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Conserved domains on  [gi|1901005851|emb|CAD5314773|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

PRP40 family protein( domain architecture ID 1003925)

PRP40 family protein similar to Homo sapiens pre-mRNA-processing factor 40 homolog A that binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function

Gene Ontology:  GO:0000398|GO:0003723
PubMed:  26494226

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRP40 super family cl34905
Splicing factor [RNA processing and modification];
185-810 1.72e-48

Splicing factor [RNA processing and modification];


The actual alignment was detected with superfamily member COG5104:

Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 182.59  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 185 QSASDWQEHTSADGRKYYYNKRTKQSNWEKPLELMTPLERADASTVWKEFTTPEGKKYYYNKVTKESKWTIPEDLKLARE 264
Cdd:COG5104    12 EARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVEP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 265 QAQlasEKTSLSeagstplSHHAASSSDLAVStvtsvvpstssaltghssspiqaglavpvtrppsvapvtptsgaisdt 344
Cdd:COG5104    92 IAE---QKHDER-------SMIGGNGNDMAIT------------------------------------------------ 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 345 eattikgdnlssrgaddsnDGATAQNNEAENKEMSVNGKANlspagDKANVEEpmvyATKQEAKAAFKSLLESVNVHSDW 424
Cdd:COG5104   114 -------------------DHETSEPKYLLGRLMSQYGITS-----TKDAVYR----LTKEEAEKEFITMLKENQVDSTW 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 425 TWEQTLKEIVHDKRYGALRTLGERKQAFNEYLGQRKKVEAEERRRRQKKAREEFVKMLEECEELSSSLKWSKAMSLFEND 504
Cdd:COG5104   166 PIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKH 245
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 505 QRFKAVDRPRDREDLFDNYIVELERKEREKAAEEHRQYMADYRKFLETCDYiKAGTQWRKIQDRLEDDDR------CSCL 578
Cdd:COG5104   246 PYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGS-ETFIIWLLNHYVFDSVVRylknkeMKPL 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 579 EKIDRLIGFEEYILDLEKEEEELKRVEKEHVRRAERKNRDAFRTLLEEHVAAGILTAKTYWLDYCIELKDLPQYQAVASN 658
Cdd:COG5104   325 DRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGR 404
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 659 TsGSTPKDLFEDVTEELEKQYHEDKSYVKDAMKSRKISMVSSWLFEDFKSAISE-----DLSTQQISDINLKLIYDDLVG 733
Cdd:COG5104   405 T-GSSPLDLFFDFIVDLENMYGFARRSYERETRTGQISPTDRRAVDEIFEAIAEkkeegEIKFDKVDKEDISLIVDGLIK 483
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 734 RVKEKEEKEARKLQRLAEEFTNLLHTFKEITVA-------SNWEDSKQLVEESQEYRSIGDE-SVSQGLFE----EYITS 801
Cdd:COG5104   484 QRNEKIQQKLQNERRILEQKKHYFWLLLQRTYTktgkpkpSTWDLASKELGESLEYKALGDEdNIRRQIFEdfkpESSAP 563

                  ....*....
gi 1901005851 802 LQEKAKEKE 810
Cdd:COG5104   564 TAESATANL 572
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
71-336 9.19e-05

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.62  E-value: 9.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851   71 TSSSQAVSVP---YIQTNKILT--SGSTQPQPNAPPMTGFATsGPPFSSPytfVPSSYPQQQPTSLVQ-----PNSQMHV 140
Cdd:PRK10263   327 TTATQSWAAPvepVTQTPPVASvdVPPAQPTVAWQPVPGPQT-GEPVIAP---APEGYPQQSQYAQPAvqynePLQQPVQ 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  141 AGVPPAANTWPVPVNQSTSLVSPVQQTGQQTPVAVSTDPGNLTPQSASD----WQEHTSADGRKYYYNKRTKQSNWEKPl 216
Cdd:PRK10263   403 PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEqqstFAPQSTYQTEQTYQQPAAQEPLYQQP- 481
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  217 ELMTPLERADASTVWKEFTTPEGKKYYYNKVTKeskwtipedlKLAREQAQLASEKTSLSEAGSTPLSHHAASSSDLA-- 294
Cdd:PRK10263   482 QPVEQQPVVEPEPVVEETKPARPPLYYFEEVEE----------KRAREREQLAAWYQPIPEPVKEPEPIKSSLKAPSVaa 551
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1901005851  295 ---VSTVTSVVPSTSSALTGHSSSPIQAGLAVPVTRPPSVAPVTP 336
Cdd:PRK10263   552 vppVEAAAAVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRP 596
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
185-810 1.72e-48

