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Conserved domains on  [gi|1958750414|ref|XP_038958159|]
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polyhomeotic-like protein 3 isoform X2 [Rattus norvegicus]

Protein Classification

SAM_Ph1,2,3 domain-containing protein( domain architecture ID 13588452)

SAM_Ph1,2,3 domain-containing protein

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 ...
 930-998 6.81e-43

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: 149.86  E-value: 6.81e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750414 930 TEPSIWTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLKD 998
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 299-584 8.68e-07

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.23  E-value: 8.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 299 QPHSLIKHQQIPLHSPPPKVSHHQLILQQQQQQIQPITLQSPSQDPPPSQHCIPLPNHGLSPASSNAQSQQHCSPiqsHP 378
Cdd:pfam03154 171 PPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSP---HP 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 379 PpltvspsqaqsAQQSVVVSPPPAHSPSQSPTIIIHPQALVQPHPLVSSALHtgpnLQQATADQVQSTAQLNLPSHLPLP 458
Cdd:pfam03154 248 P-----------LQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSH----MQHPVPPQPFPLTPQSSQSQVPPG 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 459 ASPVVHiGPVQQSALVSPGQQIVSPTSHQQYSTLQSSPIPIatpPQMSASPPAQIPPLPlqSMQSLQVQPEILSQGQVLV 538
Cdd:pfam03154 313 PSPAAP-GQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM---PHIKPPPTTPIPQLP--NPQSHKHPPHLSGPSPFQM 386

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750414 539 QNALVSEEEL-PAAEALVQLPFQTLPPPQTVAVNLQVQPPAPVDPPV 584
Cdd:pfam03154 387 NSNLPPPPALkPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPV 433
 
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 ...
 930-998 6.81e-43

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: 149.86  E-value: 6.81e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750414 930 TEPSIWTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLKD 998
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 933-997 6.72e-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: 61.52  E-value: 6.72e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750414 933 SIWTVDDVWAFIHSLpGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLK 997
Cdd:pfam00536   1 DGWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 932-999 2.48e-10

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: 57.31  E-value: 2.48e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750414  932 PSIWTVDDVWAFIHSLpGCQDVADEFRAQEIDGQALLLL-KEDHLMSTMNMKLGPALKICARINSLKDS 999
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLtSEEDLKELGITKLGHRKKILKAIQKLKEQ 68
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 299-584 8.68e-07

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: 53.23  E-value: 8.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 299 QPHSLIKHQQIPLHSPPPKVSHHQLILQQQQQQIQPITLQSPSQDPPPSQHCIPLPNHGLSPASSNAQSQQHCSPiqsHP 378
Cdd:pfam03154 171 PPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSP---HP 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 379 PpltvspsqaqsAQQSVVVSPPPAHSPSQSPTIIIHPQALVQPHPLVSSALHtgpnLQQATADQVQSTAQLNLPSHLPLP 458
Cdd:pfam03154 248 P-----------LQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSH----MQHPVPPQPFPLTPQSSQSQVPPG 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 459 ASPVVHiGPVQQSALVSPGQQIVSPTSHQQYSTLQSSPIPIatpPQMSASPPAQIPPLPlqSMQSLQVQPEILSQGQVLV 538
Cdd:pfam03154 313 PSPAAP-GQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM---PHIKPPPTTPIPQLP--NPQSHKHPPHLSGPSPFQM 386

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750414 539 QNALVSEEEL-PAAEALVQLPFQTLPPPQTVAVNLQVQPPAPVDPPV 584
Cdd:pfam03154 387 NSNLPPPPALkPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPV 433
PHA03247 PHA03247
large tegument protein UL36; Provisional
 339-586 4.52e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  339 SPSQDPPPSQHCIPLPNHGLSPASSNAQSQQHCSPIQSHPPPLTVSPSQAQSAQQSVVVS-PPPAHSPSQSPTiiihPQA 417
Cdd:PHA03247  2612 APPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPR----RRA 2687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  418 LVQP-HPLVSSALHTGPNLQQATADQVQSTAQLNLP----SHLPLPASPVVHIGPVQQSALVSPGQqiVSPTSHQQYSTL 492
Cdd:PHA03247  2688 ARPTvGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGPATPGG--PARPARPPTTAG 2765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  493 QSSPIPIATPPqmsASPPAQIPPLPLQSMQSLQVQPEILSQGQVLVQNALVSEEELPAAEAlvqlPFQTLPPPQTVAVNL 572
Cdd:PHA03247  2766 PPAPAPPAAPA---AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS----PAGPLPPPTSAQPTA 2838

