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Conserved domains on  [gi|568992903|ref|XP_006521253|]
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pre-mRNA-processing factor 40 homolog B isoform X17 [Mus musculus]

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];
118-610 5.46e-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: 177.19  E-value: 5.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 118 AGTGPPRALWSEHVAPDGRIYYYNADDKQSVWEKPSVLKSKAELLLSQCPWKEYKSDTGKPYYYNNQSQESRWTRPKDLD 197
Cdd:COG5104    8 MASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 198 DLEALVKQESAgkqqtqqlqtlqpqppqpqpdpppippgpipvpmallEPEPGRSEDCDV-LEAAQPLEQGFLQREEgps 276
Cdd:COG5104   88 KVEPIAEQKHD-------------------------------------ERSMIGGNGNDMaITDHETSEPKYLLGRL--- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 277 SSTGQHRQPQEEEEAKpepersglswsNREKAKQAFKELLRDKAVPSNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAY 356
Cdd:COG5104  128 MSQYGITSTKDAVYRL-----------TKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKY 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 357 KAQREKEEKEEARLRAKEAKQTLQHFLEQHERMTSTTRYRRAEQTFGDLEVW-AVVPERERKEVYDDVLFFLAKKEKEQA 435
Cdd:COG5104  197 FENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYsSVVNEKTKRQTFQKYKDKLGCYEKYVG 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 436 KQLRRRNIQALKSILDGMSSVNFqTTWSQAQQYLMDNPSFAQDQQLQNMDKEDALICFEEHIRALEREEEEERERARLRE 515
Cdd:COG5104  277 KHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAA 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 516 RRQQRKNREAFQSFLDELHETGQLHSMSTWMELYPAVSTDVRFANMLGQPGSTPLDLFKFYVEELKARFHDEKKIIKDil 595
Cdd:COG5104  356 AQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYER-- 433

                        490
                 ....*....|....*
gi 568992903 596 kdrgfCVEVNTAFED 610
Cdd:COG5104  434 -----ETRTGQISPT 443
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 662-710 9.03e-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: 43.72  E-value: 9.03e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568992903   662 FRSMLRQAVPaLELGTAWEEVRERFVCDSAFEQITLESERIRLFREFLQ 710
Cdd:smart00441   7 FKELLKEHEV-ITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
118-610 5.46e-47

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 177.19  E-value: 5.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 118 AGTGPPRALWSEHVAPDGRIYYYNADDKQSVWEKPSVLKSKAELLLSQCPWKEYKSDTGKPYYYNNQSQESRWTRPKDLD 197
Cdd:COG5104    8 MASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 198 DLEALVKQESAgkqqtqqlqtlqpqppqpqpdpppippgpipvpmallEPEPGRSEDCDV-LEAAQPLEQGFLQREEgps 276
Cdd:COG5104   88 KVEPIAEQKHD-------------------------------------ERSMIGGNGNDMaITDHETSEPKYLLGRL--- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 277 SSTGQHRQPQEEEEAKpepersglswsNREKAKQAFKELLRDKAVPSNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAY 356
Cdd:COG5104  128 MSQYGITSTKDAVYRL-----------TKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKY 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 357 KAQREKEEKEEARLRAKEAKQTLQHFLEQHERMTSTTRYRRAEQTFGDLEVW-AVVPERERKEVYDDVLFFLAKKEKEQA 435
Cdd:COG5104  197 FENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYsSVVNEKTKRQTFQKYKDKLGCYEKYVG 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 436 KQLRRRNIQALKSILDGMSSVNFqTTWSQAQQYLMDNPSFAQDQQLQNMDKEDALICFEEHIRALEREEEEERERARLRE 515
Cdd:COG5104  277 KHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAA 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 516 RRQQRKNREAFQSFLDELHETGQLHSMSTWMELYPAVSTDVRFANMLGQPGSTPLDLFKFYVEELKARFHDEKKIIKDil 595
Cdd:COG5104  356 AQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYER-- 433

                        490
                 ....*....|....*
gi 568992903 596 kdrgfCVEVNTAFED 610
Cdd:COG5104  434 -----ETRTGQISPT 443
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 307-356 2.34e-14