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 182.59  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 185 QSASDWQEHTSADGRKYYYNKRTKQSNWEKPLELMTPLERADASTVWKEFTTPEGKKYYYNKVTKESKWTIPEDLKLARE 264
Cdd:COG5104    12 EARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVEP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 265 QAQlasEKTSLSeagstplSHHAASSSDLAVStvtsvvpstssaltghssspiqaglavpvtrppsvapvtptsgaisdt 344
Cdd:COG5104    92 IAE---QKHDER-------SMIGGNGNDMAIT------------------------------------------------ 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 345 eattikgdnlssrgaddsnDGATAQNNEAENKEMSVNGKANlspagDKANVEEpmvyATKQEAKAAFKSLLESVNVHSDW 424
Cdd:COG5104   114 -------------------DHETSEPKYLLGRLMSQYGITS-----TKDAVYR----LTKEEAEKEFITMLKENQVDSTW 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 425 TWEQTLKEIVHDKRYGALRTLGERKQAFNEYLGQRKKVEAEERRRRQKKAREEFVKMLEECEELSSSLKWSKAMSLFEND 504
Cdd:COG5104   166 PIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKH 245
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 505 QRFKAVDRPRDREDLFDNYIVELERKEREKAAEEHRQYMADYRKFLETCDYiKAGTQWRKIQDRLEDDDR------CSCL 578
Cdd:COG5104   246 PYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGS-ETFIIWLLNHYVFDSVVRylknkeMKPL 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 579 EKIDRLIGFEEYILDLEKEEEELKRVEKEHVRRAERKNRDAFRTLLEEHVAAGILTAKTYWLDYCIELKDLPQYQAVASN 658
Cdd:COG5104   325 DRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGR 404
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 659 TsGSTPKDLFEDVTEELEKQYHEDKSYVKDAMKSRKISMVSSWLFEDFKSAISE-----DLSTQQISDINLKLIYDDLVG 733
Cdd:COG5104   405 T-GSSPLDLFFDFIVDLENMYGFARRSYERETRTGQISPTDRRAVDEIFEAIAEkkeegEIKFDKVDKEDISLIVDGLIK 483
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 734 RVKEKEEKEARKLQRLAEEFTNLLHTFKEITVA-------SNWEDSKQLVEESQEYRSIGDE-SVSQGLFE----EYITS 801
Cdd:COG5104   484 QRNEKIQQKLQNERRILEQKKHYFWLLLQRTYTktgkpkpSTWDLASKELGESLEYKALGDEdNIRRQIFEdfkpESSAP 563

                  ....*....
gi 1901005851 802 LQEKAKEKE 810
Cdd:COG5104   564 TAESATANL 572
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
406-455 9.85e-15

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 69.02  E-value: 9.85e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1901005851 406 EAKAAFKSLLESVNVHSDWTWEQTLKEIVHDKRYGALRTLGERKQAFNEY 455
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
472-526 1.02e-10

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 57.97  E-value: 1.02e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1901005851  472 KKAREEFVKMLEECEELSSSLKWSKAMSLFENDQRFKAVDRPRDREDLFDNYIVE 526
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
188-217 4.46e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 52.53  E-value: 4.46e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 1901005851 188 SDWQEHTSADGRKYYYNKRTKQSNWEKPLE 217
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PRK10263 PRK10263
DNA translocase FtsK; Provisional
71-336 9.19e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.62  E-value: 9.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851   71 TSSSQAVSVP---YIQTNKILT--SGSTQPQPNAPPMTGFATsGPPFSSPytfVPSSYPQQQPTSLVQ-----PNSQMHV 140
Cdd:PRK10263   327 TTATQSWAAPvepVTQTPPVASvdVPPAQPTVAWQPVPGPQT-GEPVIAP---APEGYPQQSQYAQPAvqynePLQQPVQ 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  141 AGVPPAANTWPVPVNQSTSLVSPVQQTGQQTPVAVSTDPGNLTPQSASD----WQEHTSADGRKYYYNKRTKQSNWEKPl 216
Cdd:PRK10263   403 PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEqqstFAPQSTYQTEQTYQQPAAQEPLYQQP- 481
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  217 ELMTPLERADASTVWKEFTTPEGKKYYYNKVTKeskwtipedlKLAREQAQLASEKTSLSEAGSTPLSHHAASSSDLA-- 294
Cdd:PRK10263   482 QPVEQQPVVEPEPVVEETKPARPPLYYFEEVEE----------KRAREREQLAAWYQPIPEPVKEPEPIKSSLKAPSVaa 551
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1901005851  295 ---VSTVTSVVPSTSSALTGHSSSPIQAGLAVPVTRPPSVAPVTP 336
Cdd:PRK10263   552 vppVEAAAAVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRP 596
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
27-156 3.06e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  27 PAASQPFH--PYGHVPPnvqsqppqySQPIQQQQLFPVRPGQPVHITsssQAVSVPYIQTNKILTSGSTQPQPNAP-PMT 103
Cdd:pfam03154 398 PLSSLSTHhpPSAHPPP---------LQLMPQSQQLPPPPAQPPVLT---QSQSLPPPAASHPPTSGLHQVPSQSPfPQH 465
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1901005851 104 GFATSGPPF----SSPYTFVPSSYPQQQPTSLVQPNSQMHVagvpPAANTWPVPVNQ 156
Cdd:pfam03154 466 PFVPGGPPPitppSGPPTSTSSAMPGIQPPSSASVSSSGPV----PAAVSCPLPPVQ 518
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
185-810 1.72e-48

