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Conserved domains on  [gi|1889930745|ref|XP_035696965|]
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polyhomeotic-like protein 2 isoform X12 [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 ...
 808-876 4.69e-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: 4.69e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930745 808 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 876
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
447-586 9.53e-08

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14971:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 614  Bit Score: 55.94  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 447 PHSRPTQPVQPsAVPQSASQPRPSAlSVLPTSQPSQRQIPTPGPQsrltpppaqpqrpqslPPPVSTSAVVSQQAPPRVP 526
Cdd:PRK14971  371 GGRGPKQHIKP-VFTQPAAAPQPSA-AAAASPSPSQSSAAAQPSA----------------PQSATQPAGTPPTVSVDPP 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 527 SPKQngVTETQTAPQEKPADPMKSPEPPkedpPASRSSDLPLALNKPQPEKQQPQRAVVK 586
Cdd:PRK14971  433 AAVP--VNPPSTAPQAVRPAQFKEEKKI----PVSKVSSLGPSTLRPIQEKAEQATGNIK 486
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 252-607 7.49e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 330
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  331 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 406
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  407 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPS--------------------AVPQSASQ 466
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparppttagppapappAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  467 PR--PSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLP-PPVSTSAVVSQQAPPRVPSPKQ-----------NG 532
Cdd:PHA03247  2781 RRltRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAPPPPPGPPPpslplggsvapGG 2860

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930745  533 VTETQTAPQEKPADPMKSPEPPKED---PPASRSSDlPLALNKPQPEKQQPQRAVVKPQILTHLIDGFIIQEGPQPFP 607
Cdd:PHA03247  2861 DVRRRPPSRSPAAKPAAPARPPVRRlarPAVSRSTE-SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
 
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 ...
 808-876 4.69e-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: 4.69e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930745 808 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 876
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 813-875 4.44e-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: 4.44e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930745 813 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 875
Cdd:pfam00536   3 WSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 810-877 5.26e-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: 5.26e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930745  810 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNM-KLGPALKICARINSLKQD 877
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
447-586 9.53e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 55.94  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 447 PHSRPTQPVQPsAVPQSASQPRPSAlSVLPTSQPSQRQIPTPGPQsrltpppaqpqrpqslPPPVSTSAVVSQQAPPRVP 526
Cdd:PRK14971  371 GGRGPKQHIKP-VFTQPAAAPQPSA-AAAASPSPSQSSAAAQPSA----------------PQSATQPAGTPPTVSVDPP 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 527 SPKQngVTETQTAPQEKPADPMKSPEPPkedpPASRSSDLPLALNKPQPEKQQPQRAVVK 586
Cdd:PRK14971  433 AAVP--VNPPSTAPQAVRPAQFKEEKKI----PVSKVSSLGPSTLRPIQEKAEQATGNIK 486
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-607 7.49e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 330
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  331 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 406
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  407 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPS--------------------AVPQSASQ 466
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparppttagppapappAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  467 PR--PSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLP-PPVSTSAVVSQQAPPRVPSPKQ-----------NG 532
Cdd:PHA03247  2781 RRltRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAPPPPPGPPPpslplggsvapGG 2860

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930745  533 VTETQTAPQEKPADPMKSPEPPKED---PPASRSSDlPLALNKPQPEKQQPQRAVVKPQILTHLIDGFIIQEGPQPFP 607
Cdd:PHA03247  2861 DVRRRPPSRSPAAKPAAPARPPVRRlarPAVSRSTE-SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 383-669 4.64e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.52  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 383 RKGSDGLPSLPKP-AADQQKTTLCRP---PAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPS 458
Cdd:NF033839  152 SSGSSTKPETPQPeNPEHQKPTTPAPdtkPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIV 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 459 AVPQSASQPRPSALSVLPTsqpsqrqiptpgPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQT 538
Cdd:NF033839  232 ALIKELDELKKQALSEIDN------------VNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGM 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 539 APQEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQravVKPQILTHLIDGFIIQEGPQP-------FPIKHN 611
Cdd:NF033839  300 QPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPE---VKPQLETPKPEVKPQPEKPKPevkpqpeKPKPEV 376

