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Conserved domains on  [gi|1958760388|ref|XP_038960404|]
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pre-mRNA-processing factor 40 homolog A isoform X6 [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];
181-694 7.09e-49

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: 183.74  E-value: 7.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 181 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEamikae 260
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVE------ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 261 esskqeectttstapvptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgsvPVAPEPEVTSIVATAVD 340
Cdd:COG5104    91 ---------------------------------------------------------------PIAEQKHDERSMIGGNG 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 341 NENTVTASAEEQaqlanttalqdlsgdissntgeeppkqetvtdftPKKE--EEESQPAKKTYTWN----TKEEAKQAFK 414
Cdd:COG5104   108 NDMAITDHETSE----------------------------------PKYLlgRLMSQYGITSTKDAvyrlTKEEAEKEFI 153

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 415 ELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTT 494
Cdd:COG5104   154 TMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYT 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 495 RYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSEAQQYLMDN 573
Cdd:COG5104   234 DWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSV 312

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 574 PTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTI 653
Cdd:COG5104   313 VRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLI 392

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1958760388 654 SSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD 694
Cdd:COG5104   393 KDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYER 433
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 757-811 5.28e-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: 52.96  E-value: 5.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958760388  757 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 811
Cdd:smart00441   1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
181-694 7.09e-49

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 183.74  E-value: 7.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 181 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEamikae 260
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVE------ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 261 esskqeectttstapvptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgsvPVAPEPEVTSIVATAVD 340
Cdd:COG5104    91 ---------------------------------------------------------------PIAEQKHDERSMIGGNG 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 341 NENTVTASAEEQaqlanttalqdlsgdissntgeeppkqetvtdftPKKE--EEESQPAKKTYTWN----TKEEAKQAFK 414
Cdd:COG5104   108 NDMAITDHETSE----------------------------------PKYLlgRLMSQYGITSTKDAvyrlTKEEAEKEFI 153

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 415 ELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTT 494
Cdd:COG5104   154 TMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYT 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 495 RYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSEAQQYLMDN 573
Cdd:COG5104   234 DWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSV 312

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 574 PTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTI 653
Cdd:COG5104   313 VRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLI 392

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1958760388 654 SSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD 694
Cdd:COG5104   393 KDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYER 433
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 408-457 3.25e-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: 70.56  E-value: 3.25e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958760388 408 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 457
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 181-208 3.61e-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: 58.31  E-value: 3.61e-11
                          10        20
                  ....*....|....*....|....*...
gi 1958760388 181 WTEHKSPDGRTYYYNTETKQSTWEKPDD 208
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 181-208 1.45e-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: 56.84  E-value: 1.45e-10
                           10        20
                   ....*....|....*....|....*...
gi 1958760388  181 WTEHKSPDGRTYYYNTETKQSTWEKPDD 208
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 757-811 5.28e-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: 52.96  E-value: 5.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958760388  757 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 811
Cdd:smart00441   1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 758-809 9.39e-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: 43.60  E-value: 9.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958760388 758 RKESAFKSMLKQatPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 809
Cdd:pfam01846   1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
 262-400 7.25e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 39.12  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 262 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAaananTSTTPTNTVGSVPVAPE------PEVTSIV 335
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNAS-----TINVTTKVTAQNITATEagtgtsTGVTSNV 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958760388 336 ATavdnENTVTASAEEQAQLAnTTALQDLSGDISSNTGEEPPKQETVTDftpkkeeeESQPAKKT 400
Cdd:PHA03255  129 TT----RSSSTTSATTRITNA-TTLAPTLSSKGTSNATKTTAELPTVPD--------ERQPSLSY 180
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
181-694 7.09e-49

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 183.74  E-value: 7.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 181 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEamikae 260
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVE------ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 261 esskqeectttstapvptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgsvPVAPEPEVTSIVATAVD 340
Cdd:COG5104    91 ---------------------------------------------------------------PIAEQKHDERSMIGGNG 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 341 NENTVTASAEEQaqlanttalqdlsgdissntgeeppkqetvtdftPKKE--EEESQPAKKTYTWN----TKEEAKQAFK 414
Cdd:COG5104   108 NDMAITDHETSE----------------------------------PKYLlgRLMSQYGITSTKDAvyrlTKEEAEKEFI 153

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 415 ELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTT 494
Cdd:COG5104   154 TMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYT 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 495 RYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSEAQQYLMDN 573
Cdd:COG5104   234 DWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSV 312

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 574 PTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTI 653
Cdd:COG5104   313 VRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLI 392

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1958760388 654 SSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD 694
Cdd:COG5104   393 KDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYER 433
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 408-457 3.25e-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: 70.56  E-value: 3.25e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958760388 408 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 457
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 181-208 3.61e-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: 58.31  E-value: 3.61e-11
                          10        20
                  ....*....|....*....|....*...
gi 1958760388 181 WTEHKSPDGRTYYYNTETKQSTWEKPDD 208
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 181-206 6.43e-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: 57.51  E-value: 6.43e-11
                          10        20
                  ....*....|....*....|....*.
gi 1958760388 181 WTEHKSPDGRTYYYNTETKQSTWEKP 206
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 181-208 1.45e-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: 56.84  E-value: 1.45e-10
                           10        20
                   ....*....|....*....|....*...
gi 1958760388  181 WTEHKSPDGRTYYYNTETKQSTWEKPDD 208
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 407-460 3.87e-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: 56.04  E-value: 3.87e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958760388  407 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 460
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 757-811 5.28e-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: 52.96  E-value: 5.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958760388  757 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 811
Cdd:smart00441   1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 219-249 2.70e-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: 50.22  E-value: 2.70e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958760388 219 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 249
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 218-249 3.50e-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: 3.50e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958760388  218 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 249
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 221-247 9.94e-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: 9.94e-08
                          10        20
                  ....*....|....*....|....*..
gi 1958760388 221 PWKEYKSDSGKPYYYNSQTKESRWAKP 247
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 541-600 9.31e-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: 46.41  E-value: 9.31e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388  541 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 600
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 758-809 9.39e-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: 43.60  E-value: 9.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958760388 758 RKESAFKSMLKQatPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 809
Cdd:pfam01846   1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 625-677 3.26e-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: 39.36  E-value: 3.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958760388 625 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMlgQPGSTALDLFKFY 677
Cdd:pfam01846   4 EAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
 262-400 7.25e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 39.12  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760388 262 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAaananTSTTPTNTVGSVPVAPE------PEVTSIV 335
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNAS-----TINVTTKVTAQNITATEagtgtsTGVTSNV 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958760388 336 ATavdnENTVTASAEEQAQLAnTTALQDLSGDISSNTGEEPPKQETVTDftpkkeeeESQPAKKT 400
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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