                          250
                   ....*....|....
gi 1958750414  573 QVQPPAPVDPPVGM 586
Cdd:PHA03247  2839 PPPPPGPPPPSLPL 2852
 
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 ...
 930-998 6.81e-43

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: 149.86  E-value: 6.81e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750414 930 TEPSIWTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLKD 998
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 69
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 932-995 4.58e-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: 124.51  E-value: 4.58e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750414 932 PSIWTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINS 995
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 ...
 935-993 1.67e-22

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: 91.74  E-value: 1.67e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750414 935 WTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARI 993
Cdd:cd09579     4 WTVDDVCSFIGSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQV 62
SAM_Scm-like-3MBT3,4 cd09582
SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 932-997 5.47e-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: 84.64  E-value: 5.47e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958750414 932 PSIWTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLK 997
Cdd:cd09582     1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66
SAM_Scm cd09578
SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex ...
 932-997 4.41e-18

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: 79.39  E-value: 4.41e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750414 932 PSIWTVDDVWAFIHSL--PGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLK 997
Cdd:cd09578     4 PSTWSVEDVVQFIKEAdpQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLK 71
SAM_Atherin-like cd09583
SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin ...
 932-996 3.55e-13

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: 65.37  E-value: 3.55e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750414 932 PSIWTVDDVWAFIHSLpGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSL 996
Cdd:cd09583     1 PSNWSVEDVVQYFKTA-GFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKL 64
SAM_Scm-like-4MBT cd09580
SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 932-997 6.33e-13

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: 64.70  E-value: 6.33e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958750414 932 PSIWTVDDVWAFIhSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLK 997
Cdd:cd09580     1 PSTWGVKDVSQFL-RENDCGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLK 65
SAM_Scm-like-4MBT1,2 cd09581
SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 930-997 6.80e-13

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: 65.16  E-value: 6.80e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750414 930 TEPSIWTVDDVWAFIHSlPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLK 997
Cdd:cd09581    10 SNPLFWSVDDVVRFIKS-TDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIERVK 76
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 933-997 6.72e-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: 61.52  E-value: 6.72e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958750414 933 SIWTVDDVWAFIHSLpGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLK 997
Cdd:pfam00536   1 DGWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 932-999 2.48e-10

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: 57.31  E-value: 2.48e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750414  932 PSIWTVDDVWAFIHSLpGCQDVADEFRAQEIDGQALLLL-KEDHLMSTMNMKLGPALKICARINSLKDS 999
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLtSEEDLKELGITKLGHRKKILKAIQKLKEQ 68
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 299-584 8.68e-07

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: 53.23  E-value: 8.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 299 QPHSLIKHQQIPLHSPPPKVSHHQLILQQQQQQIQPITLQSPSQDPPPSQHCIPLPNHGLSPASSNAQSQQHCSPiqsHP 378
Cdd:pfam03154 171 PPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSP---HP 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 379 PpltvspsqaqsAQQSVVVSPPPAHSPSQSPTIIIHPQALVQPHPLVSSALHtgpnLQQATADQVQSTAQLNLPSHLPLP 458
Cdd:pfam03154 248 P-----------LQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSH----MQHPVPPQPFPLTPQSSQSQVPPG 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 459 ASPVVHiGPVQQSALVSPGQQIVSPTSHQQYSTLQSSPIPIatpPQMSASPPAQIPPLPlqSMQSLQVQPEILSQGQVLV 538
Cdd:pfam03154 313 PSPAAP-GQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM---PHIKPPPTTPIPQLP--NPQSHKHPPHLSGPSPFQM 386