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: 67.87  E-value: 2.34e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568992903  307 KAKQAFKELLRDKAVPSNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAY 356
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 306-359 1.24e-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: 1.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568992903   306 EKAKQAFKELLRDKAVP-SNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAYKAQ 359
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 166-195 1.86e-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: 1.86e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 568992903 166 CPWKEYKSDTGKPYYYNNQSQESRWTRPKD 195
Cdd:cd00201    2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 662-710 9.03e-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: 43.72  E-value: 9.03e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568992903   662 FRSMLRQAVPaLELGTAWEEVRERFVCDSAFEQITLESERIRLFREFLQ 710
Cdd:smart00441   7 FKELLKEHEV-ITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
118-610 5.46e-47

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 177.19  E-value: 5.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 118 AGTGPPRALWSEHVAPDGRIYYYNADDKQSVWEKPSVLKSKAELLLSQCPWKEYKSDTGKPYYYNNQSQESRWTRPKDLD 197
Cdd:COG5104    8 MASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 198 DLEALVKQESAgkqqtqqlqtlqpqppqpqpdpppippgpipvpmallEPEPGRSEDCDV-LEAAQPLEQGFLQREEgps 276
Cdd:COG5104   88 KVEPIAEQKHD-------------------------------------ERSMIGGNGNDMaITDHETSEPKYLLGRL--- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 277 SSTGQHRQPQEEEEAKpepersglswsNREKAKQAFKELLRDKAVPSNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAY 356
Cdd:COG5104  128 MSQYGITSTKDAVYRL-----------TKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKY 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 357 KAQREKEEKEEARLRAKEAKQTLQHFLEQHERMTSTTRYRRAEQTFGDLEVW-AVVPERERKEVYDDVLFFLAKKEKEQA 435
Cdd:COG5104  197 FENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYsSVVNEKTKRQTFQKYKDKLGCYEKYVG 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 436 KQLRRRNIQALKSILDGMSSVNFqTTWSQAQQYLMDNPSFAQDQQLQNMDKEDALICFEEHIRALEREEEEERERARLRE 515
Cdd:COG5104  277 KHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAA 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992903 516 RRQQRKNREAFQSFLDELHETGQLHSMSTWMELYPAVSTDVRFANMLGQPGSTPLDLFKFYVEELKARFHDEKKIIKDil 595
Cdd:COG5104  356 AQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYER-- 433

                        490
                 ....*....|....*
gi 568992903 596 kdrgfCVEVNTAFED 610
Cdd:COG5104  434 -----ETRTGQISPT 443
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 307-356 2.34e-14

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: 67.87  E-value: 2.34e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568992903  307 KAKQAFKELLRDKAVPSNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAY 356
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 306-359 1.24e-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: 1.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568992903   306 EKAKQAFKELLRDKAVP-SNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAYKAQ 359
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 127-152 1.52e-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: 50.97  E-value: 1.52e-08
                          10        20
                  ....*....|....*....|....*.
gi 568992903  127 WSEHVAPDGRIYYYNADDKQSVWEKP 152
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 166-195 1.86e-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: 1.86e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 568992903 166 CPWKEYKSDTGKPYYYNNQSQESRWTRPKD 195
Cdd:cd00201    2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 167-193 9.35e-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: 48.66  E-value: 9.35e-08
                          10        20
                  ....*....|....*....|....*..
gi 568992903  167 PWKEYKSDTGKPYYYNNQSQESRWTRP 193
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 127-152 1.32e-07

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: 48.29  E-value: 1.32e-07
                         10        20
                 ....*....|....*....|....*.
gi 568992903 127 WSEHVAPDGRIYYYNADDKQSVWEKP 152
Cdd:cd00201    4 WEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 167-195 1.76e-07

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: 47.98  E-value: 1.76e-07
                           10        20
                   ....*....|....*....|....*....
gi 568992903   167 PWKEYKSDTGKPYYYNNQSQESRWTRPKD 195
Cdd:smart00456   5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 127-152 3.29e-07

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: 47.21  E-value: 3.29e-07
                           10        20
                   ....*....|....*....|....*.
gi 568992903   127 WSEHVAPDGRIYYYNADDKQSVWEKP 152
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKP 31
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 521-576 1.10e-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: 45.91  E-value: 1.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568992903  521 KNREAFQSFLDELHetgqLHSMSTWMELYPAVSTDVRFANMlgQPGSTPLDLFKFY 576
Cdd:pfam01846   1 KAREAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 662-710 9.03e-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: 43.72  E-value: 9.03e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568992903   662 FRSMLRQAVPaLELGTAWEEVRERFVCDSAFEQITLESERIRLFREFLQ 710
Cdd:smart00441   7 FKELLKEHEV-ITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
 
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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