cdd:PRK07764  686 APAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP-----PDPAGAPAQPPP 760

                         330
                  ....*....|..
gi 1867163749 417 AMPLGPVTPALP 428
Cdd:PRK07764  761 PPAPAPAAAPAA 772
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
210-405 2.61e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 210 PLSPQLIFTPTATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTPAAAaSGPTPTQPVLPSLALKPTPGGSQPLPTPAQ 289
Cdd:PRK12323  399 PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA-PAPAPAPAAAPAAAARPAAAGPRPVAAAAA 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 290 SRNTAQASPAGAKPgiADSVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAQLQPhqLLPQPSSKHLQPQ 369
Cdd:PRK12323  478 AAPARAAPAAAPAP--ADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFET--LAPAPAAAPAPRA 553

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1867163749 370 FVIQQQPQPQQQQPPPQQSRPVLQAEPHPQLASVSP 405
Cdd:PRK12323  554 AAATEPVVAPRPPRASASGLPDMFDGDWPALAARLP 589
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 140-312 3.93e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 140 LAASPAAAQLLNRAQSVNSAAASGI-----------AQQAVLLGNTSSPA----LTASQ-AQMYLRAQMAQPGNLV---- 199
Cdd:PRK14950  253 LAEALLAKDLKAALRTLNAVAADGAdlrqftrdlveYLRQVMLLNSGADRslldLTADEkAALQKVSQIANLEALTkwvk 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 200 -------QVARSLGGTVPLSPQLI---FTPTATVATVQPELGTGSPARPpTPAQVQnltlrtqqTPAAAASGPTPTQPVL 269
Cdd:PRK14950  333 afsqldfQLRTTSYGQLPLELAVIealLVPVPAPQPAKPTAAAPSPVRP-TPAPST--------RPKAAAAANIPPKEPV 403

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1867163749 270 PSLALKPTPG---GSQPLPT--PAQSRNTAQASPAGAKPgIADSVMEP 312
Cdd:PRK14950  404 RETATPPPVPprpVAPPVPHtpESAPKLTRAAIPVDEKP-KYTPPAPP 450
PRK11901 PRK11901
hypothetical protein; Reviewed
 120-300 5.21e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 40.05  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 120 GSTSGSNVSAQAPAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAV------------LLGNTSSpALTASQAQMy 187
Cdd:PRK11901   83 GSSSLSSGNQSSPSAANNTSDGHDASGVKNTAPPQDISAPPISPTPTQAAppqtpngqqrieLPGNISD-ALSQQQGQV- 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 188 lraqmaqpGNLVQVARSLGGTVPlspqlifTPTATVATVQPELGTGSPARPPTPAqvqnltlrtqqtPAAAASGPTPTQP 267
Cdd:PRK11901  161 --------NAASQNAQGNTSTLP-------TAPATVAPSKGAKVPATAETHPTPP------------QKPATKKPAVNHH 213

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1867163749 268 VLPSLALKPTPggsQPLPTPAQSRNTA-QASPAG 300
Cdd:PRK11901  214 KTATVAVPPAT---SGKPKSGAASARAlSSAPAS 244
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 226-568 7.16e-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: 40.14  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 226 VQPELGTGSPARPPTPAQVQnltlrtqqtpaAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPGI 305
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQ-----------AATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 306 AD--SVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAaHPLiaPAYAQLQPHQLLPQP--SSKHLQPQFVIQQQPQPQQQ 381
Cdd:pfam03154 243 PSphPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMP-HSL--QTGPSHMQHPVPPQPfpLTPQSSQSQVPPGPSPAAPG 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 382 QPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPlGPVTPALPLQCPTANLHKPGGSQQCH-------PPTPDTGP 454
Cdd:pfam03154 320 QSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKP-PPTTPIPQLPNPQSHKHPPHLSGPSPfqmnsnlPPPPALKP 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163749 455 QNGHPEGVP---HTPQRRFQHTSavilQLQPASPVPQQCVPDDWKEVAPGEKSVPETRSGPSPHQQAIVTA--MPGGLPV 529
Cdd:pfam03154 399 LSSLSTHHPpsaHPPPLQLMPQS----QQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHpfVPGGPPP 474

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1867163749 530 PTSPNIQPSPAHETGQGIVHALTDLSSPGMTSGNGNSAS 568
Cdd:pfam03154 475 ITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCP 513
 
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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