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Conserved domains on  [gi|1889930739|ref|XP_035696962|]
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polyhomeotic-like protein 2 isoform X9 [Branchiostoma floridae]

Protein Classification

polyhomeotic family protein( domain architecture ID 10176022)

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

Gene Ontology:  GO:0005515
PubMed:  15928333|11992127

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 872-940 4.84e-46

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


:

Pssm-ID: 188976  Cd Length: 69  Bit Score: 158.72  E-value: 4.84e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930739 872 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 940
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 252-660 6.19e-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: 70.35  E-value: 6.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 330
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  331 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 406
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  407 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPV-----QAVPAQQTSPKPTAPSPPITKMEAQH 481
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggpARPARPPTTAGPPAPAPPAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  482 IPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTP--------G 553
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapgG 2860

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  554 PQSR--------LTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEkPADPMKSPEPPKEDPPAS 625
Cdd:PHA03247  2861 DVRRrppsrspaAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP-QPPPPPQPQPPPPPPPRP 2939

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1889930739  626 RSSDLPLALNKPQPEkqqPQRAVVKPQiLTHLIDG 660
Cdd:PHA03247  2940 QPPLAPTTDPAGAGE---PSGAVPQPW-LGALVPG 2970
 
Name Accession Description Interval E-value
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 872-940 4.84e-46

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


Pssm-ID: 188976  Cd Length: 69  Bit Score: 158.72  E-value: 4.84e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930739 872 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 940
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 877-939 4.77e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 61.90  E-value: 4.77e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930739 877 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 939
Cdd:pfam00536   3 WSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-660 6.19e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 70.35  E-value: 6.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 330
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  331 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 406
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  407 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPV-----QAVPAQQTSPKPTAPSPPITKMEAQH 481
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggpARPARPPTTAGPPAPAPPAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  482 IPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTP--------G 553
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapgG 2860

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  554 PQSR--------LTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEkPADPMKSPEPPKEDPPAS 625
Cdd:PHA03247  2861 DVRRrppsrspaAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP-QPPPPPQPQPPPPPPPRP 2939

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1889930739  626 RSSDLPLALNKPQPEkqqPQRAVVKPQiLTHLIDG 660
Cdd:PHA03247  2940 QPPLAPTTDPAGAGE---PSGAVPQPW-LGALVPG 2970
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 874-941 5.66e-11

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 58.85  E-value: 5.66e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930739  874 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNM-KLGPALKICARINSLKQD 941
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 245-642 1.64e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 245 QGSVQALPLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSSTVDKTKSQSSHPVPQAIAIGQPSSAKAVPVQYS 324
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHP 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 325 PTKQTAPEPPVSKLEAHS----SLHLLASHAHHASSRSPTHDRGISAMSPpfrhsvqWPNGNRKGSDGLPSLPKPAADQQ 400
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPlpqpSLHGQMPPMPHSLQTGPSHMQHPVPPQP-------FPLTPQSSQSQVPPGPSPAAPGQ 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 401 KTTLCRPPAPKPEGyhpymgsrgQDTTSPTTPTTVPSPTFLQHSQRPhsrPTQPVQAVPAQQTSPKPTAPSPPITKMEAQ 480
Cdd:pfam03154 321 SQQRIHTPPSQSQL---------QSQQPPREQPLPPAPLSMPHIKPP---PTTPIPQLPNPQSHKHPPHLSGPSPFQMNS 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 481 HIPHHVPVPVVPRPPLHNRPATTPPSPTFQ---QRLPTSP------TVQPSAVPQSASQPRPSALSVLPTSQPSQRQIPT 551
Cdd:pfam03154 389 NLPPPPALKPLSSLSTHHPPSAHPPPLQLMpqsQQLPPPPaqppvlTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFV 468

