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Conserved domains on  [gi|1720400006|ref|XP_006498256|]
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pre-mRNA-processing factor 40 homolog A isoform X1 [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];
223-740 1.76e-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: 179.51  E-value: 1.76e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  223 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELedleamiKAE 302
Cdd:COG5104     17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER-------KKV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  303 ESSKQEECTTASTAPVptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgsvpvapepevtsivatavd 382
Cdd:COG5104     90 EPIAEQKHDERSMIGG---------------------------------------------------------------- 105
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  383 NENTVTVSTEEQAQLANTTAIQDLSGDISSNTgeepakqetvsDFTPKKeeeesqpakktytwnTKEEAKQAFKELLKEK 462
Cdd:COG5104    106 NGNDMAITDHETSEPKYLLGRLMSQYGITSTK-----------DAVYRL---------------TKEEAEKEFITMLKEN 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  463 RVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAE 542
Cdd:COG5104    160 QVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFK 239
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  543 QMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAED 621
Cdd:COG5104    240 SIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKN 318
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  622 EELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRF 701
Cdd:COG5104    319 KEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRF 398
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1720400006  702 TNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 740
Cdd:COG5104    399 LNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
803-857 3.13e-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: 53.73  E-value: 3.13e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1720400006   803 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 857
Cdd:smart00441    1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
223-740 1.76e-47

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 179.51  E-value: 1.76e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  223 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELedleamiKAE 302
Cdd:COG5104     17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER-------KKV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  303 ESSKQEECTTASTAPVptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgsvpvapepevtsivatavd 382
Cdd:COG5104     90 EPIAEQKHDERSMIGG---------------------------------------------------------------- 105
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  383 NENTVTVSTEEQAQLANTTAIQDLSGDISSNTgeepakqetvsDFTPKKeeeesqpakktytwnTKEEAKQAFKELLKEK 462
Cdd:COG5104    106 NGNDMAITDHETSEPKYLLGRLMSQYGITSTK-----------DAVYRL---------------TKEEAEKEFITMLKEN 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  463 RVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAE 542
Cdd:COG5104    160 QVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFK 239
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  543 QMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAED 621
Cdd:COG5104    240 SIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKN 318
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  622 EELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRF 701
Cdd:COG5104    319 KEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRF 398
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1720400006  702 TNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 740
Cdd:COG5104    399 LNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
450-499 2.47e-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: 70.95  E-value: 2.47e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720400006  450 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 499
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 2.74e-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: 2.74e-11
                           10        20
                   ....*....|....*....|....*...
gi 1720400006  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 1.20e-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: 1.20e-10
                            10        20
                    ....*....|....*....|....*...
gi 1720400006   223 WTEHKSPDGRTYYYNTETKQSTWEKPDD 250
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
803-857 3.13e-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: 53.73  E-value: 3.13e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1720400006   803 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 857
Cdd:smart00441    1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
804-855 7.77e-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: 43.98  E-value: 7.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720400006  804 RKESAFKSMLKQatPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 855
Cdd:pfam01846    1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
223-740 1.76e-47

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 179.51  E-value: 1.76e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  223 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELedleamiKAE 302
Cdd:COG5104     17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER-------KKV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  303 ESSKQEECTTASTAPVptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgsvpvapepevtsivatavd 382
Cdd:COG5104     90 EPIAEQKHDERSMIGG---------------------------------------------------------------- 105
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  383 NENTVTVSTEEQAQLANTTAIQDLSGDISSNTgeepakqetvsDFTPKKeeeesqpakktytwnTKEEAKQAFKELLKEK 462
Cdd:COG5104    106 NGNDMAITDHETSEPKYLLGRLMSQYGITSTK-----------DAVYRL---------------TKEEAEKEFITMLKEN 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  463 RVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAE 542
Cdd:COG5104    160 QVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFK 239
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  543 QMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSEAQQYLMDNPTFAED 621
Cdd:COG5104    240 SIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLLNHYVFDSVVRYLKN 318
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006  622 EELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRF 701
Cdd:COG5104    319 KEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMKWKNAYPLIKDDPRF 398
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1720400006  702 TNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 740
Cdd:COG5104    399 LNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
450-499 2.47e-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: 70.95  E-value: 2.47e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720400006  450 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 499
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 2.74e-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: 2.74e-11
                           10        20
                   ....*....|....*....|....*...
gi 1720400006  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 5.28e-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: 5.28e-11
                           10        20
                   ....*....|....*....|....*.
gi 1720400006  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 1.20e-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: 1.20e-10
                            10        20
                    ....*....|....*....|....*...
gi 1720400006   223 WTEHKSPDGRTYYYNTETKQSTWEKPDD 250
Cdd:smart00456    6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
449-502 2.23e-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: 56.81  E-value: 2.23e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1720400006   449 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 502
Cdd:smart00441    1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
803-857 3.13e-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: 53.73  E-value: 3.13e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1720400006   803 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 857
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 2.13e-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: 2.13e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1720400006  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 3.10e-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: 3.10e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1720400006   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 8.47e-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: 8.47e-08
                           10        20
                   ....*....|....*....|....*..
gi 1720400006  263 PWKEYKSDSGKPYYYNSQTKESRWAKP 289
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
583-642 6.16e-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: 47.18  E-value: 6.16e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400006   583 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 642
Cdd:smart00441    1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
804-855 7.77e-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: 43.98  E-value: 7.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720400006  804 RKESAFKSMLKQatPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 855
Cdd:pfam01846    1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
667-723 4.84e-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: 35.90  E-value: 4.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720400006  667 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMLgqpvfsLGSTALDLFKFY 723
Cdd:pfam01846    4 EAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKALL------DGSEREELFEDY 50
 
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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