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Conserved domains on  [gi|1475408880|ref|NP_001352525|]
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pre-mRNA-processing factor 40 homolog A isoform 4 [Homo sapiens]

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];
152-815 2.33e-45

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: 173.34  E-value: 2.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 152 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 230
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 231 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 310
Cdd:COG5104    87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 311 anastsasntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 390
Cdd:COG5104   103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 391 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 466
Cdd:COG5104   126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 467 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 545
Cdd:COG5104   204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 546 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 625
Cdd:COG5104   284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 626 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKDILK-D 704
Cdd:COG5104   363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYERETRtG 438

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 705 KGFVVEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA--- 777
Cdd:COG5104   439 QISPTDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtkt 518

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 1475408880 778 ---PPIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 815
Cdd:COG5104   519 gkpKPSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
152-815 2.33e-45

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 173.34  E-value: 2.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 152 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 230
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 231 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 310
Cdd:COG5104    87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 311 anastsasntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 390
Cdd:COG5104   103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 391 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 466
Cdd:COG5104   126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 467 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 545
Cdd:COG5104   204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 546 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 625
Cdd:COG5104   284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 626 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKDILK-D 704
Cdd:COG5104   363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYERETRtG 438

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 705 KGFVVEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA--- 777
Cdd:COG5104   439 QISPTDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtkt 518

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 1475408880 778 ---PPIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 815
Cdd:COG5104   519 gkpKPSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 410-459 4.17e-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: 70.18  E-value: 4.17e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1475408880 410 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 459
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 161-188 2.61e-11

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: 58.69  E-value: 2.61e-11
                          10        20
                  ....*....|....*....|....*...
gi 1475408880 161 WTEHKSPDGRTYYYNTETKQSTWEKPDD 188
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 161-188 8.60e-11

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: 57.61  E-value: 8.60e-11
                           10        20
                   ....*....|....*....|....*...
gi 1475408880  161 WTEHKSPDGRTYYYNTETKQSTWEKPDD 188
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03255 PHA03255
BDLF3; Provisional
 260-402 1.75e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.12  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 260 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTvpvVPEPEVTSIVAT 339
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475408880 340 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 402
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
152-815 2.33e-45

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 173.34  E-value: 2.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 152 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 230
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 231 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 310
Cdd:COG5104    87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 311 anastsasntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 390
Cdd:COG5104   103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 391 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 466
Cdd:COG5104   126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 467 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 545
Cdd:COG5104   204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 546 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 625
Cdd:COG5104   284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 626 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKDILK-D 704
Cdd:COG5104   363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYERETRtG 438

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 705 KGFVVEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA--- 777
Cdd:COG5104   439 QISPTDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtkt 518

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 1475408880 778 ---PPIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 815
Cdd:COG5104   519 gkpKPSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 410-459 4.17e-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: 70.18  E-value: 4.17e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1475408880 410 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 459
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 161-188 2.61e-11

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: 58.69  E-value: 2.61e-11
                          10        20
                  ....*....|....*....|....*...
gi 1475408880 161 WTEHKSPDGRTYYYNTETKQSTWEKPDD 188
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 161-186 4.55e-11

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: 58.29  E-value: 4.55e-11
                          10        20
                  ....*....|....*....|....*.
gi 1475408880 161 WTEHKSPDGRTYYYNTETKQSTWEKP 186
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 161-188 8.60e-11

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: 57.61  E-value: 8.60e-11
                           10        20
                   ....*....|....*....|....*...
gi 1475408880  161 WTEHKSPDGRTYYYNTETKQSTWEKPDD 188
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 409-462 4.78e-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: 56.04  E-value: 4.78e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1475408880  409 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 462
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 763-817 9.65e-09

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: 52.19  E-value: 9.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1475408880  763 KRKESAFKSMLKQAaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 817
Cdd:smart00441   1 EEAKEAFKELLKEH-EVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 199-229 2.03e-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: 50.60  E-value: 2.03e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1475408880 199 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 229
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 198-229 2.27e-08

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: 50.68  E-value: 2.27e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1475408880  198 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 229
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 201-227 7.53e-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: 49.04  E-value: 7.53e-08
                          10        20
                  ....*....|....*....|....*..
gi 1475408880 201 PWKEYKSDSGKPYYYNSQTKESRWAKP 227
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 543-602 1.20e-06

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: 46.41  E-value: 1.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880  543 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 602
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 764-815 1.08e-05

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: 43.60  E-value: 1.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1475408880 764 RKESAFKSMLKQaaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 815
Cdd:pfam01846   1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
 260-402 1.75e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.12  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 260 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTvpvVPEPEVTSIVAT 339
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475408880 340 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 402
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
alt PHA02566
ADP-ribosyltransferase; Provisional
 368-573 2.81e-03

ADP-ribosyltransferase; Provisional


Pssm-ID: 222881 [Multi-domain]  Cd Length: 684  Bit Score: 41.65  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 368 VEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFkELLKEKRVPSNASWEQAMKMIINDPRYSALA 447
Cdd:PHA02566  192 VYISKKTGEKVTKVEAIAASIAKEEEKRTDQAVITKTKISRRAIAKAQ-SLESDREAELFQKFENSANDYNKPAEAPLIP 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475408880 448 KLSEKKQAFNAyKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMT-STTRYKKAEQMFGE-------MEVWNAISERdR 519
Cdd:PHA02566  271 PAEEIKTNEGS-GAIKTMVAASRFESSDYELDYFRKFIFLRHIGEVdEKIKLKISEAIKQEdqtsiknLEKFAASVDE-L 348

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1475408880 520 LEIYEDVLFFLSKKEKEQAKQLRKRNwealKNILDNMANVTYSTTWSEAQ-QYLM 573
Cdd:PHA02566  349 LEDYKDIVFENSLDALEWINDLNKGR----KGMPDEVKAELTRSKWKQAKtKFLM 399
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 627-683 6.69e-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: 35.51  E-value: 6.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1475408880 627 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMLgqpvfsLGSTALDLFKFY 683
Cdd:pfam01846   4 EAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKALL------DGSEREELFEDY 50
 
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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