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930745 612 SILVESRRPHISLAKDQLSPEAGPSSENGSTLLIQSPDGKQPSKKPKKLQDKTLLKCE 669
Cdd:NF033839  377 KPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQ 434
 
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 ...
 808-876 4.69e-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: 4.69e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930745 808 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 876
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 810-873 1.35e-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: 1.35e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889930745 810 PARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINS 873
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 ...
 812-871 1.90e-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: 1.90e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 812 RWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARI 871
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 ...
 810-875 1.94e-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: 1.94e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930745 810 PARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 875
Cdd:cd09582     1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Scm cd09578
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ...
 809-876 8.33e-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: 8.33e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 809 NPARWSVEEVWEFIRSLPGCS--DFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 876
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 ...
 809-876 3.16e-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: 3.16e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930745 809 NPARWSVEEVWEFIRSlPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 876
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 ...
 810-875 3.68e-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: 3.68e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930745 810 PARWSVEEVWEFIRsLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 875
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 ...
 810-876 5.53e-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: 5.53e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889930745 810 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 876
Cdd:cd09583     1 PSNWSVEDVVQYFKTA-GFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQ 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 813-875 4.44e-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: 4.44e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930745 813 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 875
Cdd:pfam00536   3 WSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 810-877 5.26e-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: 5.26e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930745  810 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNM-KLGPALKICARINSLKQD 877
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
447-586 9.53e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 55.94  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 447 PHSRPTQPVQPsAVPQSASQPRPSAlSVLPTSQPSQRQIPTPGPQsrltpppaqpqrpqslPPPVSTSAVVSQQAPPRVP 526
Cdd:PRK14971  371 GGRGPKQHIKP-VFTQPAAAPQPSA-AAAASPSPSQSSAAAQPSA----------------PQSATQPAGTPPTVSVDPP 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 527 SPKQngVTETQTAPQEKPADPMKSPEPPkedpPASRSSDLPLALNKPQPEKQQPQRAVVK 586
Cdd:PRK14971  433 AAVP--VNPPSTAPQAVRPAQFKEEKKI----PVSKVSSLGPSTLRPIQEKAEQATGNIK 486
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-607 7.49e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 330
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  331 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 406
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  407 PPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPS--------------------AVPQSASQ 466
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparppttagppapappAAPAAGPP 2780

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  467 PR--PSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLP-PPVSTSAVVSQQAPPRVPSPKQ-----------NG 532
Cdd:PHA03247  2781 RRltRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAPPPPPGPPPpslplggsvapGG 2860

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930745  533 VTETQTAPQEKPADPMKSPEPPKED---PPASRSSDlPLALNKPQPEKQQPQRAVVKPQILTHLIDGFIIQEGPQPFP 607
Cdd:PHA03247  2861 DVRRRPPSRSPAAKPAAPARPPVRRlarPAVSRSTE-SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-596 1.96e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSSTVDKTKSQSSHPVPQAIAIG------QPSSAKAVPVQYSP 325
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRprrraaRPTVGSLTSLADPP 2702

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  326 TKQTAPEPPVSKLEAHSSLHLLASHAHHASSRSPthdrgISAMSPPFRHSVQWPNG-NRKGSDGLPSLPKPAADQQKTTL 404
Cdd:PHA03247  2703 PPPPTPEPAPHALVSATPLPPGPAAARQASPALP-----AAPAPPAVPAGPATPGGpARPARPPTTAGPPAPAPPAAPAA 2777

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  405 CRPPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPSAVPQSASQPRPSALSVLPTSQ----- 479
Cdd:PHA03247  2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLggsva 2857

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  480 ---PSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEKPAdpmKSPEPPKE 556
Cdd:PHA03247  2858 pggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPP---PQPQPPPP 2934