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 182.59  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 185 QSASDWQEHTSADGRKYYYNKRTKQSNWEKPLELMTPLERADASTVWKEFTTPEGKKYYYNKVTKESKWTIPEDLKLARE 264
Cdd:COG5104    12 EARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVEP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 265 QAQlasEKTSLSeagstplSHHAASSSDLAVStvtsvvpstssaltghssspiqaglavpvtrppsvapvtptsgaisdt 344
Cdd:COG5104    92 IAE---QKHDER-------SMIGGNGNDMAIT------------------------------------------------ 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 345 eattikgdnlssrgaddsnDGATAQNNEAENKEMSVNGKANlspagDKANVEEpmvyATKQEAKAAFKSLLESVNVHSDW 424
Cdd:COG5104   114 -------------------DHETSEPKYLLGRLMSQYGITS-----TKDAVYR----LTKEEAEKEFITMLKENQVDSTW 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 425 TWEQTLKEIVHDKRYGALRTLGERKQAFNEYLGQRKKVEAEERRRRQKKAREEFVKMLEECEELSSSLKWSKAMSLFEND 504
Cdd:COG5104   166 PIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKH 245
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 505 QRFKAVDRPRDREDLFDNYIVELERKEREKAAEEHRQYMADYRKFLETCDYiKAGTQWRKIQDRLEDDDR------CSCL 578
Cdd:COG5104   246 PYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGS-ETFIIWLLNHYVFDSVVRylknkeMKPL 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 579 EKIDRLIGFEEYILDLEKEEEELKRVEKEHVRRAERKNRDAFRTLLEEHVAAGILTAKTYWLDYCIELKDLPQYQAVASN 658
Cdd:COG5104   325 DRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGR 404
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 659 TsGSTPKDLFEDVTEELEKQYHEDKSYVKDAMKSRKISMVSSWLFEDFKSAISE-----DLSTQQISDINLKLIYDDLVG 733
Cdd:COG5104   405 T-GSSPLDLFFDFIVDLENMYGFARRSYERETRTGQISPTDRRAVDEIFEAIAEkkeegEIKFDKVDKEDISLIVDGLIK 483
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 734 RVKEKEEKEARKLQRLAEEFTNLLHTFKEITVA-------SNWEDSKQLVEESQEYRSIGDE-SVSQGLFE----EYITS 801
Cdd:COG5104   484 QRNEKIQQKLQNERRILEQKKHYFWLLLQRTYTktgkpkpSTWDLASKELGESLEYKALGDEdNIRRQIFEdfkpESSAP 563

                  ....*....
gi 1901005851 802 LQEKAKEKE 810
Cdd:COG5104   564 TAESATANL 572
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
406-455 9.85e-15

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 69.02  E-value: 9.85e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1901005851 406 EAKAAFKSLLESVNVHSDWTWEQTLKEIVHDKRYGALRTLGERKQAFNEY 455
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
473-523 1.31e-13

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 65.94  E-value: 1.31e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1901005851 473 KAREEFVKMLEECEeLSSSLKWSKAMSLFENDQRFKAVDRPRDREDLFDNY 523
Cdd:pfam01846   1 KAREAFKELLKEHK-ITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
472-526 1.02e-10

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 57.97  E-value: 1.02e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1901005851  472 KKAREEFVKMLEECEELSSSLKWSKAMSLFENDQRFKAVDRPRDREDLFDNYIVE 526
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
188-217 4.46e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 52.53  E-value: 4.46e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 1901005851 188 SDWQEHTSADGRKYYYNKRTKQSNWEKPLE 217
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
188-215 1.77e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 50.58  E-value: 1.77e-08
                          10        20
                  ....*....|....*....|....*...
gi 1901005851 188 SDWQEHTSADGRKYYYNKRTKQSNWEKP 215
Cdd:pfam00397   3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
406-458 6.85e-08

