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Conserved domains on  [gi|672045150|ref|XP_008759931|]
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pre-mRNA-processing factor 40 homolog A isoform X8 [Rattus norvegicus]

Protein Classification

pre-mRNA-processing factor 40 family protein( domain architecture ID 13418230)

pre-mRNA-processing factor 40 (PRPF40) family protein similar to mammalian PRPF40 homologs A and B that may be involved in pre-mRNA splicing; contains WW and FF domains

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];
223-758 1.37e-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: 174.11  E-value: 1.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  223 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEgyqnti 302
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVE------ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  303 vagglitksnlhamikaeesskqeectttstapvptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgs 382
Cdd:COG5104       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  383 vPVAPEPEVTSIVATAVDNENTVTASAEEQaqlanttalqdlsgdissntgeeppkqetvtdftPKKE--EEESQPAKKT 460
Cdd:COG5104    91 -PIAEQKHDERSMIGGNGNDMAITDHETSE----------------------------------PKYLlgRLMSQYGITS 135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  461 YTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEA 536
Cdd:COG5104   136 TKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKY 215

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  537 KESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMA 615
Cdd:COG5104   216 INEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLG 295

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  616 NVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELH 695
Cdd:COG5104   296 SETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLY 374

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672045150  696 EHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 758
Cdd:COG5104   375 SEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 821-875 2.01e-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: 54.12  E-value: 2.01e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 672045150    821 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 875
Cdd:smart00441    1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
223-758 1.37e-45

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 174.11  E-value: 1.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  223 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEgyqnti 302
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVE------ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  303 vagglitksnlhamikaeesskqeectttstapvptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgs 382
Cdd:COG5104       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  383 vPVAPEPEVTSIVATAVDNENTVTASAEEQaqlanttalqdlsgdissntgeeppkqetvtdftPKKE--EEESQPAKKT 460
Cdd:COG5104    91 -PIAEQKHDERSMIGGNGNDMAITDHETSE----------------------------------PKYLlgRLMSQYGITS 135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  461 YTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEA 536
Cdd:COG5104   136 TKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKY 215

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  537 KESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMA 615
Cdd:COG5104   216 INEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLG 295

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  616 NVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELH 695
Cdd:COG5104   296 SETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLY 374

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672045150  696 EHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 758
Cdd:COG5104   375 SEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 468-517 1.57e-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: 1.57e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 672045150   468 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 517
Cdd:pfam01846    1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 223-250 2.79e-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: 2.79e-11
                          10        20
                  ....*....|....*....|....*...
gi 672045150  223 WTEHKSPDGRTYYYNTETKQSTWEKPDD 250
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 223-250 1.22e-10

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: 57.23  E-value: 1.22e-10
                            10        20
                    ....*....|....*....|....*...
gi 672045150    223 WTEHKSPDGRTYYYNTETKQSTWEKPDD 250
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 821-875 2.01e-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: 54.12  E-value: 2.01e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 672045150    821 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 875
Cdd:smart00441    1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 822-873 5.67e-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: 5.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 672045150   822 RKESAFKSMLKQatPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 873
Cdd:pfam01846    1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
 322-460 7.79e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 39.12  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  322 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAaananTSTTPTNTVGSVPVAPE------PEVTSIV 395
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNAS-----TINVTTKVTAQNITATEagtgtsTGVTSNV 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672045150  396 ATavdnENTVTASAEEQAQLAnTTALQDLSGDISSNTGEEPPKQETVTDftpkkeeeESQPAKKT 460
Cdd:PHA03255  129 TT----RSSSTTSATTRITNA-TTLAPTLSSKGTSNATKTTAELPTVPD--------ERQPSLSY 180
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
223-758 1.37e-45

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 174.11  E-value: 1.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  223 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEgyqnti 302
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVE------ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  303 vagglitksnlhamikaeesskqeectttstapvptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgs 382
Cdd:COG5104       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  383 vPVAPEPEVTSIVATAVDNENTVTASAEEQaqlanttalqdlsgdissntgeeppkqetvtdftPKKE--EEESQPAKKT 460
Cdd:COG5104    91 -PIAEQKHDERSMIGGNGNDMAITDHETSE----------------------------------PKYLlgRLMSQYGITS 135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  461 YTWN----TKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEA 536
Cdd:COG5104   136 TKDAvyrlTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKY 215

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  537 KESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMA 615
Cdd:COG5104   216 INEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLG 295

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  616 NVTYsTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELH 695
Cdd:COG5104   296 SETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLY 374

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672045150  696 EHGQLHSMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 758
Cdd:COG5104   375 SEGKIYYRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 468-517 1.57e-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: 1.57e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 672045150   468 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 517
Cdd:pfam01846    1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 223-250 2.79e-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: 2.79e-11
                          10        20
                  ....*....|....*....|....*...
gi 672045150  223 WTEHKSPDGRTYYYNTETKQSTWEKPDD 250
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 223-248 5.64e-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: 57.90  E-value: 5.64e-11
                           10        20
                   ....*....|....*....|....*.
gi 672045150   223 WTEHKSPDGRTYYYNTETKQSTWEKP 248
Cdd:pfam00397    5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 223-250 1.22e-10

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: 57.23  E-value: 1.22e-10
                            10        20
                    ....*....|....*....|....*...
gi 672045150    223 WTEHKSPDGRTYYYNTETKQSTWEKPDD 250
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 467-520 1.38e-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: 57.58  E-value: 1.38e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 672045150    467 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 520
Cdd:smart00441    1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 821-875 2.01e-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: 54.12  E-value: 2.01e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 672045150    821 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 875
Cdd:smart00441    1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 261-291 2.17e-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: 2.17e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 672045150  261 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 291
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 260-291 3.16e-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: 50.29  E-value: 3.16e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 672045150    260 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 291
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 263-289 9.05e-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: 9.05e-08
                           10        20
                   ....*....|....*....|....*..
gi 672045150   263 PWKEYKSDSGKPYYYNSQTKESRWAKP 289
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 601-660 4.03e-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: 4.03e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150    601 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 660
Cdd:smart00441    1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 822-873 5.67e-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: 5.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 672045150   822 RKESAFKSMLKQatPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 873
Cdd:pfam01846    1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 685-741 3.49e-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: 3.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 672045150   685 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMLgqpvfsLGSTALDLFKFY 741
Cdd:pfam01846    4 EAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKALL------DGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
 322-460 7.79e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 39.12  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672045150  322 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAaananTSTTPTNTVGSVPVAPE------PEVTSIV 395
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNAS-----TINVTTKVTAQNITATEagtgtsTGVTSNV 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672045150  396 ATavdnENTVTASAEEQAQLAnTTALQDLSGDISSNTGEEPPKQETVTDftpkkeeeESQPAKKT 460
Cdd:PHA03255  129 TT----RSSSTTSATTRITNA-TTLAPTLSSKGTSNATKTTAELPTVPD--------ERQPSLSY 180
 
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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