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1889930745  557 DPPASRSSDLPLALNKPQPEkqqPQRAVVKPQiLTHLIDG 596
Cdd:PHA03247  2935 PPPRPQPPLAPTTDPAGAGE---PSGAVPQPW-LGALVPG 2970
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 813-876 2.70e-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: 2.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930745 813 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMK-LGPALKICARINSLKQ 876
Cdd:cd09505     5 WSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKM 68
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 817-872 6.23e-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: 6.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930745 817 EVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARIN 872
Cdd:cd09487     1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
813-875 8.54e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.18  E-value: 8.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930745 813 WSVEEVWEFIRSLpGCSDFADEFRSQEIDG-QALMLLKEDHLMsAMNM-KLGPALKICARINSLK 875
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 ...
 813-875 2.29e-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: 2.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930745 813 WSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSaMNMKLGPALKICARINSLK 875
Cdd:cd09528     3 WTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLIIHSFNELN 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
 221-568 2.72e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  221 PATTSGSTGSSSTPPALLSQISRGQGSVQALPL--RGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPkkTDSSTVDKTKS 298
Cdd:PHA03247  2720 PLPPGPAAARQASPALPAAPAPPAVPAGPATPGgpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRP--AVASLSESRES 2797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  299 QSSHPVPQAIAIGQPSSAKAVPVQYSPTKQTAPEPPVSKLEAHSSLHLLASHAHHASSRSPThdrGISAMSPPFRHSVQW 378
Cdd:PHA03247  2798 LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG---GDVRRRPPSRSPAAK 2874

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  379 PNGNRKGSdgLPSLPKPAADQQKTTLCRPPAPKPEGYHPYMGSRGQDTTSPTTPTTVpsptflQHSQRPHSRPTQPVQPS 458
Cdd:PHA03247  2875 PAAPARPP--VRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP------QPPPPPPPRPQPPLAPT 2946

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  459 AVPQSASQPRPSAL-----SVLPTSQPSQR-QIPTPGPqSRLTPPPAQPQRPQSLPPPVS---TSAVVSQQAPPRVPSPK 529
Cdd:PHA03247  2947 TDPAGAGEPSGAVPqpwlgALVPGRVAVPRfRVPQPAP-SREAPASSTPPLTGHSLSRVSswaSSLALHEETDPPPVSLK 3025

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1889930745  530 QN----GVTETQTAPQEKPADPMKS------PEPPKEDPPASRSSDLPL 568
Cdd:PHA03247  3026 QTlwppDDTEDSDADSLFDSDSERSdlealdPLPPEPHDPFAHEPDPAT 3074
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
442-581 6.70e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 46.69  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 442 QHSQRPHSRPTQPVQPSAVPQSASQPRPSALsvlpTSQPSQrqiptpgpqsrltpppaqpqrpqslPPPVSTSAVVSQQA 521
Cdd:PRK14971  377 QHIKPVFTQPAAAPQPSAAAAASPSPSQSSA----AAQPSA-------------------------PQSATQPAGTPPTV 427

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 522 PPRVPSPKQngVTETQTAPQEKPADPMKSPEPPkedPPASRSSDLPLALNKPQPEKQQPQ 581
Cdd:PRK14971  428 SVDPPAAVP--VNPPSTAPQAVRPAQFKEEKKI---PVSKVSSLGPSTLRPIQEKAEQAT 482
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 234-562 2.43e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  234 PPALLSQISRGQGSVQALPLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSST-VDKTKSQSSHPVPQAIAIGQ 312
Cdd:PHA03307    97 PASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAgASPAAVASDAASSRQAALPL 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  313 PSSAKAVPVQYSPTKQTAPEPPVSKLEAHSS-LHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQWPNGNRKGSDGLPS 391
Cdd:PHA03307   177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPrRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  392 LPKPAADQQKTTLCRPPAPKPEGY-HPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPSAVPQSASQPRPS 470
Cdd:PHA03307   257 LPRPAPITLPTRIWEASGWNGPSSrPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESS 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  471 ALSVLPTSQPSQRQiPTPGPQSRLTPPPAQPQRPQSLPPPVSTSA-----------------VVSQQAPPRVP------S 527
Cdd:PHA03307   337 RGAAVSPGPSPSRS-PSPSRPPPPADPSSPRKRPRPSRAPSSPAAsagrptrrraraavagrARRRDATGRFPagrprpS 415