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 49.88  E-value: 6.85e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1901005851  406 EAKAAFKSLLESVNV-HSDWTWEQTLKEIVHDKRYGALRTLGERKQAFNEYLGQ 458
Cdd:smart00441   2 EAKEAFKELLKEHEViTPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
231-258 9.16e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 48.68  E-value: 9.16e-08
                          10        20
                  ....*....|....*....|....*...
gi 1901005851 231 WKEFTTPEGKKYYYNKVTKESKWTIPED 258
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
231-256 1.02e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 48.66  E-value: 1.02e-07
                          10        20
                  ....*....|....*....|....*.
gi 1901005851 231 WKEFTTPEGKKYYYNKVTKESKWTIP 256
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
190-215 1.17e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.37  E-value: 1.17e-07
                           10        20
                   ....*....|....*....|....*.
gi 1901005851  190 WQEHTSADGRKYYYNKRTKQSNWEKP 215
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKP 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
231-258 3.73e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 47.21  E-value: 3.73e-07
                           10        20
                   ....*....|....*....|....*...
gi 1901005851  231 WKEFTTPEGKKYYYNKVTKESKWTIPED 258
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
PRK10263 PRK10263
DNA translocase FtsK; Provisional
71-336 9.19e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.62  E-value: 9.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851   71 TSSSQAVSVP---YIQTNKILT--SGSTQPQPNAPPMTGFATsGPPFSSPytfVPSSYPQQQPTSLVQ-----PNSQMHV 140
Cdd:PRK10263   327 TTATQSWAAPvepVTQTPPVASvdVPPAQPTVAWQPVPGPQT-GEPVIAP---APEGYPQQSQYAQPAvqynePLQQPVQ 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  141 AGVPPAANTWPVPVNQSTSLVSPVQQTGQQTPVAVSTDPGNLTPQSASD----WQEHTSADGRKYYYNKRTKQSNWEKPl 216
Cdd:PRK10263   403 PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEqqstFAPQSTYQTEQTYQQPAAQEPLYQQP- 481
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  217 ELMTPLERADASTVWKEFTTPEGKKYYYNKVTKeskwtipedlKLAREQAQLASEKTSLSEAGSTPLSHHAASSSDLA-- 294
Cdd:PRK10263   482 QPVEQQPVVEPEPVVEETKPARPPLYYFEEVEE----------KRAREREQLAAWYQPIPEPVKEPEPIKSSLKAPSVaa 551
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1901005851  295 ---VSTVTSVVPSTSSALTGHSSSPIQAGLAVPVTRPPSVAPVTP 336
Cdd:PRK10263   552 vppVEAAAAVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRP 596
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
251-389 9.95e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 46.11  E-value: 9.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 251 SKWTIPEDLKLAREQAQLASEKTSLSEAGSTPLSHHAASSSDLAV------STVTSVVPSTSSALTGHSSSPIQAglAVP 324
Cdd:pfam17823  73 TKGTSAAHLNSTEVTAEHTPHGTDLSEPATREGAADGAASRALAAaassspSSAAQSLPAAIAALPSEAFSAPRA--AAC 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901005851 325 VTrPPSVAPVTPTSGAISDTEATTIKGDNLSSRGADDSNDGATAQNNEAenkemSVNGKANLSPA 389
Cdd:pfam17823 151 RA-NASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTA-----ASSAPATLTPA 209
PHA03369 PHA03369
capsid maturational protease; Provisional
76-377 2.52e-04

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 44.99  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  76 AVSVPYIQTNKILTSGSTQPQPNAPPMTGFATSGPPFSSPYTFVPSSYPQQQPTSLVQPNSQMHVAGVPPAANTWPVPVN 155
Cdd:PHA03369  363 AAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTN 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 156 QSTSLVSPVQQ--TGQQTPVAVSTDPGNLTPQSASDWQEHTSAdgRKYyynkRTKQSNWEKPLELMTPLERADASTVwKE 233
Cdd:PHA03369  443 PYVMPISMANMvyPGHPQEHGHERKRKRGGELKEELIETLKLV--KKL----KEEQESLAKELEATAHKSEIKKIAE-SE 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851 234 FTTPEGKKYYYNKVTKESKWTIPEDLKLAREQAQLASEKTSLSEAGSTPLSHHAASSSDLAVS--TVTSVVPSTSSALTG 311
Cdd:PHA03369  516 FKNAGAKTAAANIEPNCSADAAAPATKRARPETKTELEAVVRFPYQIRNMESPAFVHSFTSTTlaAAAGQGSDTAEALAG 595
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901005851 312 ------HSSSPIQAGL-----AVPVTrPPSVAPVTPTSGAISDTEATTIKGdnlssrgaddSNDGATAQNNEAENKE 377
Cdd:PHA03369  596 aietllTQASAQPAGLslpapAVPVN-ASTPASTPPPLAPQEPPQPGTSAP----------SLETSLPQQKPVLSKG 661
PRK10856 PRK10856
cytoskeleton protein RodZ;
72-200 4.95e-04