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958750414 539 QNALVSEEEL-PAAEALVQLPFQTLPPPQTVAVNLQVQPPAPVDPPV 584
Cdd:pfam03154 387 NSNLPPPPALkPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPV 433
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 341-506 8.86e-07

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 53.12  E-value: 8.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 341 SQDPPPSQHciPLPNHGLSPASSNAQSQQhcsPIQSHPPPLTVSPSQAQSAQQsvvvsPPPAHSPSQSPTIIIHPQALVQ 420
Cdd:pfam09770 205 AQAKKPAQQ--PAPAPAQPPAAPPAQQAQ---QQQQFPPQIQQQQQPQQQPQQ-----PQQHPGQGHPVTILQRPQSPQP 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 421 PHPLVSSALHTGPNLQQATADQVQSTAQLNLPSHlpLPASPVVHIGPVQQSALVSPGQQivsptSHQQYSTLQSSPIPIA 500
Cdd:pfam09770 275 DPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNR--LSAARVGYPQNPQPGVQPAPAHQ-----AHRQQGSFGRQAPIIT 347


                  ....*.
gi 1958750414 501 TPPQMS 506
Cdd:pfam09770 348 HPQQLA 353
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 932-999 3.30e-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: 3.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958750414 932 PSIWTVDDVWAFIHSLpGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMK-LGPALKICARINSLKDS 999
Cdd:cd09505     2 LQDWSEEDVCTWLRSI-GLEQYVEVFRANNIDGKELLNLTKESLSKDLKIEsLGHRNKILRKIEELKMK 69
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 939-994 1.06e-05

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: 43.77  E-value: 1.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958750414 939 DVWAFIHSLpGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARIN 994
Cdd:cd09487     1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 339-586 4.52e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  339 SPSQDPPPSQHCIPLPNHGLSPASSNAQSQQHCSPIQSHPPPLTVSPSQAQSAQQSVVVS-PPPAHSPSQSPTiiihPQA 417
Cdd:PHA03247  2612 APPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPR----RRA 2687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  418 LVQP-HPLVSSALHTGPNLQQATADQVQSTAQLNLP----SHLPLPASPVVHIGPVQQSALVSPGQqiVSPTSHQQYSTL 492
Cdd:PHA03247  2688 ARPTvGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGPATPGG--PARPARPPTTAG 2765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  493 QSSPIPIATPPqmsASPPAQIPPLPLQSMQSLQVQPEILSQGQVLVQNALVSEEELPAAEAlvqlPFQTLPPPQTVAVNL 572
Cdd:PHA03247  2766 PPAPAPPAAPA---AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS----PAGPLPPPTSAQPTA 2838

                          250
                   ....*....|....
gi 1958750414  573 QVQPPAPVDPPVGM 586
Cdd:PHA03247  2839 PPPPPGPPPPSLPL 2852
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 935-997 7.11e-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: 41.63  E-value: 7.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958750414 935 WTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMStMNMKLGPALKICARINSLK 997
Cdd:cd09528     3 WTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLVD-MGLPHGPALLIIHSFNELN 64
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 935-997 2.22e-04

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 40.23  E-value: 2.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958750414 935 WTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSTMNMKLGPALKICARINSLK 997
Cdd:cd09535     3 WSPEQVAEWLLSAGFDDSVCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSLR 65
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 291-420 3.24e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 44.64  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 291 APASYSPIQPHSLIKHQQIPLHSPPPKVSHhqlilQQQQQQIQPITLQSPSQDPPPSQHCIPlpnHGLSPASSNAQSQQH 370
Cdd:pfam09770 213 QPAPAPAQPPAAPPAQQAQQQQQFPPQIQQ-----QQQPQQQPQQPQQHPGQGHPVTILQRP---QSPQPDPAQPSIQPQ 284

