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Conserved domains on  [gi|151301228|ref|NP_060362|]
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pre-mRNA-processing factor 40 homolog A isoform 1 [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];
110-769 7.90e-47

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: 177.58  E-value: 7.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 110 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 188
Cdd:COG5104    7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 189 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 268
Cdd:COG5104   87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 269 anastsasntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 348
Cdd:COG5104  103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 349 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 424
Cdd:COG5104  126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 425 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 503
Cdd:COG5104  204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 504 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 583
Cdd:COG5104  284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 584 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFV 662
Cdd:COG5104  363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISP 442

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 663 VEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------P 732
Cdd:COG5104  443 TDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpK 522

                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 151301228 733 PIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 769
Cdd:COG5104  523 PSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
110-769 7.90e-47

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 177.58  E-value: 7.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 110 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 188
Cdd:COG5104    7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 189 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 268
Cdd:COG5104   87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 269 anastsasntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 348
Cdd:COG5104  103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 349 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 424
Cdd:COG5104  126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 425 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 503
Cdd:COG5104  204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 504 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 583
Cdd:COG5104  284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 584 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFV 662
Cdd:COG5104  363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISP 442

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 663 VEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------P 732
Cdd:COG5104  443 TDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpK 522

                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 151301228 733 PIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 769
Cdd:COG5104  523 PSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 368-417 5.38e-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: 69.79  E-value: 5.38e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 151301228  368 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 417
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 119-146 2.44e-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: 2.44e-11
                         10        20
                 ....*....|....*....|....*...
gi 151301228 119 WTEHKSPDGRTYYYNTETKQSTWEKPDD 146
Cdd:cd00201    4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 119-146 7.66e-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: 7.66e-11
                           10        20
                   ....*....|....*....|....*...
gi 151301228   119 WTEHKSPDGRTYYYNTETKQSTWEKPDD 146
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03255 PHA03255
BDLF3; Provisional
 218-360 1.84e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.12  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 218 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTvpvVPEPEVTSIVAT 297
Cdd:PHA03255  54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151301228 298 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 360
Cdd:PHA03255 131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
110-769 7.90e-47

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 177.58  E-value: 7.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 110 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 188
Cdd:COG5104    7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 189 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 268
Cdd:COG5104   87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 269 anastsasntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 348
Cdd:COG5104  103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 349 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 424
Cdd:COG5104  126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 425 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 503
Cdd:COG5104  204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 504 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 583
Cdd:COG5104  284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 584 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFV 662
Cdd:COG5104  363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISP 442

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 663 VEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------P 732
Cdd:COG5104  443 TDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpK 522

                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 151301228 733 PIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 769
Cdd:COG5104  523 PSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 368-417 5.38e-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: 69.79  E-value: 5.38e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 151301228  368 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 417
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 119-146 2.44e-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: 2.44e-11
                         10        20
                 ....*....|....*....|....*...
gi 151301228 119 WTEHKSPDGRTYYYNTETKQSTWEKPDD 146
Cdd:cd00201    4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 119-144 4.10e-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: 4.10e-11
                          10        20
                  ....*....|....*....|....*.
gi 151301228  119 WTEHKSPDGRTYYYNTETKQSTWEKP 144
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 119-146 7.66e-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: 7.66e-11
                           10        20
                   ....*....|....*....|....*...
gi 151301228   119 WTEHKSPDGRTYYYNTETKQSTWEKPDD 146
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 367-420 7.43e-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: 55.27  E-value: 7.43e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 151301228   367 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 420
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 717-771 1.40e-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: 51.81  E-value: 1.40e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 151301228   717 KRKESAFKSMLKQAaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 771
Cdd:smart00441   1 EEAKEAFKELLKEH-EVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 157-187 1.91e-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: 1.91e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 151301228 157 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 187
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 156-187 2.06e-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: 2.06e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 151301228   156 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 187
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 159-185 6.90e-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: 6.90e-08
                          10        20
                  ....*....|....*....|....*..
gi 151301228  159 PWKEYKSDSGKPYYYNSQTKESRWAKP 185
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 501-560 1.71e-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: 45.64  E-value: 1.71e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228   501 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 560
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 718-769 1.29e-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: 43.21  E-value: 1.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 151301228  718 RKESAFKSMLKQaaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 769
Cdd:pfam01846   1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
 218-360 1.84e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.12  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 218 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTvpvVPEPEVTSIVAT 297
Cdd:PHA03255  54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151301228 298 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 360
Cdd:PHA03255 131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 585-637 4.68e-04

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: 38.59  E-value: 4.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 151301228  585 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMlgQPGSTALDLFKFY 637
Cdd:pfam01846   4 EAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
alt PHA02566
ADP-ribosyltransferase; Provisional
 326-531 3.54e-03

ADP-ribosyltransferase; Provisional


Pssm-ID: 222881 [Multi-domain]  Cd Length: 684  Bit Score: 41.27  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 326 VEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFkELLKEKRVPSNASWEQAMKMIINDPRYSALA 405
Cdd:PHA02566 192 VYISKKTGEKVTKVEAIAASIAKEEEKRTDQAVITKTKISRRAIAKAQ-SLESDREAELFQKFENSANDYNKPAEAPLIP 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301228 406 KLSEKKQAFNAyKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMT-STTRYKKAEQMFGE-------MEVWNAISERdR 477
Cdd:PHA02566 271 PAEEIKTNEGS-GAIKTMVAASRFESSDYELDYFRKFIFLRHIGEVdEKIKLKISEAIKQEdqtsiknLEKFAASVDE-L 348

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 151301228 478 LEIYEDVLFFLSKKEKEQAKQLRKRNwealKNILDNMANVTYSTTWSEAQ-QYLM 531
Cdd:PHA02566 349 LEDYKDIVFENSLDALEWINDLNKGR----KGMPDEVKAELTRSKWKQAKtKFLM 399
 
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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