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 552 PGPQSRLTP----PPAQPQRPQSLPPPVSTSAVVSQQAPprvpspkqnGVTETQTAPQEKPADPMKSPEPPKEDPPASRS 627
Cdd:pfam03154 469 PGGPPPITPpsgpPTSTSSAMPGIQPPSSASVSSSGPVP---------AAVSCPLPPVQIKEEALDEAEEPESPPPPPRS 539

                         410
                  ....*....|....*.
gi 1889930739 628 -SDLPLALNKPQPEKQ 642
Cdd:pfam03154 540 pSPEPTVVNTPSHASQ 555
 
Name Accession Description Interval E-value
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 872-940 4.84e-46

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


Pssm-ID: 188976  Cd Length: 69  Bit Score: 158.72  E-value: 4.84e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930739 872 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 940
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 874-937 1.45e-34

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


Pssm-ID: 188908  Cd Length: 64  Bit Score: 126.05  E-value: 1.45e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889930739 874 PARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINS 937
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 ...
 876-935 2.04e-21

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


Pssm-ID: 188978  Cd Length: 68  Bit Score: 88.66  E-value: 2.04e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 876 RWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARI 935
Cdd:cd09579     3 KWTVDDVCSFIGSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQV 62
SAM_Scm-like-3MBT3,4 cd09582
SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 874-939 2.08e-20

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


Pssm-ID: 188981  Cd Length: 66  Bit Score: 85.79  E-value: 2.08e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930739 874 PARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 939
Cdd:cd09582     1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Scm cd09578
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ...
 873-940 8.95e-20

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


Pssm-ID: 188977  Cd Length: 72  Bit Score: 84.01  E-value: 8.95e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 873 NPARWSVEEVWEFIRSLPGCS--DFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 940
Cdd:cd09578     3 DPSTWSVEDVVQFIKEADPQAlaPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72
SAM_Scm-like-4MBT1,2 cd09581
SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 873-940 3.40e-14

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


Pssm-ID: 188980  Cd Length: 85  Bit Score: 68.63  E-value: 3.40e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930739 873 NPARWSVEEVWEFIRSlPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 940
Cdd:cd09581    11 NPLFWSVDDVVRFIKS-TDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIERVKV 77
SAM_Scm-like-4MBT cd09580
SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 874-939 3.95e-14

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


Pssm-ID: 188979  Cd Length: 67  Bit Score: 67.78  E-value: 3.95e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930739 874 PARWSVEEVWEFIRsLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 939
Cdd:cd09580     1 PSTWGVKDVSQFLR-ENDCGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLK 65
SAM_Atherin-like cd09583
SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ...
 874-940 5.94e-14

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


Pssm-ID: 188982  Cd Length: 69  Bit Score: 67.30  E-value: 5.94e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889930739 874 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 940
Cdd:cd09583     1 PSNWSVEDVVQYFKTA-GFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQ 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 877-939 4.77e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 61.90  E-value: 4.77e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930739 877 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 939
Cdd:pfam00536   3 WSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-660 6.19e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 70.35  E-value: 6.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 330
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  331 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 406
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  407 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPV-----QAVPAQQTSPKPTAPSPPITKMEAQH 481
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggpARPARPPTTAGPPAPAPPAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  482 IPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTP--------G 553
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapgG 2860

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  554 PQSR--------LTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEkPADPMKSPEPPKEDPPAS 625
Cdd:PHA03247  2861 DVRRrppsrspaAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP-QPPPPPQPQPPPPPPPRP 2939

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1889930739  626 RSSDLPLALNKPQPEkqqPQRAVVKPQiLTHLIDG 660
Cdd:PHA03247  2940 QPPLAPTTDPAGAGE---PSGAVPQPW-LGALVPG 2970
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 874-941 5.66e-11

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 58.85  E-value: 5.66e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930739  874 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNM-KLGPALKICARINSLKQD 941
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-631 4.31e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 4.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSSTVDKTKSQSSHPVPQAIAIG------QPSSAKAVPVQYSP 325
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRprrraaRPTVGSLTSLADPP 2702

