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Conserved domains on  [gi|966976407|ref|XP_014965610|]
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pre-mRNA-processing factor 40 homolog A isoform X1 [Macaca mulatta]

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];
216-879 1.02e-46

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: 1.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  216 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 294
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  295 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 374
Cdd:COG5104    87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  375 anaststsntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 454
Cdd:COG5104   103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  455 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 530
Cdd:COG5104   126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  531 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 609
Cdd:COG5104   204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  610 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 689
Cdd:COG5104   284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  690 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKDILK-D 768
Cdd:COG5104   363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYERETRtG 438
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  769 KGFVVEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA--- 841
Cdd:COG5104   439 QISPTDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtkt 518
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 966976407  842 ---PPIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 879
Cdd:COG5104   519 gkpKPSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
216-879 1.02e-46

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 177.58  E-value: 1.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  216 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 294
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  295 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 374
Cdd:COG5104    87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  375 anaststsntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 454
Cdd:COG5104   103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  455 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 530
Cdd:COG5104   126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  531 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 609
Cdd:COG5104   204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  610 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 689
Cdd:COG5104   284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  690 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKDILK-D 768
Cdd:COG5104   363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYERETRtG 438
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  769 KGFVVEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA--- 841
Cdd:COG5104   439 QISPTDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtkt 518
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 966976407  842 ---PPIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 879
Cdd:COG5104   519 gkpKPSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
474-523 1.64e-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: 71.33  E-value: 1.64e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 966976407   474 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 523
Cdd:pfam01846    1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
225-252 2.07e-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: 59.08  E-value: 2.07e-11
                          10        20
                  ....*....|....*....|....*...
gi 966976407  225 WTEHKSPDGRTYYYNTETKQSTWEKPDD 252
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
225-252 7.91e-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: 7.91e-11
                            10        20
                    ....*....|....*....|....*...
gi 966976407    225 WTEHKSPDGRTYYYNTETKQSTWEKPDD 252
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03255 PHA03255
BDLF3; Provisional
324-466 3.12e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 43.35  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  324 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSTSNTVSGTvpvVPEPEVTSIVAT 403
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976407  404 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 466
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
216-879 1.02e-46

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 177.58  E-value: 1.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  216 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 294
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  295 EdlegyqntivagslitksnlhamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaan 374
Cdd:COG5104    87 K------------------------KVEPIAEQKHDERSM---------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  375 anaststsntvsgtvpvvpepevtsivATVVDNEntvtisteeqaqltstPAIQDqsvevssntGEETSKQETVAdftpk 454
Cdd:COG5104   103 ---------------------------IGGNGND----------------MAITD---------HETSEPKYLLG----- 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  455 keEEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKE 530
Cdd:COG5104   126 --RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKD 203
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  531 EKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRN 609
Cdd:COG5104   204 QREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTA 283
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  610 WEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKN 689
Cdd:COG5104   284 LGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHH 362
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  690 RESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKDILK-D 768
Cdd:COG5104   363 RDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYERETRtG 438
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  769 KGFVVEVNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA--- 841
Cdd:COG5104   439 QISPTDRRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtkt 518
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 966976407  842 ---PPIELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 879
Cdd:COG5104   519 gkpKPSTWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
474-523 1.64e-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: 71.33  E-value: 1.64e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 966976407   474 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 523
Cdd:pfam01846    1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
225-252 2.07e-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: 59.08  E-value: 2.07e-11
                          10        20
                  ....*....|....*....|....*...
gi 966976407  225 WTEHKSPDGRTYYYNTETKQSTWEKPDD 252
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
225-250 4.07e-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: 4.07e-11
                           10        20
                   ....*....|....*....|....*.
gi 966976407   225 WTEHKSPDGRTYYYNTETKQSTWEKP 250
Cdd:pfam00397    5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
225-252 7.91e-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: 7.91e-11
                            10        20
                    ....*....|....*....|....*...
gi 966976407    225 WTEHKSPDGRTYYYNTETKQSTWEKPDD 252
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
473-526 1.62e-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: 57.20  E-value: 1.62e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 966976407    473 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 526
Cdd:smart00441    1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
827-881 3.37e-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: 53.73  E-value: 3.37e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 966976407    827 KRKESAFKSMLKQAaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 881
Cdd:smart00441    1 EEAKEAFKELLKEH-EVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
263-293 1.69e-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: 50.99  E-value: 1.69e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 966976407  263 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 293
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
262-293 2.17e-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: 2.17e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 966976407    262 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 293
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
265-291 6.99e-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: 6.99e-08
                           10        20
                   ....*....|....*....|....*..
gi 966976407   265 PWKEYKSDSGKPYYYNSQTKESRWAKP 291
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
607-666 4.61e-07

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: 47.57  E-value: 4.61e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407    607 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 666
Cdd:smart00441    1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
828-879 5.93e-06

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: 44.37  E-value: 5.93e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 966976407   828 RKESAFKSMLKQaaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 879
Cdd:pfam01846    1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
324-466 3.12e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 43.35  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  324 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSTSNTVSGTvpvVPEPEVTSIVAT 403
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966976407  404 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 466
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
alt PHA02566
ADP-ribosyltransferase; Provisional
432-637 1.98e-03

ADP-ribosyltransferase; Provisional


Pssm-ID: 222881 [Multi-domain]  Cd Length: 684  Bit Score: 42.04  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  432 VEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFkELLKEKRVPSNASWEQAMKMIINDPRYSALA 511
Cdd:PHA02566  192 VYISKKTGEKVTKVEAIAASIAKEEEKRTDQAVITKTKISRRAIAKAQ-SLESDREAELFQKFENSANDYNKPAEAPLIP 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966976407  512 KLSEKKQAFNAyKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMT-STTRYKKAEQMFGE-------MEVWNAISERdR 583
Cdd:PHA02566  271 PAEEIKTNEGS-GAIKTMVAASRFESSDYELDYFRKFIFLRHIGEVdEKIKLKISEAIKQEdqtsiknLEKFAASVDE-L 348
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 966976407  584 LEIYEDVLFFLSKKEKEQAKQLRKRNwealKNILDNMANVTYSTTWSEAQ-QYLM 637
Cdd:PHA02566  349 LEDYKDIVFENSLDALEWINDLNKGR----KGMPDEVKAELTRSKWKQAKtKFLM 399
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
691-747 3.69e-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: 36.28  E-value: 3.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 966976407   691 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMLgqpvfsLGSTALDLFKFY 747
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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