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Conserved domains on  [gi|16198009|gb|AAL13780|]
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LD24714p [Drosophila melanogaster]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRP40 super family cl34905
Splicing factor [RNA processing and modification];
54-634 9.53e-59

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: 210.32  E-value: 9.53e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009  54 TEWTEHKAPDGRPYYYNQNTKQSSWEKPEALMTPAELLHNQCPWKEYRSDTGKVYYHNVATKETCWEPPPEYvdmkakak 133
Cdd:COG5104  15 SEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER-------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 134 aeeAAAAAKAVAAMTSSSLAGMVPpaalasilpaalpVAPRLPTPEIHSPLTPSSNENSSSAMdqamaatlaaievpqqN 213
Cdd:COG5104  87 ---KKVEPIAEQKHDERSMIGGNG-------------NDMAITDHETSEPKYLLGRLMSQYGI----------------T 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 214 AKKDdksesAVVFKDKREAIESFKELLRDRNVPSNANWDQCVKIISKDPRYAAFKNLNERKQTFNAYKTQKIKDEREESR 293
Cdd:COG5104 135 STKD-----AVYRLTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEE 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 294 LKAKKAKEDLEQFLMSSDKMNSQMKYFRCEEVFAGTRTWTAV-PEPDRRDIYEDCIFNLAKREKEEARLLKKRNMKVLGE 372
Cdd:COG5104 210 NKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEE 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 373 LLESMTSINHaTTWSEAQVMLLDNVAFKNDVTLLGMDKEDALIVFEEHIRTLEKEEDEEREREKKRMKRQQRKNRDSFLA 452
Cdd:COG5104 290 VLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRT 368
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 453 LLDSLHEEGKLTSMSLWVELYPIISADLRFSAMLGQSGSTPLDLFKFYVENLKARFHDEKKII-REILKEKAFVVQAKTS 531
Cdd:COG5104 369 LLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYeRETRTGQISPTDRRAV 448
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 532 FEDFATVVCEDKRSASLDAGNVKLTYNSLLEKAEAIEKERMKEEVRRLRKLENEIKNE-WL---EANVSVAEPYESA--- 604
Cdd:COG5104 449 DEIFEAIAEKKEEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYfWLllqRTYTKTGKPKPSTwdl 528
                       570       580       590
                ....*....|....*....|....*....|..
gi 16198009 605 --KKLVEHLEAFALYEKEIGVEKIWEDFVKES 634
Cdd:COG5104 529 asKELGESLEYKALGDEDNIRRQIFEDFKPES 560
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
54-634 9.53e-59

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 210.32  E-value: 9.53e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009  54 TEWTEHKAPDGRPYYYNQNTKQSSWEKPEALMTPAELLHNQCPWKEYRSDTGKVYYHNVATKETCWEPPPEYvdmkakak 133
Cdd:COG5104  15 SEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER-------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 134 aeeAAAAAKAVAAMTSSSLAGMVPpaalasilpaalpVAPRLPTPEIHSPLTPSSNENSSSAMdqamaatlaaievpqqN 213
Cdd:COG5104  87 ---KKVEPIAEQKHDERSMIGGNG-------------NDMAITDHETSEPKYLLGRLMSQYGI----------------T 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 214 AKKDdksesAVVFKDKREAIESFKELLRDRNVPSNANWDQCVKIISKDPRYAAFKNLNERKQTFNAYKTQKIKDEREESR 293
Cdd:COG5104 135 STKD-----AVYRLTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEE 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 294 LKAKKAKEDLEQFLMSSDKMNSQMKYFRCEEVFAGTRTWTAV-PEPDRRDIYEDCIFNLAKREKEEARLLKKRNMKVLGE 372
Cdd:COG5104 210 NKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEE 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 373 LLESMTSINHaTTWSEAQVMLLDNVAFKNDVTLLGMDKEDALIVFEEHIRTLEKEEDEEREREKKRMKRQQRKNRDSFLA 452
Cdd:COG5104 290 VLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRT 368
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 453 LLDSLHEEGKLTSMSLWVELYPIISADLRFSAMLGQSGSTPLDLFKFYVENLKARFHDEKKII-REILKEKAFVVQAKTS 531
Cdd:COG5104 369 LLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYeRETRTGQISPTDRRAV 448
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 532 FEDFATVVCEDKRSASLDAGNVKLTYNSLLEKAEAIEKERMKEEVRRLRKLENEIKNE-WL---EANVSVAEPYESA--- 604
Cdd:COG5104 449 DEIFEAIAEKKEEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYfWLllqRTYTKTGKPKPSTwdl 528
                       570       580       590
                ....*....|....*....|....*....|..
gi 16198009 605 --KKLVEHLEAFALYEKEIGVEKIWEDFVKES 634
Cdd:COG5104 529 asKELGESLEYKALGDEDNIRRQIFEDFKPES 560
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
231-280 1.71e-13

