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Conserved domains on  [gi|1889930725|ref|XP_035696955|]
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polyhomeotic-like protein 3 isoform X2 [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 ...
 980-1048 5.60e-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: 5.60e-46
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930725  980 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 1048
Cdd:cd09577      1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 390-760 1.52e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.65  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  390 PSLPKPAADQQKTTlcRPPAPKPEGyhPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQAVPAQQ---TSPK 466
Cdd:PHA03247  2557 PAAPPAAPDRSVPP--PRPAPRPSE--PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDpppPSPS 2632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  467 PTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPMGA-SSLGSPPPPEaKTGHVH 545
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSlTSLADPPPPP-PTPEPA 2711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  546 HVHPHVQPPVQPPPPQPVQAHNPQGHAVQAAHVPPTHIQAAHVQPTHVQPLSQPLPLALATHKPVQTAPPLPQQPPLGPS 625
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  626 PVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNG 705
Cdd:PHA03247  2792 SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889930725  706 VTETTAPQEKPADPMKSPEPPKEDPPASRSSDLPlalnKPQPEKQQPQRAVVKPQ 760
Cdd:PHA03247  2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQP----ERPPQPQAPPPPQPQPQ 2922
 
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 ...
 980-1048 5.60e-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: 5.60e-46
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930725  980 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 1048
Cdd:cd09577      1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 985-1047 5.33e-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: 5.33e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930725  985 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 1047
Cdd:pfam00536    3 WSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 982-1049 6.32e-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: 6.32e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930725   982 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNM-KLGPALKICARINSLKQD 1049
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
 390-760 1.52e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.65  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  390 PSLPKPAADQQKTTlcRPPAPKPEGyhPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQAVPAQQ---TSPK 466
Cdd:PHA03247  2557 PAAPPAAPDRSVPP--PRPAPRPSE--PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDpppPSPS 2632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  467 PTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPMGA-SSLGSPPPPEaKTGHVH 545
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSlTSLADPPPPP-PTPEPA 2711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  546 HVHPHVQPPVQPPPPQPVQAHNPQGHAVQAAHVPPTHIQAAHVQPTHVQPLSQPLPLALATHKPVQTAPPLPQQPPLGPS 625
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  626 PVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNG 705
Cdd:PHA03247  2792 SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889930725  706 VTETTAPQEKPADPMKSPEPPKEDPPASRSSDLPlalnKPQPEKQQPQRAVVKPQ 760
Cdd:PHA03247  2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQP----ERPPQPQAPPPPQPQPQ 2922
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 445-760 1.98e-05

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: 49.00  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  445 QRPHSRPTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGI 524
Cdd:pfam03154  185 SPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQ 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  525 PMGASSLGSPPPP---EAKTGHVHHVHPHVQPPVQPPPPQPVQAHNP------QGHAVQAAHVPPTHIQAAHVQPTHVQP 595
Cdd:pfam03154  265 PLPQPSLHGQMPPmphSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaaPGQSQQRIHTPPSQSQLQSQQPPREQP 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  596 LSqPLPLALATHKPVQTAPPLPQQPPLG---PSPVAQPSAVPQSASQPRPSA---LSVLPTSQP-------------SQR 656
Cdd:pfam03154  345 LP-PAPLSMPHIKPPPTTPIPQLPNPQShkhPPHLSGPSPFQMNSNLPPPPAlkpLSSLSTHHPpsahppplqlmpqSQQ 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  657 QIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVP--SPKQNGVTETTAPQEKPADPMKSPEPPKEDPPASr 734
Cdd:pfam03154  424 LPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPfvPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSS- 502

                          330       340
                   ....*....|....*....|....*.
gi 1889930725  735 SSDLPLALNKPQPEKQQPQRAVVKPQ 760
Cdd:pfam03154  503 SGPVPAAVSCPLPPVQIKEEALDEAE 528
 
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 ...
 980-1048 5.60e-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: 5.60e-46
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930725  980 PNPARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 1048
Cdd:cd09577      1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 982-1045 1.62e-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: 1.62e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889930725  982 PARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINS 1045
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 ...
 984-1043 2.28e-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: 2.28e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  984 RWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARI 1043
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 ...
 982-1047 2.32e-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: 2.32e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930725  982 PARWSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 1047
Cdd:cd09582      1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Scm cd09578
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ...
 981-1048 1.00e-19