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1889930745  528 PKQNGVTETQTAPQEKPADPMKSPEPPKEDPPASR 562
Cdd:PHA03307   416 PLDAGAASGAFYARYPLLTPSGEPWPGSPPPPPGR 450
PHA03247 PHA03247
large tegument protein UL36; Provisional
 256-567 2.97e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  256 PPVPPSSanqskPSQSKQLDQSEKRVSTSPKKTDSSTVDKTKSQSSHPVPQAIAI-GQPSSAKAVPVQYSPTKQTAPEPP 334
Cdd:PHA03247  2701 PPPPPPT-----PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAP 2775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  335 VSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQWPNGNRKGSDGLPSLPKPAADQqkttlcrPPAPKPEG 414
Cdd:PHA03247  2776 AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP-------PPPGPPPP 2848

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  415 YHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSR------PTQPVQPSAVPQSASQPRPSalsvlPTSQPSQRQIPTP 488
Cdd:PHA03247  2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRrlarpaVSRSTESFALPPDQPERPPQ-----PQAPPPPQPQPQP 2923

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  489 GPQSRLTPPPAQPQRPQSLPPPVSTSAVVSqQAPPRVPSPKQNGVTETQTA-PQEKPADPMKSPEPPKEDPPASRSSDLP 567
Cdd:PHA03247  2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAG-EPSGAVPQPWLGALVPGRVAvPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 810-877 5.37e-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: 5.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889930745 810 PARWSVEEVWEFIRSLpGCSDFADEFRSQE-IDGQALMLLKEDHLMS-AMNMK-LGPALKICARINSLKQD 877
Cdd:cd09515     1 VHEWTCEDVAKWLKKE-GFSKYVDLLCNKHrIDGKVLLSLTEEDLRSpPLEIKvLGDIKRLWLAIRKLQRQ 70
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 813-862 9.11e-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: 9.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889930745 813 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLG 862
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 ...
 813-875 1.07e-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: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930745 813 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 875
Cdd:cd09534     1 WDEEFVEEWLNEL-NCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR 62
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 396-659 1.90e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  396 AADQQKTTLCRPPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPSAvPQSASQPRPSAlsvl 475
Cdd:PHA03307    57 AGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPT-PPPASPPPSPA---- 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  476 PTSQPSQRQIPTPGPQSRltpppaqpqrPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAPQEKPAD-PMKSPEPP 554
Cdd:PHA03307   132 PDLSEMLRPVGSPGPPPA----------ASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEpPPSTPPAA 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  555 KEDPPASRSSDL--PLALNKPQPEKQQPQRAVVKPQILTHLIDGFIIQEGPQPFPIKHNSILVESRRPHISLAKDQLSPE 632
Cdd:PHA03307   202 ASPRPPRRSSPIsaSASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSR 281

                          250       260
                   ....*....|....*....|....*..
gi 1889930745  633 AGPSSENGStllIQSPDGKQPSKKPKK 659
Cdd:PHA03307   282 PGPASSSSS---PRERSPSPSPSSPGS 305
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 447-554 3.44e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 40.87  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 447 PHSRPTQPVQPSAVPQSASQPRPSaLSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVP 526
Cdd:PHA03269   46 PHQAASRAPDPAVAPTSAASRKPD-LAQAPTPAASEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPDAAEAFTSAAQAHE 124

                          90       100
                  ....*....|....*....|....*...
gi 1889930745 527 SPKQNGVTETQTAPQekPADPMKSPEPP 554
Cdd:PHA03269  125 APADAGTSAASKKPD--PAAHTQHSPPP 150
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 449-576 3.65e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 449 SRPTQPVQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSrltppPAQPQRPQSLPPPVSTSAVVSQQ-APPRVPS 527
Cdd:PRK14951  369 AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAAS-----APAAPPAAAPPAPVAAPAAAAPAaAPAAAPA 443

