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Conserved domains on  [gi|2065208893|ref|NP_001382409|]
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pre-mRNA-processing factor 40 homolog A isoform 15 [Homo sapiens]

Protein Classification

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];
298-716 1.85e-31

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: 130.97  E-value: 1.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 298 EEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEK 373
Cdd:COG5104   126 RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQR 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 374 EEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWE 452
Cdd:COG5104   206 EEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALG 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 453 ALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRE 532
Cdd:COG5104   286 RLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRD 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 533 SFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFVVE 611
Cdd:COG5104   365 EFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISPTD 444

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 612 VNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------PPI 681
Cdd:COG5104   445 RRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpKPS 524

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2065208893 682 ELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 716
Cdd:COG5104   525 TWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 104-134 1.04e-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: 51.37  E-value: 1.04e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2065208893 104 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 134
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
PHA03255 super family cl31530
BDLF3; Provisional
 165-307 1.68e-04

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.12  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 165 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTvpvVPEPEVTSIVAT 244
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065208893 245 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 307
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
298-716 1.85e-31

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 130.97  E-value: 1.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 298 EEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEK 373
Cdd:COG5104   126 RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQR 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 374 EEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWE 452
Cdd:COG5104   206 EEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALG 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 453 ALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRE 532
Cdd:COG5104   286 RLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRD 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 533 SFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFVVE 611
Cdd:COG5104   365 EFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISPTD 444

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 612 VNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------PPI 681
Cdd:COG5104   445 RRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpKPS 524

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2065208893 682 ELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 716
Cdd:COG5104   525 TWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 315-364 7.79e-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: 7.79e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2065208893 315 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 364
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 314-367 1.11e-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: 54.89  E-value: 1.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2065208893  314 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 367
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 104-134 1.04e-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: 51.37  E-value: 1.04e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2065208893 104 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 134
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 103-134 1.09e-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: 51.45  E-value: 1.09e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2065208893  103 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 134
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 106-132 3.88e-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: 49.81  E-value: 3.88e-08
                          10        20
                  ....*....|....*....|....*..
gi 2065208893 106 PWKEYKSDSGKPYYYNSQTKESRWAKP 132
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
PHA03255 PHA03255
BDLF3; Provisional
 165-307 1.68e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.12  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 165 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTvpvVPEPEVTSIVAT 244
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065208893 245 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 307
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
alt PHA02566
ADP-ribosyltransferase; Provisional
 273-478 3.56e-03

ADP-ribosyltransferase; Provisional


Pssm-ID: 222881 [Multi-domain]  Cd Length: 684  Bit Score: 40.88  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 273 VEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFkELLKEKRVPSNASWEQAMKMIINDPRYSALA 352
Cdd:PHA02566  192 VYISKKTGEKVTKVEAIAASIAKEEEKRTDQAVITKTKISRRAIAKAQ-SLESDREAELFQKFENSANDYNKPAEAPLIP 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 353 KLSEKKQAFNAyKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMT-STTRYKKAEQMFGE-------MEVWNAISERdR 424
Cdd:PHA02566  271 PAEEIKTNEGS-GAIKTMVAASRFESSDYELDYFRKFIFLRHIGEVdEKIKLKISEAIKQEdqtsiknLEKFAASVDE-L 348

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2065208893 425 LEIYEDVLFFLSKKEKEQAKQLRKRNwealKNILDNMANVTYSTTWSEAQ-QYLM 478
Cdd:PHA02566  349 LEDYKDIVFENSLDALEWINDLNKGR----KGMPDEVKAELTRSKWKQAKtKFLM 399
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
298-716 1.85e-31

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 130.97  E-value: 1.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 298 EEESQPAKKTYTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEK 373
Cdd:COG5104   126 RLMSQYGITSTKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQR 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 374 EEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWE 452
Cdd:COG5104   206 EEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALG 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 453 ALKNILDNMANVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRE 532
Cdd:COG5104   286 RLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRD 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 533 SFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFVVE 611
Cdd:COG5104   365 EFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISPTD 444

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 612 VNTTFEDFVAII----SSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------PPI 681
Cdd:COG5104   445 RRAVDEIFEAIAekkeEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpKPS 524

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2065208893 682 ELDAVWEDIRERFVKEPAFEDitlESERKRIFKDF 716
Cdd:COG5104   525 TWDLASKELGESLEYKALGDE---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 315-364 7.79e-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: 7.79e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2065208893 315 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 364
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 314-367 1.11e-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: 54.89  E-value: 1.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2065208893  314 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 367
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 104-134 1.04e-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: 51.37  E-value: 1.04e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2065208893 104 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 134
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 103-134 1.09e-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: 51.45  E-value: 1.09e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2065208893  103 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 134
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 664-718 2.01e-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: 51.04  E-value: 2.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2065208893  664 KRKESAFKSMLKQAaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 718
Cdd:smart00441   1 EEAKEAFKELLKEH-EVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 106-132 3.88e-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: 49.81  E-value: 3.88e-08
                          10        20
                  ....*....|....*....|....*..
gi 2065208893 106 PWKEYKSDSGKPYYYNSQTKESRWAKP 132
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 448-507 2.36e-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: 45.26  E-value: 2.36e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893  448 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 507
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 665-716 1.64e-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: 42.83  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2065208893 665 RKESAFKSMLKQaaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 716
Cdd:pfam01846   1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
 165-307 1.68e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.12  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 165 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTvpvVPEPEVTSIVAT 244
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065208893 245 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 307
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 532-584 5.82e-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: 5.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2065208893 532 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMlgQPGSTALDLFKFY 584
Cdd:pfam01846   4 EAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
alt PHA02566
ADP-ribosyltransferase; Provisional
 273-478 3.56e-03

ADP-ribosyltransferase; Provisional


Pssm-ID: 222881 [Multi-domain]  Cd Length: 684  Bit Score: 40.88  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 273 VEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFkELLKEKRVPSNASWEQAMKMIINDPRYSALA 352
Cdd:PHA02566  192 VYISKKTGEKVTKVEAIAASIAKEEEKRTDQAVITKTKISRRAIAKAQ-SLESDREAELFQKFENSANDYNKPAEAPLIP 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208893 353 KLSEKKQAFNAyKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMT-STTRYKKAEQMFGE-------MEVWNAISERdR 424
Cdd:PHA02566  271 PAEEIKTNEGS-GAIKTMVAASRFESSDYELDYFRKFIFLRHIGEVdEKIKLKISEAIKQEdqtsiknLEKFAASVDE-L 348

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2065208893 425 LEIYEDVLFFLSKKEKEQAKQLRKRNwealKNILDNMANVTYSTTWSEAQ-QYLM 478
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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