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: 1.00e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  981 NPARWSVEEVWEFIRSLPGCS--DFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 1048
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 ...
 981-1048 3.62e-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: 3.62e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930725  981 NPARWSVEEVWEFIRSlPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 1048
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 ...
 982-1047 4.42e-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: 4.42e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930725  982 PARWSVEEVWEFIRsLPGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 1047
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 ...
 982-1048 6.63e-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: 6.63e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889930725  982 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLKQ 1048
Cdd:cd09583      1 PSNWSVEDVVQYFKTA-GFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQ 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 985-1047 5.33e-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: 5.33e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930725  985 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 1047
Cdd:pfam00536    3 WSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 982-1049 6.32e-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: 6.32e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889930725   982 PARWSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNM-KLGPALKICARINSLKQD 1049
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGItKLGHRKKILKAIQKLKEQ 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
 390-760 1.52e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.65  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  390 PSLPKPAADQQKTTlcRPPAPKPEGyhPYMGSRGQDTTSPTTPTTVPSPTFLQHSQRPHSRPTQPVQAVPAQQ---TSPK 466
Cdd:PHA03247  2557 PAAPPAAPDRSVPP--PRPAPRPSE--PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDpppPSPS 2632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  467 PTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPMGA-SSLGSPPPPEaKTGHVH 545
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSlTSLADPPPPP-PTPEPA 2711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  546 HVHPHVQPPVQPPPPQPVQAHNPQGHAVQAAHVPPTHIQAAHVQPTHVQPLSQPLPLALATHKPVQTAPPLPQQPPLGPS 625
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  626 PVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNG 705
Cdd:PHA03247  2792 SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889930725  706 VTETTAPQEKPADPMKSPEPPKEDPPASRSSDLPlalnKPQPEKQQPQRAVVKPQ 760
Cdd:PHA03247  2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQP----ERPPQPQAPPPPQPQPQ 2922
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-736 2.53e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.88  E-value: 2.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  252 PLRGPPVPPSSANQSKPSQSKQLDQSEKRVSTSPKKTDSStvdktkSQSSHP-VPQAIAIGQPSSAKAVPvqySPTKQTA 330
Cdd:PHA03247  2553 PPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP------PQSARPrAPVDDRGDPRGPAPPSP---LPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  331 PEPPVSKLEAHSSLHLLASHAHHASSRSPTHDRGISAMSPPFRHSVQwpnGNRKGSDGLPSLPKPAADQQK----TTLCR 406
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTvgslTSLAD 2700

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  407 PPAPKPEgyhpymgsrgqdttspttpttvpsptflqhsqrPHSRPTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHV 486
Cdd:PHA03247  2701 PPPPPPT---------------------------------PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  487 PVPVVPRPPLHNRPATTPPSPtfqqrlPTSPTVqsmgiPMGASSLGSPPPPEAKTGHVHHVHPHVQPPVQPPPPQPVQAH 566
Cdd:PHA03247  2748 PATPGGPARPARPPTTAGPPA------PAPPAA-----PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  567 NPQGHAVQAAHVPPTHIQAAHVQPTHVQPLSQPLPLA-----------LATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQ 635
Cdd:PHA03247  2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvapggdvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE 2896

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  636 SASQPrPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNG--------VT 707
Cdd:PHA03247  2897 SFALP-PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGalvpgrvaVP 2975

                          490       500       510
                   ....*....|....*....|....*....|
gi 1889930725  708 ETTAPQEKPADPM-KSPEPPKEDPPASRSS 736
Cdd:PHA03247  2976 RFRVPQPAPSREApASSTPPLTGHSLSRVS 3005
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 985-1048 3.24e-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: 3.24e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930725  985 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMK-LGPALKICARINSLKQ 1048
Cdd:cd09505      5 WSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKM 68
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 989-1044 7.47e-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: 7.47e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889930725  989 EVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARIN 1044
Cdd:cd09487      1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
985-1047 1.03e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.18  E-value: 1.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889930725  985 WSVEEVWEFIRSLpGCSDFADEFRSQEIDG-QALMLLKEDHLMsAMNM-KLGPALKICARINSLK 1047
Cdd:pfam07647    4 WSLESVADWLRSI-GLEQYTDNFRDQGITGaELLLRLTLEDLK-RLGItSVGHRRKILKKIQELK 66
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 445-760 1.98e-05