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 371 CSPIQSHPPPLTVSPSQA-------------QSAQQSVVVSPPPAH-------SPSQSPTIIIHPQALVQ 420
Cdd:pfam09770 285 AQQFHQQPPPVPVQPTQIlqnpnrlsaarvgYPQNPQPGVQPAPAHqahrqqgSFGRQAPIITHPQQLAQ 354
PHA03247 PHA03247
large tegument protein UL36; Provisional
 226-587 3.28e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  226 SSSQNGPPKSAGQTQSLTICHNKTTVTSSKISQRDPSPESKKGGSPGLESRSTAVTRTSSIHQLIAPASyspiqphslik 305
Cdd:PHA03247  2667 ARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAL----------- 2735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  306 hqqiPLHSPPPKVSHHQLILQQQQQQIQPITLQSPSQDPPPSQHCIPLPNHGLSPASSNAQSQQHCSPIQSHPPPLTV-- 383
Cdd:PHA03247  2736 ----PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAav 2811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  384 ---SPSQAQSAQQSVVVSPPPAHSPSQSPTIiihPQALVQPHPLVSSALHTGPNLQQATADQvqSTAQLNLPSHLPLPAS 460
Cdd:PHA03247  2812 lapAAALPPAASPAGPLPPPTSAQPTAPPPP---PGPPPPSLPLGGSVAPGGDVRRRPPSRS--PAAKPAAPARPPVRRL 2886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  461 PVVHIGPVQQSALVSPGQQIVSPTSHqqystLQSSPIPIATPPQmsasPPAQIPPLPLQSMQSLQVQPEILSQGQVLVQN 540
Cdd:PHA03247  2887 ARPAVSRSTESFALPPDQPERPPQPQ-----APPPPQPQPQPPP----PPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1958750414  541 ALVSEEELPAAEALVQLPFQTLPPPQTvavnlQVQPPAPVDPPVGMH 587
Cdd:PHA03247  2958 AVPQPWLGALVPGRVAVPRFRVPQPAP-----SREAPASSTPPLTGH 2999
PTZ00249 PTZ00249
variable surface protein Vir28; Provisional
 341-463 1.17e-03

variable surface protein Vir28; Provisional


Pssm-ID: 140276 [Multi-domain]  Cd Length: 516  Bit Score: 42.71  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 341 SQDPPPSQHCIPLPNHGLSPASSNAQSQQHCSPIQSHPPPLTVSPSQAQSAQQSVVVSPPPAHSPSQSPTIIIHPQALVQ 420
Cdd:PTZ00249  244 SFSSPHAHGRPPVETRPPNPVSVSSPQAHGRHPGETHTPPLVTVPSSKAHDRNPVQTPTPTSVSGYSSQAKGLEKQAGGE 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958750414 421 PH----------PLVSSALHTGPNLQQATADQVQSTAQLNLPSHLPLPASPVV 463
Cdd:PTZ00249  324 SErtssvpseqfPLPLPVLLPLGQSGPLESSESEETDEYAGPKGLPEPELELV 376
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 397-587 1.71e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 42.33  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 397 VSPPPAHSPSQSPTIIIHPQALVQPHPLVSSalhtgpnLQQATAD---QVQSTAQLNLPSHLPLPASPVVHIGPVQQSAL 473
Cdd:pfam09770 165 VAPKKAAAPAPAPQPAAQPASLPAPSRKMMS-------LEEVEAAmraQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFP 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 474 VSPGQQIVSPTSHQQ--YSTLQSSPIPIATPPQMSASPPAQIPPLPlQSMQSLQVQPEILSQGQVLVQNALVseeeLPAA 551
Cdd:pfam09770 238 PQIQQQQQPQQQPQQpqQHPGQGHPVTILQRPQSPQPDPAQPSIQP-QAQQFHQQPPPVPVQPTQILQNPNR----LSAA 312