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: 65.17  E-value: 1.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 16198009   231 EAIESFKELLRDRNVPSNANWDQCVKIISKDPRYAAFKNLNERKQTFNAY 280
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
56-82 7.84e-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: 57.15  E-value: 7.84e-11
                        10        20
                ....*....|....*....|....*..
gi 16198009  56 WTEHKAPDGRPYYYNQNTKQSSWEKPE 82
Cdd:cd00201   4 WEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
56-82 2.85e-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: 55.68  E-value: 2.85e-10
                           10        20
                   ....*....|....*....|....*..
gi 16198009     56 WTEHKAPDGRPYYYNQNTKQSSWEKPE 82
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPR 32
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
54-634 9.53e-59

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 210.32  E-value: 9.53e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009  54 TEWTEHKAPDGRPYYYNQNTKQSSWEKPEALMTPAELLHNQCPWKEYRSDTGKVYYHNVATKETCWEPPPEYvdmkakak 133
Cdd:COG5104  15 SEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER-------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 134 aeeAAAAAKAVAAMTSSSLAGMVPpaalasilpaalpVAPRLPTPEIHSPLTPSSNENSSSAMdqamaatlaaievpqqN 213
Cdd:COG5104  87 ---KKVEPIAEQKHDERSMIGGNG-------------NDMAITDHETSEPKYLLGRLMSQYGI----------------T 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 214 AKKDdksesAVVFKDKREAIESFKELLRDRNVPSNANWDQCVKIISKDPRYAAFKNLNERKQTFNAYKTQKIKDEREESR 293
Cdd:COG5104 135 STKD-----AVYRLTKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEE 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 294 LKAKKAKEDLEQFLMSSDKMNSQMKYFRCEEVFAGTRTWTAV-PEPDRRDIYEDCIFNLAKREKEEARLLKKRNMKVLGE 372
Cdd:COG5104 210 NKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEE 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 373 LLESMTSINHaTTWSEAQVMLLDNVAFKNDVTLLGMDKEDALIVFEEHIRTLEKEEDEEREREKKRMKRQQRKNRDSFLA 452
Cdd:COG5104 290 VLRSLGSETF-IIWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRT 368
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 453 LLDSLHEEGKLTSMSLWVELYPIISADLRFSAMLGQSGSTPLDLFKFYVENLKARFHDEKKII-REILKEKAFVVQAKTS 531
Cdd:COG5104 369 LLRKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYeRETRTGQISPTDRRAV 448
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16198009 532 FEDFATVVCEDKRSASLDAGNVKLTYNSLLEKAEAIEKERMKEEVRRLRKLENEIKNE-WL---EANVSVAEPYESA--- 604
Cdd:COG5104 449 DEIFEAIAEKKEEGEIKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYfWLllqRTYTKTGKPKPSTwdl 528
                       570       580       590
                ....*....|....*....|....*....|..
gi 16198009 605 --KKLVEHLEAFALYEKEIGVEKIWEDFVKES 634
Cdd:COG5104 529 asKELGESLEYKALGDEDNIRRQIFEDFKPES 560
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
231-280 1.71e-13

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: 65.17  E-value: 1.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 16198009   231 EAIESFKELLRDRNVPSNANWDQCVKIISKDPRYAAFKNLNERKQTFNAY 280
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
54-81 4.41e-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: 4.41e-11
                          10        20
                  ....*....|....*....|....*...
gi 16198009    54 TEWTEHKAPDGRPYYYNQNTKQSSWEKP 81
Cdd:pfam00397   3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
56-82 7.84e-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: 57.15  E-value: 7.84e-11
                        10        20
                ....*....|....*....|....*..
gi 16198009  56 WTEHKAPDGRPYYYNQNTKQSSWEKPE 82
Cdd:cd00201   4 WEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
56-82 2.85e-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: 55.68  E-value: 2.85e-10
                           10        20
                   ....*....|....*....|....*..
gi 16198009     56 WTEHKAPDGRPYYYNQNTKQSSWEKPE 82
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPR 32
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
96-122 3.28e-09

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: 52.51  E-value: 3.28e-09
                          10        20
                  ....*....|....*....|....*..
gi 16198009    96 PWKEYRSDTGKVYYHNVATKETCWEPP 122
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
95-124 6.83e-09

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: 51.76  E-value: 6.83e-09
                        10        20        30
                ....*....|....*....|....*....|
gi 16198009  95 CPWKEYRSDTGKVYYHNVATKETCWEPPPE 124
Cdd:cd00201   2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
96-124 3.21e-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: 49.91  E-value: 3.21e-08
                           10        20
                   ....*....|....*....|....*....
gi 16198009     96 PWKEYRSDTGKVYYHNVATKETCWEPPPE 124
Cdd:smart00456   5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
445-500 2.91e-07

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: 47.45  E-value: 2.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16198009   445 KNRDSFLALLDSLheegKLTSMSLWVELYPIISADLRFSAMlgQSGSTPLDLFKFY 500
Cdd:pfam01846   1 KAREAFKELLKEH----KITPYSTWSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
230-281 3.42e-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: 3.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 16198009    230 REAIESFKELLRDRNVP-SNANWDQCVKIISKDPRYAAFKNLNERKQTFNAYK 281
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHI 53
 
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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