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  326 TKQTAPEPPVSKLEAHSSLHLLASHAHHASSRSPthdrgISAMSPPFRHSVQWPNG-NRKGSDGLPSLPKPAADQQKTTL 404
Cdd:PHA03247  2703 PPPPTPEPAPHALVSATPLPPGPAAARQASPALP-----AAPAPPAVPAGPATPGGpARPARPPTTAGPPAPAPPAAPAA 2777

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  405 CRPPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRP--TQPVQAVPAQQTSPKPTAPSPPITKMEAQHI 482
Cdd:PHA03247  2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPagPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  483 PHHVPVPVVPRPPLHNRPATTPPSPTfqQRLPtSPTVQPSAVPQSASQPRPSALsvlPTSQPSQRQIPTPGPQSRLTPPP 562
Cdd:PHA03247  2858 PGGDVRRRPPSRSPAAKPAAPARPPV--RRLA-RPAVSRSTESFALPPDQPERP---PQPQAPPPPQPQPQPPPPPQPQP 2931

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889930739  563 AQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNG--VTETQTAPQEKPADPMKSPEPPKEDPPASRSSDLP 631
Cdd:PHA03247  2932 PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGalVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
523-650 1.75e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 51.70  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 523 AVPQSASQPRPSAlSVLPTSQPSQRQIPTPGPQsrltpppaqpqrpqslPPPVSTSAVVSQQAPPRVPSPKQngVTETQT 602
Cdd:PRK14971  382 VFTQPAAAPQPSA-AAAASPSPSQSSAAAQPSA----------------PQSATQPAGTPPTVSVDPPAAVP--VNPPST 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1889930739 603 APQEKPADPMKSPEPPkedpPASRSSDLPLALNKPQPEKQQPQRAVVK 650
Cdd:PRK14971  443 APQAVRPAQFKEEKKI----PVSKVSSLGPSTLRPIQEKAEQATGNIK 486
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 877-940 2.90e-06

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 45.77  E-value: 2.90e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930739 877 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMK-LGPALKICARINSLKQ 940
Cdd:cd09505     5 WSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKM 68
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 881-936 6.69e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.15  E-value: 6.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930739 881 EVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARIN 936
Cdd:cd09487     1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
877-939 9.18e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.18  E-value: 9.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930739 877 WSVEEVWEFIRSLpGCSDFADEFRSQEIDG-QALMLLKEDHLMsAMNM-KLGPALKICARINSLK 939
Cdd:pfam07647   4 WSLESVADWLRSI-GLEQYTDNFRDQGITGaELLLRLTLEDLK-RLGItSVGHRRKILKKIQELK 66
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 877-939 2.46e-05

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


Pssm-ID: 188927  Cd Length: 64  Bit Score: 42.79  E-value: 2.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930739 877 WSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSaMNMKLGPALKICARINSLK 939
Cdd:cd09528     3 WTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLIIHSFNELN 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
 256-632 9.94e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 9.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  256 PPVPPSSanqskPSQSKQLDQSEKRVSTSPKKTDSSTVDKTKSQSSHPVPQAIAI-GQPSSAKAVPVQYSPTKQTAPEPP 334
Cdd:PHA03247  2701 PPPPPPT-----PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAP 2775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  335 VSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQWPNGNRKGSDGLPSLPKPAADQqkttlcrPPAPKPEG 414
Cdd:PHA03247  2776 AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP-------PPPGPPPP 2848

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  415 YHPYMGS---------RGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPV-QAVPAQQTSPKPTAPSPPITKMEAQHIPh 484
Cdd:PHA03247  2849 SLPLGGSvapggdvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFaLPPDQPERPPQPQAPPPPQPQPQPPPPP- 2927

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  485 hvpvpvvprpplhnRPATTPPSPTFQQRlPTSPTVQPSAVPQ-SASQPRPSALSVLPTSQPSQR-QIPTPGPqSRLTPPP 562
Cdd:PHA03247  2928 --------------QPQPPPPPPPRPQP-PLAPTTDPAGAGEpSGAVPQPWLGALVPGRVAVPRfRVPQPAP-SREAPAS 2991