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889930745 528 PKQNGVTETQTAPQEKPADPMK-SPEPPKEDPPASRSSDLPLALNKPQPE 576
Cdd:PRK14951  444 AVALAPAPPAQAAPETVAIPVRvAPEPAVASAAPAPAAAPAAARLTPTEE 493
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 252-561 4.22e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 252 PLRGP---PVPPSSANQSKPSQSKQLDQSEKRVST---SPKKTDSSTVDKTKSQSSHPVPQAIAI--------GQPSSAK 317
Cdd:PTZ00449  510 PPEGPeasGLPPKAPGDKEGEEGEHEDSKESDEPKeggKPGETKEGEVGKKPGPAKEHKPSKIPTlskkpefpKDPKHPK 589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 318 AVPVQYSPTKQTAPEPPVSKLEAH--SSLHLLASHAHHASSRSPThdrgiSAMSPPFRHSVQWPNGNRK-GSDGLPSLPK 394
Cdd:PTZ00449  590 DPEEPKKPKRPRSAQRPTRPKSPKlpELLDIPKSPKRPESPKSPK-----RPPPPQRPSSPERPEGPKIiKSPKPPKSPK 664

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 395 PAADqqkttlcrpPAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPSAVPqsASQPRPSALSV 474
Cdd:PTZ00449  665 PPFD---------PKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLP--PKLPRDEEFPF 733

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 475 LPTSQPSQrqiPTPGPQSRLTpppaqpqrpqslpPPVSTSAVVsQQAPPRVPSP---KQNGVTETQTAPQEKPADPMKSP 551
Cdd:PTZ00449  734 EPIGDPDA---EQPDDIEFFT-------------PPEEERTFF-HETPADTPLPdilAEEFKEEDIHAETGEPDEAMKRP 796

                         330
                  ....*....|
gi 1889930745 552 EPPKEDPPAS 561
Cdd:PTZ00449  797 DSPSEHEDKP 806
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 383-669 4.64e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.52  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 383 RKGSDGLPSLPKP-AADQQKTTLCRP---PAPKPEGYHPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQPS 458
Cdd:NF033839  152 SSGSSTKPETPQPeNPEHQKPTTPAPdtkPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIV 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 459 AVPQSASQPRPSALSVLPTsqpsqrqiptpgPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQT 538
Cdd:NF033839  232 ALIKELDELKKQALSEIDN------------VNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGM 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 539 APQEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQravVKPQILTHLIDGFIIQEGPQP-------FPIKHN 611
Cdd:NF033839  300 QPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPE---VKPQLETPKPEVKPQPEKPKPevkpqpeKPKPEV 376

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930745 612 SILVESRRPHISLAKDQLSPEAGPSSENGSTLLIQSPDGKQPSKKPKKLQDKTLLKCE 669
Cdd:NF033839  377 KPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQ 434
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 452-587 4.99e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 4.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745  452 TQPVQPSAVPQSASQPRPSALSV-LPTSQPSQRQIPTPGPQsrlTPPPAQPQRPQSLPP-PVSTSAVVSQQAPPRVPSPK 529
Cdd:PRK10263   327 TTATQSWAAPVEPVTQTPPVASVdVPPAQPTVAWQPVPGPQ---TGEPVIAPAPEGYPQqSQYAQPAVQYNEPLQQPVQP 403

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930745  530 QNGVTETQTAPQEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQ----------QPQRAVVKP 587
Cdd:PRK10263   404 QQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQqstfapqstyQTEQTYQQP 471
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 827-876 5.73e-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: 5.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889930745 827 GCSDFADEFRSQEIDGQALMLLKEDHLMSaMNMKLGPALKICARINSLKQ 876
Cdd:cd09517    13 HLEEYLPVFEREKIDLEALMLLTDEDLQS-LKLPLGPRRKLLNAIAKRKQ 61
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
452-580 6.10e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 452 TQPVQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAvvSQQAPPRVPSPKQN 531
Cdd:PRK12323  372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAA--ARQASARGPGGAPA 449

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1889930745 532 GVTETQTAPQEKPADPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQP 580
Cdd:PRK12323  450 PAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPP 498
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 461-584 6.30e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.08  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930745 461 PQSASQPRPSALSVLPTSQPSQRQIPTPGPQSrltpppaqPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVTETQTAP 540
Cdd:PRK14951  366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQA--------AAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAA 437

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1889930745 541 QEKPadPMKSPEPPKEDPPASRSSDLPLALNKPQPEKQQPQRAV 584
Cdd:PRK14951  438 PAAA--PAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAP 479
 
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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