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Conserved domains on  [gi|1690553887|ref|NP_001357944|]
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pre-mRNA-processing factor 40 homolog A isoform 1 [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];
161-696 4.28e-44

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: 169.49  E-value: 4.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 161 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELedlegyqnti 240
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER---------- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 241 vagglitksnlhamiKAEESSKQEECTTASTAPVptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgs 320
Cdd:COG5104    87 ---------------KKVEPIAEQKHDERSMIGG---------------------------------------------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 321 vpvapepevtsivatavdNENTVTVSTEEQAQLANTTAIQDLSGDISSNTgeepakqetvsDFTPKKeeeesqpakktyt 400
Cdd:COG5104   106 ------------------NGNDMAITDHETSEPKYLLGRLMSQYGITSTK-----------DAVYRL------------- 143
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 401 wnTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQR 480
Cdd:COG5104   144 --TKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCK 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 481 FLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsT 559
Cdd:COG5104   222 MLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-I 300
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 560 TWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLH 639
Cdd:COG5104   301 IWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIY 380
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1690553887 640 SMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 696
Cdd:COG5104   381 YRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
759-813 8.54e-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: 52.19  E-value: 8.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1690553887  759 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 813
Cdd:smart00441   1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
161-696 4.28e-44

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 169.49  E-value: 4.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 161 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELedlegyqnti 240
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER---------- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 241 vagglitksnlhamiKAEESSKQEECTTASTAPVptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgs 320
Cdd:COG5104    87 ---------------KKVEPIAEQKHDERSMIGG---------------------------------------------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 321 vpvapepevtsivatavdNENTVTVSTEEQAQLANTTAIQDLSGDISSNTgeepakqetvsDFTPKKeeeesqpakktyt 400
Cdd:COG5104   106 ------------------NGNDMAITDHETSEPKYLLGRLMSQYGITSTK-----------DAVYRL------------- 143
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 401 wnTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQR 480
Cdd:COG5104   144 --TKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCK 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 481 FLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsT 559
Cdd:COG5104   222 MLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-I 300
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 560 TWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLH 639
Cdd:COG5104   301 IWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIY 380
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1690553887 640 SMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 696
Cdd:COG5104   381 YRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
406-455 5.46e-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: 69.79  E-value: 5.46e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1690553887 406 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 455
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
161-188 3.28e-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: 3.28e-11
                          10        20
                  ....*....|....*....|....*...
gi 1690553887 161 WTEHKSPDGRTYYYNTETKQSTWEKPDD 188
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
161-188 1.10e-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: 1.10e-10
                           10        20
                   ....*....|....*....|....*...
gi 1690553887  161 WTEHKSPDGRTYYYNTETKQSTWEKPDD 188
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
759-813 8.54e-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: 52.19  E-value: 8.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1690553887  759 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 813
Cdd:smart00441   1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
760-811 1.34e-05

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: 43.21  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1690553887 760 RKESAFKSMLKQatPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 811
Cdd:pfam01846   1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
161-696 4.28e-44

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 169.49  E-value: 4.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 161 WTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELedlegyqnti 240
Cdd:COG5104    17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER---------- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 241 vagglitksnlhamiKAEESSKQEECTTASTAPVptteipttmstmaaaeaaaavvaaaaaaaaaanantsttptntvgs 320
Cdd:COG5104    87 ---------------KKVEPIAEQKHDERSMIGG---------------------------------------------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 321 vpvapepevtsivatavdNENTVTVSTEEQAQLANTTAIQDLSGDISSNTgeepakqetvsDFTPKKeeeesqpakktyt 400
Cdd:COG5104   106 ------------------NGNDMAITDHETSEPKYLLGRLMSQYGITSTK-----------DAVYRL------------- 143
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 401 wnTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQR 480
Cdd:COG5104   144 --TKEEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCK 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 481 FLENHEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsT 559
Cdd:COG5104   222 MLAGNSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-I 300
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887 560 TWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLH 639
Cdd:COG5104   301 IWLLNHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIY 380
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1690553887 640 SMSSWMELYPTISSDIRFTNMLGQPvfslGSTALDLFKFYVEDLKARYHDEKKIIKD 696
Cdd:COG5104   381 YRMKWKNAYPLIKDDPRFLNLLGRT----GSSPLDLFFDFIVDLENMYGFARRSYER 433
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
406-455 5.46e-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: 69.79  E-value: 5.46e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1690553887 406 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 455
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
161-188 3.28e-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: 3.28e-11
                          10        20
                  ....*....|....*....|....*...
gi 1690553887 161 WTEHKSPDGRTYYYNTETKQSTWEKPDD 188
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
161-186 5.62e-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: 5.62e-11
                          10        20
                  ....*....|....*....|....*.
gi 1690553887 161 WTEHKSPDGRTYYYNTETKQSTWEKP 186
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
161-188 1.10e-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: 1.10e-10
                           10        20
                   ....*....|....*....|....*...
gi 1690553887  161 WTEHKSPDGRTYYYNTETKQSTWEKPDD 188
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
405-458 6.32e-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: 55.66  E-value: 6.32e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1690553887  405 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 458
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
759-813 8.54e-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: 52.19  E-value: 8.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1690553887  759 KRKESAFKSMLKQaTPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 813
Cdd:smart00441   1 EEAKEAFKELLKE-HEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
199-229 2.43e-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: 2.43e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1690553887 199 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 229
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
198-229 2.85e-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: 2.85e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1690553887  198 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 229
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
201-227 9.03e-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: 9.03e-08
                          10        20
                  ....*....|....*....|....*..
gi 1690553887 201 PWKEYKSDSGKPYYYNSQTKESRWAKP 227
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
539-598 1.40e-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: 46.03  E-value: 1.40e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553887  539 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 598
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
760-811 1.34e-05

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: 43.21  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1690553887 760 RKESAFKSMLKQatPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 811
Cdd:pfam01846   1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
623-679 8.04e-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: 35.51  E-value: 8.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1690553887 623 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMLgqpvfsLGSTALDLFKFY 679
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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