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  563 AQPQRPQSLPPPVS---TSAVVSQQAPPRVPSPKQN----GVTETQTAPQEKPADPMKS------PEPPKEDPPASRSSD 629
Cdd:PHA03247  2992 STPPLTGHSLSRVSswaSSLALHEETDPPPVSLKQTlwppDDTEDSDADSLFDSDSERSdlealdPLPPEPHDPFAHEPD 3071


                   ...
gi 1889930739  630 LPL 632
Cdd:PHA03247  3072 PAT 3074
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 444-630 1.28e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 444 SQRPHSRPTQPVQAV--PAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQP 521
Cdd:PRK07764  608 PPEEAARPAAPAAPAapAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 522 SAVPQSASQPRPSALSVLPTSQPSQRQI--PTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTE 599
Cdd:PRK07764  688 AAPAAPAGAAPAQPAPAPAATPPAGQADdpAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPA 767

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1889930739 600 TQTAPQEKPADPMKSPEPPKEDPPAS-----RSSDL 630
Cdd:PRK07764  768 AAPAAAPPPSPPSEEEEMAEDDAPSMddedrRDAEE 803
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
504-645 2.38e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 44.77  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 504 PPSPTFQQrlPTSPTvQPSAVPQSASQPRPSALsvlpTSQPSQrqiptpgpqsrltpppaqpqrpqslPPPVSTSAVVSQ 583
Cdd:PRK14971  378 HIKPVFTQ--PAAAP-QPSAAAAASPSPSQSSA----AAQPSA-------------------------PQSATQPAGTPP 425

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889930739 584 QAPPRVPSPKQngVTETQTAPQEKPADPMKSPEPPkedPPASRSSDLPLALNKPQPEKQQPQ 645
Cdd:PRK14971  426 TVSVDPPAAVP--VNPPSTAPQAVRPAQFKEEKKI---PVSKVSSLGPSTLRPIQEKAEQAT 482
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 390-631 4.65e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.31  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  390 PSLPKPAADQQKTTLCRPPAPKPEGYHPYMGSRGQDttspttpttvpsptflqHSQRPHSRPTQPVQAVPAQQTSPKPTA 469
Cdd:PRK10263   344 PPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEG-----------------YPQQSQYAQPAVQYNEPLQQPVQPQQP 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  470 PSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQPSAVPQsasqprPSALSVLPTSQPSQRQI 549
Cdd:PRK10263   407 YYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQ------TEQTYQQPAAQEPLYQQ 480

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  550 PTPGPQsrltpppaqpqrpqslPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEKPA-------DPMKSPEPPKEDP 622
Cdd:PRK10263   481 PQPVEQ----------------QPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAawyqpipEPVKEPEPIKSSL 544


                   ....*....
gi 1889930739  623 PASRSSDLP 631
Cdd:PRK10263   545 KAPSVAAVP 553
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
447-651 5.05e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 447 PHSRPTQPVQAVPAQQTSPKPTAPSPPitkmEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQPSAVPQ 526
Cdd:PRK12323  374 PATAAAAPVAQPAPAAAAPAAAAPAPA----APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 527 SASQP--RPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPpvstsavvSQQAPPRVPSPkqngvTETQTAP 604
Cdd:PRK12323  450 PAPAPaaAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPP--------WEELPPEFASP-----APAQPDA 516

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1889930739 605 QEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQRAVVKP 651
Cdd:PRK12323  517 APAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAP 563
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 440-598 5.22e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 440 FLQHSQRPHSRPTQPVQAVPAQQTSPKPTAPSPPITkmeaqhiphhvpvpvvprpplhnrPATTPPSPTFQQRLPTSPTV 519
Cdd:PRK07764  374 LLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAA------------------------PAPAAAAPAAAAAPAPAAAP 429

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930739 520 QPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVT 598
Cdd:PRK07764  430 QPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADD 508
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 874-941 5.77e-04