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958750414 552 EALVQLPFQTLPPPQTVAVNLQVQPPAPVDPPVGMH 587
Cdd:pfam09770 313 RVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITH 348
PHA03247 PHA03247
large tegument protein UL36; Provisional
 261-682 1.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  261 PSPESKKGGSPGLESRSTAVTRTSSIHQLIAP-------ASYSPIQPHSLIK--HQQIPLHSPPPKVSHHQLILQQQQQQ 331
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPpqrprrrAARPTVGSLTSLAdpPPPPPTPEPAPHALVSATPLPPGPAA 2727

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  332 IQPITLQSPSQDPPPsqhciPLPNHGLSPASSNAQSQqhcspiqshpPPLTVSPSQAQSAQQSVVVSPPPAHSPSQSPTI 411
Cdd:PHA03247  2728 ARQASPALPAAPAPP-----AVPAGPATPGGPARPAR----------PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLS 2792

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  412 IIHPQALVQPHPLVSSALHTGPNlqqATADQVQSTAQLNLPSHLPLPASPVVHIGPVQQSalVSPGQQIVSPTSHQQYST 491
Cdd:PHA03247  2793 ESRESLPSPWDPADPPAAVLAPA---AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS--LPLGGSVAPGGDVRRRPP 2867

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  492 LQSSPIPIATPPQMSASPPAQipPLPLQSMQSLQVQPEilsqgqvlvqnalvsEEELPAAEALVQLPFQTLPPPQTVAVN 571
Cdd:PHA03247  2868 SRSPAAKPAAPARPPVRRLAR--PAVSRSTESFALPPD---------------QPERPPQPQAPPPPQPQPQPPPPPQPQ 2930

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414  572 LQVQPPAPVDPPvgmhlnqchlhkvfslkvyqvedvceeerpeesdecarmdrtpPPPTLSPAAITVGRGedlTSEHPLL 651
Cdd:PHA03247  2931 PPPPPPPRPQPP-------------------------------------------LAPTTDPAGAGEPSG---AVPQPWL 2964

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1958750414  652 EQVeLPAVASVSASVIKSPSDPTHVSAPAPP 682
Cdd:PHA03247  2965 GAL-VPGRVAVPRFRVPQPAPSREAPASSTP 2994
SAM_PNT smart00251
SAM / Pointed domain; A subfamily of the SAM domain
 932-976 2.18e-03

SAM / Pointed domain; A subfamily of the SAM domain


Pssm-ID: 128547  Cd Length: 82  Bit Score: 38.01  E-value: 2.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958750414  932 PSIWTVDDVWAFIhslpgcQDVADEFRAQEID-------GQALLLL-KEDHLM 976
Cdd:smart00251  17 PQLWTEDHVLEWL------EWAVKEFSLSPIDfskfdmsGKELCSMsKEEFLE 63
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 363-590 2.67e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.56  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 363 SNAQSQQHCSPIQSHPPPLTvSPSQAQSAQQSVVVSPPPAHSPSQSPT--------------------------IIIHPQ 416
Cdd:pfam09770  92 SDAIEEEQVRFNRQQPAARA-AQSSAQPPASSLPQYQYASQQSQQPSKpvrtgyekykepepipdlqvdaslwgVAPKKA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 417 ALVQPHPLVSSAlhtgPNLQQATADQVQS----TAQLNLPSHLPLPASPVVHIGPVQQSALVSPGQQIVSPTSHQQYSTL 492
Cdd:pfam09770 171 AAPAPAPQPAAQ----PASLPAPSRKMMSleevEAAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQP 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750414 493 QSSPIPiaTPPQMSASPPAQIpplpLQSMQSLQVQPEILSQGQVLVQNAlvseeelPAAEALVQLPFQTL-----PPPQT 567
Cdd:pfam09770 247 QQQPQQ--PQQHPGQGHPVTI----LQRPQSPQPDPAQPSIQPQAQQFH-------QQPPPVPVQPTQILqnpnrLSAAR 313

                         250       260
                  ....*....|....*....|...
gi 1958750414 568 VAVNLQVQPPAPVDPPVGMHLNQ 590
Cdd:pfam09770 314 VGYPQNPQPGVQPAPAHQAHRQQ 336
 
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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