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: 49.00  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  445 QRPHSRPTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGI 524
Cdd:pfam03154  185 SPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQ 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  525 PMGASSLGSPPPP---EAKTGHVHHVHPHVQPPVQPPPPQPVQAHNP------QGHAVQAAHVPPTHIQAAHVQPTHVQP 595
Cdd:pfam03154  265 PLPQPSLHGQMPPmphSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaaPGQSQQRIHTPPSQSQLQSQQPPREQP 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  596 LSqPLPLALATHKPVQTAPPLPQQPPLG---PSPVAQPSAVPQSASQPRPSA---LSVLPTSQP-------------SQR 656
Cdd:pfam03154  345 LP-PAPLSMPHIKPPPTTPIPQLPNPQShkhPPHLSGPSPFQMNSNLPPPPAlkpLSSLSTHHPpsahppplqlmpqSQQ 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  657 QIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVP--SPKQNGVTETTAPQEKPADPMKSPEPPKEDPPASr 734
Cdd:pfam03154  424 LPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPfvPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSS- 502

                          330       340
                   ....*....|....*....|....*.
gi 1889930725  735 SSDLPLALNKPQPEKQQPQRAVVKPQ 760
Cdd:pfam03154  503 SGPVPAAVSCPLPPVQIKEEALDEAE 528
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 985-1047 2.75e-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: 2.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930725  985 WSVEEVWEFIRSLPGCSDFADEFRSQEIDGQALMLLKEDHLMSaMNMKLGPALKICARINSLK 1047
Cdd:cd09528      3 WTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLIIHSFNELN 64
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 525-742 7.10e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 7.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  525 PMGASSLGSPPPPEAKTGHVHHVHPHVQPPVQPPPPQPVQAHNPQGHAVQAAHVPPTHIQAAHvqptHVQPLSQPLPLAL 604
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEH----HPKHVAVPDASDG 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  605 ATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPP-- 682
Cdd:PRK07764   666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPep 745

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930725  683 ---PVSTSAVVSQQAPPRVPSPKQNGVTETTAPQEKPADPMKSPEPPKEDPPASRSSDLPLAL 742
Cdd:PRK07764   746 ddpPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMEL 808
PHA03378 PHA03378
EBNA-3B; Provisional
 574-750 3.48e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  574 QAAHVPPTHIQAAHVQPTHVQplSQPLPLALATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQP-------RPSALS 646
Cdd:PHA03378   653 QPPQVEITPYKPTWTQIGHIP--YQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPaaatgraRPPAAA 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  647 VLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRV-PSPKQNgvtettaPQEKPAdpmksPEP 725
Cdd:PHA03378   731 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQApPAPQQR-------PRGAPT-----PQP 798

                          170       180
                   ....*....|....*....|....*
gi 1889930725  726 PKEDPPASRSSDLPLALNKPQPEKQ 750
Cdd:PHA03378   799 PPQAGPTSMQLMPRAAPGQQGPTKQ 823
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 982-1049 6.45e-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: 6.45e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889930725  982 PARWSVEEVWEFIRSLpGCSDFADEFRSQE-IDGQALMLLKEDHLMS-AMNMK-LGPALKICARINSLKQD 1049
Cdd:cd09515      1 VHEWTCEDVAKWLKKE-GFSKYVDLLCNKHrIDGKVLLSLTEEDLRSpPLEIKvLGDIKRLWLAIRKLQRQ 70
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 582-741 8.45e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.32  E-value: 8.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  582 HIQAAHVQPTHVQPLSQPLPLALATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTP 661
Cdd:PRK07994   360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAK 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  662 GPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPR---VPSPKQNGVTETTAPQEKPADPMKSPEPPKEDPPASRSSDL 738
Cdd:PRK07994   440 KSEPAAASRARPVNSALERLASVRPAPSALEKAPAKkeaYRWKATNPVEVKKEPVATPKALKKALEHEKTPELAAKLAAE 519


                   ...
gi 1889930725  739 PLA 741
Cdd:PRK07994   520 AIE 522
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 985-1034 1.09e-03