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 39.16  E-value: 5.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889930739 874 PARWSVEEVWEFIRSLpGCSDFADEFRSQE-IDGQALMLLKEDHLMS-AMNMK-LGPALKICARINSLKQD 941
Cdd:cd09515     1 VHEWTCEDVAKWLKKE-GFSKYVDLLCNKHrIDGKVLLSLTEEDLRSpPLEIKvLGDIKRLWLAIRKLQRQ 70
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
451-635 5.97e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 451 PTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPP---SPTFQQRLPTSPTVQPSAVPQS 527
Cdd:PRK07003  373 PARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPaapAPPATADRGDDAADGDAPVPAK 452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 528 ASQPRPSALSVLP-TSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSpkqngvTETQTAPQE 606
Cdd:PRK07003  453 ANARASADSRCDErDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS------REDAPAAAA 526

                         170       180
                  ....*....|....*....|....*....
gi 1889930739 607 KPAdPMKSPEPPKEDPPASRSSDLPLALN 635
Cdd:PRK07003  527 PPA-PEARPPTPAAAAPAARAGGAAAALD 554
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 877-926 9.79e-04

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 38.44  E-value: 9.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889930739 877 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLG 926
Cdd:cd09501     4 WSVADVQTWLKQI-GFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSG 52
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 877-939 1.15e-03

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 37.96  E-value: 1.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930739 877 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 939
Cdd:cd09534     1 WDEEFVEEWLNEL-NCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR 62
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 245-642 1.64e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 245 QGSVQALPLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSSTVDKTKSQSSHPVPQAIAIGQPSSAKAVPVQYS 324
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHP 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 325 PTKQTAPEPPVSKLEAHS----SLHLLASHAHHASSRSPTHDRGISAMSPpfrhsvqWPNGNRKGSDGLPSLPKPAADQQ 400
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPlpqpSLHGQMPPMPHSLQTGPSHMQHPVPPQP-------FPLTPQSSQSQVPPGPSPAAPGQ 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 401 KTTLCRPPAPKPEGyhpymgsrgQDTTSPTTPTTVPSPTFLQHSQRPhsrPTQPVQAVPAQQTSPKPTAPSPPITKMEAQ 480
Cdd:pfam03154 321 SQQRIHTPPSQSQL---------QSQQPPREQPLPPAPLSMPHIKPP---PTTPIPQLPNPQSHKHPPHLSGPSPFQMNS 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 481 HIPHHVPVPVVPRPPLHNRPATTPPSPTFQ---QRLPTSP------TVQPSAVPQSASQPRPSALSVLPTSQPSQRQIPT 551
Cdd:pfam03154 389 NLPPPPALKPLSSLSTHHPPSAHPPPLQLMpqsQQLPPPPaqppvlTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFV 468

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 552 PGPQSRLTP----PPAQPQRPQSLPPPVSTSAVVSQQAPprvpspkqnGVTETQTAPQEKPADPMKSPEPPKEDPPASRS 627
Cdd:pfam03154 469 PGGPPPITPpsgpPTSTSSAMPGIQPPSSASVSSSGPVP---------AAVSCPLPPVQIKEEALDEAEEPESPPPPPRS 539

                         410
                  ....*....|....*.
gi 1889930739 628 -SDLPLALNKPQPEKQ 642
Cdd:pfam03154 540 pSPEPTVVNTPSHASQ 555
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 449-652 1.67e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 449 SRPTQPVQAVPAQQTsPKPTAPSPPitkmeAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQPSAVPQSA 528
Cdd:PRK07764  598 EGPPAPASSGPPEEA-ARPAAPAAP-----AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 529 SQPRPSALSVLPTSQPSQRQIPTPGPQsrltpppaqpqrpqslPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEKP 608
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAP----------------AQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA 735