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 43.48  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  72 SSSQAVSVPyIQTNKILTSGSTQPQPNAPPMTGFATSGPPFSSPytfvPSSYPQQQPTSLVQPNSqmhvAGVPPAANTWP 151
Cdd:PRK10856  155 SQNSGQSVP-LDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATA----PAPAVDPQQNAVVAPSQ----ANVDTAATPAP 225
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1901005851 152 VPV-NQSTSLVSPVQQTGQQTPVAvstDPGNLTPQ-SASDWQEHTSADGRK 200
Cdd:PRK10856  226 AAPaTPDGAAPLPTDQAGVSTPAA---DPNALVMNfTADCWLEVTDATGKK 273
PHA03247 PHA03247
large tegument protein UL36; Provisional
5-184 1.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851    5 PPQSSgtqfRPMVPGQ-QGQHFVPAASQPFHPYGHVPPNVQSQPPQYSQPIQQQQLFPVRPGQPVHITSSSQAVSVPYIQ 83
Cdd:PHA03247  2592 PPQSA----RPRAPVDdRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA 2667
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851   84 TNKILTSGSTQP-----QPNAPPMTGFATS--GPPFSSPytfVPSSYPQQQPTSLVQPNSQMHVAGVPPAANTWPVPVNQ 156
Cdd:PHA03247  2668 RRLGRAAQASSPpqrprRRAARPTVGSLTSlaDPPPPPP---TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
                          170       180
                   ....*....|....*....|....*...
gi 1901005851  157 STSLVSPVQQTGQQTPVAVSTDPGNLTP 184
Cdd:PHA03247  2745 PAGPATPGGPARPARPPTTAGPPAPAPP 2772
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
615-670 2.96e-03

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 36.67  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1901005851 615 KNRDAFRTLLEEHVaagiLTAKTYWLDYCIELKDLPQYQAVasnTSGSTPKDLFED 670
Cdd:pfam01846   1 KAREAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKAL---LDGSEREELFED 49
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
27-156 3.06e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  27 PAASQPFH--PYGHVPPnvqsqppqySQPIQQQQLFPVRPGQPVHITsssQAVSVPYIQTNKILTSGSTQPQPNAP-PMT 103
Cdd:pfam03154 398 PLSSLSTHhpPSAHPPP---------LQLMPQSQQLPPPPAQPPVLT---QSQSLPPPAASHPPTSGLHQVPSQSPfPQH 465
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1901005851 104 GFATSGPPF----SSPYTFVPSSYPQQQPTSLVQPNSQMHVagvpPAANTWPVPVNQ 156
Cdd:pfam03154 466 PFVPGGPPPitppSGPPTSTSSAMPGIQPPSSASVSSSGPV----PAAVSCPLPPVQ 518
APC_basic pfam05956
APC basic domain; This region of the APC family of proteins is known as the basic domain. It ...
88-184 5.71e-03

APC basic domain; This region of the APC family of proteins is known as the basic domain. It contains a high proportion of positively charged amino acids and interacts with microtubules.


Pssm-ID: 428690 [Multi-domain]  Cd Length: 336  Bit Score: 39.86  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901005851  88 LTSGSTQPQPNAPPmtGFATSGPPFSSPYTFVPSSYPQQQPTSLVQPNSQMHVAGVPPAANTWPVPVNQSTSLV------ 161
Cdd:pfam05956  58 LADLSPPKRSATPP--ARISKAPSSGSSRDSTPSRPPQKKLTSPSQSPGRLPGSGGRNKLSPLPKTKSPARASTkksgsh 135
                          90       100
                  ....*....|....*....|....*..
gi 1901005851 162 ----SPVQQTGQQTPVAVSTDPGNLTP 184
Cdd:pfam05956 136 ktqkSPVRIPFMQTPTKQTGLPRNPSP 162
 
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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