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: 1.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1889930725  985 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLG 1034
Cdd:cd09501      4 WSVADVQTWLKQI-GFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSG 52
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 601-740 1.14e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.78  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  601 PLALATHKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQRQiptPGPQSRLTPPPAQPqrpqsl 680
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAP---PAPVAAPAAAAPAA------ 436

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  681 PPPVSTSAVVSQQAPPRVPSPKQNGVTETTAPQEKPADPmksPEPPKEDPPASRSSDLPL 740
Cdd:PRK14951   437 APAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASA---APAPAAAPAAARLTPTEE 493
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 451-760 1.14e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  451 PTQPVQAVPAQQTSPKPTAPSPPITKMEAQHIPHHVPVPVVPRPPLHNRPATTPPSPTFQQRLPTSPTVQSMGIPMGASS 530
Cdd:PRK07764   419 AAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  531 LGSPPPPEAKTGHVHHVHPHVQPPVQPPPPQPVQAHNPQghaVQAAHVPPTHIQAAHVQPTHVQPLSQP-----LPLALA 605
Cdd:PRK07764   499 APAAPAGADDAATLRERWPEILAAVPKRSRKTWAILLPE---ATVLGVRGDTLVLGFSTGGLARRFASPgnaevLVTALA 575

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  606 -----THKPVQTAPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQRQIPTPGPQSRLTPPPAQPQRPQSL 680
Cdd:PRK07764   576 eelggDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPK 655

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  681 PPPVSTSAVVSQQAPPRVPSPKQNGVTETTAPQEKPADPMKSPEPPKEDPPASRSSDLPLAlnkPQPEKQQPQRAVVKPQ 760
Cdd:PRK07764   656 HVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADD---PAAQPPQAAQGASAPS 732
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 985-1047 1.29e-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: 1.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889930725  985 WSVEEVWEFIRSLpGCSDFADEFRSQEIDGQALMLLKEDHLMSAMNMKLGPALKICARINSLK 1047
Cdd:cd09534      1 WDEEFVEEWLNEL-NCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR 62
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
632-753 1.37e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.46  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  632 AVPQSASQPRPSAlSVLPTSQPSQRQIPTPGPQsrltpppaQPqrpqslppPVSTSAVVSQQAPPRVPSPKQNgVTETTA 711
Cdd:PRK14971   382 VFTQPAAAPQPSA-AAAASPSPSQSSAAAQPSA--------PQ--------SATQPAGTPPTVSVDPPAAVPV-NPPSTA 443

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1889930725  712 PQEKPADPMKSPEPPkedPPASRSSDLPLALNKPQPEKQQPQ 753
Cdd:PRK14971   444 PQAVRPAQFKEEKKI---PVSKVSSLGPSTLRPIQEKAEQAT 482
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
577-704 5.62e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 40.53  E-value: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  577 HVPPTHIQAaHVQPTHVQPLSQPLPLALATHKPVQTaPPLPQQPPLGPSPVAQPSAVPQSASQPRPSALSVLPTSQPSQR 656
Cdd:PRK14971   369 ASGGRGPKQ-HIKPVFTQPAAAPQPSAAAAASPSPS-QSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTAPQA 446

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1889930725  657 QIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQN 704
Cdd:PRK14971   447 VRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAPTGTQK 494
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 570-707 5.94e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889930725  570 GHAVQAAHVPPTHIQAAHVQPTHVQPLSQPLPLALATHKPvqtapplpqqpplgpSPVAQPSAVPQSASQPRPSALSVLP 649
Cdd:PRK07764   386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP---------------AAAPQPAPAPAPAPAPPSPAGNAPA 450

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889930725  650 TSQPSQRQIPTPGPQSRLTPPPAQPQRPQSLPPPVSTSAVVSQQAPPRVPSPKQNGVT 707
Cdd:PRK07764   451 GGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADD 508
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 999-1048 6.88e-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: 6.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1889930725  999 GCSDFADEFRSQEIDGQALMLLKEDHLMSaMNMKLGPALKICARINSLKQ 1048
Cdd:cd09517     13 HLEEYLPVFEREKIDLEALMLLTDEDLQS-LKLPLGPRRKLLNAIAKRKQ 61
 
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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