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1889930739 609 ADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQRAVVKPQ 652
Cdd:PRK07764  736 DDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 234-626 2.20e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  234 PPALLSQISRGQGSVQALPLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSST-VDKTKSQSSHPVPqaiaiGQ 312
Cdd:PHA03307    97 PASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAgASPAAVASDAASS-----RQ 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  313 PSSAKAVPVQYSPTKQTAPEPPVSKLeahsslhllASHAHHASSRSPTHDRGISAMSPPfrhsvqwPNGNRKGSDGLPSl 392
Cdd:PHA03307   172 AALPLSSPEETARAPSSPPAEPPPST---------PPAAASPRPPRRSSPISASASSPA-------PAPGRSAADDAGA- 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  393 pkpAADQQKTTLCRPPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQAVPAQQTSPKPTAPSP 472
Cdd:PHA03307   235 ---SSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSS 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739  473 PiTKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTfQQRLPTSPTVQPSAVPQSASQPRPSALSVLPTSQPSQRqiptp 552
Cdd:PHA03307   312 P-RASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS-PSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGR----- 384

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889930739  553 gPQSRLTPPPAQPQRPQSLPPPVSTsavvsqqAPPRVPSPKQNGVTETQTAPQEKPADPMKSPEPPKEDPPASR 626
Cdd:PHA03307   385 -PTRRRARAAVAGRARRRDATGRFP-------AGRPRPSPLDAGAASGAFYARYPLLTPSGEPWPGSPPPPPGR 450
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 500-634 2.99e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.39  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 500 PATTPPSPTfQQRLPTSPTVQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSA 579
Cdd:PRK07994  372 PQSAAPAAS-AQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPAAASRAR 450

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930739 580 VVSqQAPPRVPSPKQNgVTETQTAPQEKPADPMKSPEPP-KEDPPASRSSDLPLAL 634
Cdd:PRK07994  451 PVN-SALERLASVRPA-PSALEKAPAKKEAYRWKATNPVeVKKEPVATPKALKKAL 504
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 501-618 3.90e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 40.87  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 501 ATTPPSPTFQQRLPTSPTVQPSAVPQSASQPRPSaLSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAV 580
Cdd:PHA03269   36 ATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPD-LAQAPTPAASEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPDAAE 114

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1889930739 581 VSQQAPPRVPSPKQNGVTETQTAPQekPADPMKSPEPP 618
Cdd:PHA03269  115 AFTSAAQAHEAPADAGTSAASKKPD--PAAHTQHSPPP 150
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 381-634 5.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 381 GNRKGSDGLPSLPKPAADQQKTTLCRPPAPKPEGyhpymgsrgqdttspttpttvpsptflqhsQRPHSRPTQPVQAVPA 460
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPA------------------------------APAAPAPAGAAAAPAE 638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 461 QQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTfqqrlptsPTVQPSAVPQSASQPRPSALSVLP 540
Cdd:PRK07764  639 ASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA--------PAAPAAPAGAAPAQPAPAPAATPP 710

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 541 TSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPP----PVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEKPADPMKSPE 616
Cdd:PRK07764  711 AGQADDPAAQPPQAAQGASAPSPAADDPVPLPPepddPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDA 790

                         250
                  ....*....|....*...
gi 1889930739 617 PPKEDPPASRSSDLPLAL 634
Cdd:PRK07764  791 PSMDDEDRRDAEEVAMEL 808
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
 516-645 5.97e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 40.46  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 516 SPTVQPSAVPQSASQPRP---SALSVLPTSQPSQRQIP---------TPGPQSRLTPPPAQPQRPQSLPPPVSTSA-VVS 582
Cdd:PRK08691  379 SPSAQTAEKETAAKKPQPrpeAETAQTPVQTASAAAMPsegktagpvSNQENNDVPPWEDAPDEAQTAAGTAQTSAkSIQ 458

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930739 583 QQAPPRVPSPKQNGVTETQTAPQEKPADPMKSPEPPKEDP---PASRSSDLPLALNKPQPEKQQPQ 645
Cdd:PRK08691  459 TASEAETPPENQVSKNKAADNETDAPLSEVPSENPIQATPndeAVETETFAHEAPAEPFYGYGFPD 524
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 891-940 7.07e-03

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


Pssm-ID: 188916  Cd Length: 66  Bit Score: 36.16  E-value: 7.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889930739 891 GCSDFADEFRSQEIDGQALMLLKEDHLMSaMNMKLGPALKICARINSLKQ 940
Cdd:cd09517    13 HLEEYLPVFEREKIDLEALMLLTDEDLQS-LKLPLGPRRKLLNAIAKRKQ 61
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 449-678 7.77e-03

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: 39.94  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 449 SRPTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQPSAVPQSA 528
Cdd:pfam17823 113 RALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAAS 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 529 SQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEKP 608
Cdd:pfam17823 193 SAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINM 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 609 ADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQRAVVKPqilthlidgfIIQEGPQPFPIKHNSIL 678
Cdd:pfam17823 273 GDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTDQP----------VHNTAGEPTPSPSNTTL 332
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 465-629 8.24e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.85  E-value: 8.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 465 PKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPtfQQRLPTSPTVQPSAVPQSASQPRPSALSVLPTSQP 544
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPP--ASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKA 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 545 -------SQRQIPTPGPQSRLTPPPAQpqrpqslpPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQE--KPADPMKSP 615
Cdd:PRK07994  439 kksepaaASRARPVNSALERLASVRPA--------PSALEKAPAKKEAYRWKATNPVEVKKEPVATPKAlkKALEHEKTP 510

                         170
                  ....*....|....
gi 1889930739 616 EPPKEDPPASRSSD 629
Cdd:PRK07994  511 ELAAKLAAEAIERD 524
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 444-672 8.28e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 39.91  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 444 SQRPhsRPTQPVQAVPAQQTSPKPTAPSPPITKME---AQHIPHHVPVPVVPRPPLHNRPATTP-PSPTFQQRlPTSPTV 519
Cdd:PLN03209  325 SQRV--PPKESDAADGPKPVPTKPVTPEAPSPPIEeepPQPKAVVPRPLSPYTAYEDLKPPTSPiPTPPSSSP-ASSKSV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 520 QPSAVPQSA-SQPRPSALSVLPTSQPSQRQIPTPGPQS---RLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQN 595
Cdd:PLN03209  402 DAVAKPAEPdVVPSPGSASNVPEVEPAQVEAKKTRPLSpyaRYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPAT 481

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889930739 596 GVTETQTAPQEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQraVVKPQILTHLIDGFIIQEgPQPFPI 672
Cdd:PLN03209  482 AATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVK--VGNSAPPTALADEQHHAQ-PKPRPL 555
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 525-648 9.01e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.70  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 525 PQSASQPRPSALSVLPTSQPSQRQIPTPGPQSrltpppaqPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAP 604
Cdd:PRK14951  366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQA--------AAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAA 437

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1889930739 605 QEKPadPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQRAV 648
Cdd:PRK14951  438 PAAA--PAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAP 479
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 451-656 9.53e-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: 39.63  E-value: 9.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 451 PTQPVQAVPAQQTSPKPTAPSPPITKM------EAQHIphhvpvpvvprpplhnrpATTPPSPTFQqrlPTSPTVQPSAV 524
Cdd:pfam09770 167 PKKAAAPAPAPQPAAQPASLPAPSRKMmsleevEAAMR------------------AQAKKPAQQP---APAPAQPPAAP 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930739 525 PQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAP-PRVPSPKQNGVTETQTA 603
Cdd:pfam09770 226 PAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQfHQQPPPVPVQPTQILQN 305

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1889930739 604 PQEKPADPMKSPEPPKEDPPAsrssdlplalNKPQPEKQQPQRAVVKPQILTH 656
Cdd:pfam09770 306 PNRLSAARVGYPQNPQPGVQP----------APAHQAHRQQGSFGRQAPIITH 348
 
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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