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Conserved domains on  [gi|398364759|ref|NP_012913|]
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Prp40p [Saccharomyces cerevisiae S288C]

Protein Classification

PRP40 family protein( domain architecture ID 11473808)

PRP40 family protein similar to Saccharomyces cerevisiae pre-mRNA-processing protein PRP40 required for pre-spliceosome formation, which is the first step of pre-mRNA splicing

Gene Ontology:  GO:0000398|GO:0003723

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
1-583 0e+00

Splicing factor [RNA processing and modification];


:

Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 846.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759   1 MSIWKEAKDASGRIYYYNTLTKKSTWEKPKELISQEELLLRENGWKAAKTADGKVYYYNPTTRETSWTIPAFEKKVEPIA 80
Cdd:COG5104   14 RSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759  81 EQKHDTVSHAQVNGNRIALTAGEKQEPGRTINEEESQYANNSKLLNVRRRTKEEAEKEFITMLKENQVDSTWSFSRIISE 160
Cdd:COG5104   94 EQKHDERSMIGGNGNDMAITDHETSEPKYLLGRLMSQYGITSTKDAVYRLTKEEAEKEFITMLKENQVDSTWPIFRAIEE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 161 LgtRDPRYWMVDDDPLWKKEMFEKYLSNRSADQLLKEHNETSKFKEAFQKMLQNNSHIKYYTRWPTAKRLIADEPIYKhS 240
Cdd:COG5104  174 L--RDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYS-S 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 241 VVNEKTKRQTFQDYIDTLIDTQKESKKKLKTQALKELREYLNGIIttssSETFITWQqlLNHYVFDKSKRYMANRHFKVL 320
Cdd:COG5104  251 VVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLG----SETFIIWL--LNHYVFDSVVRYLKNKEMKPL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 321 THEDVLNEYLKIVNTIENDLQNKLNELRLRNYTRDRIARDNFKSLLREVPIKIKANTR--WSDIYPHIKSDPRFLHMLGR 398
Cdd:COG5104  325 DRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRmkWKNAYPLIKDDPRFLNLLGR 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 399 NGSSCLDLFLDF-VDEQRMYIFAQRSIAQQTLIDQNFEWNDADSDEITKQNIEKVLENDRKFDKVDKEDISLIVDGLIKQ 477
Cdd:COG5104  405 TGSSPLDLFFDFiVDLENMYGFARRSYERETRTGQISPTDRRAVDEIFEAIAEKKEEGEIKFDKVDKEDISLIVDGLIKQ 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 478 RNEKIQQKLQNERRILEQKKHYFWLLLQRTYTKTGKPKPSTWDLASKELGESLEYKALGDEDNIRRQIFEDFKPESSAPT 557
Cdd:COG5104  485 RNEKIQQKLQNERRILEQKKHYFWLLLQRTYTKTGKPKPSTWDLASKELGESLEYKALGDEDNIRRQIFEDFKPESSAPT 564
                        570       580
                 ....*....|....*....|....*.
gi 398364759 558 AESATANLTLTASKKRHLTPAVELDY 583
Cdd:COG5104  565 AESATANLTLTASKKRHLTPAVELDY 590
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
1-583 0e+00

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 846.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759   1 MSIWKEAKDASGRIYYYNTLTKKSTWEKPKELISQEELLLRENGWKAAKTADGKVYYYNPTTRETSWTIPAFEKKVEPIA 80
Cdd:COG5104   14 RSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759  81 EQKHDTVSHAQVNGNRIALTAGEKQEPGRTINEEESQYANNSKLLNVRRRTKEEAEKEFITMLKENQVDSTWSFSRIISE 160
Cdd:COG5104   94 EQKHDERSMIGGNGNDMAITDHETSEPKYLLGRLMSQYGITSTKDAVYRLTKEEAEKEFITMLKENQVDSTWPIFRAIEE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 161 LgtRDPRYWMVDDDPLWKKEMFEKYLSNRSADQLLKEHNETSKFKEAFQKMLQNNSHIKYYTRWPTAKRLIADEPIYKhS 240
Cdd:COG5104  174 L--RDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYS-S 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 241 VVNEKTKRQTFQDYIDTLIDTQKESKKKLKTQALKELREYLNGIIttssSETFITWQqlLNHYVFDKSKRYMANRHFKVL 320
Cdd:COG5104  251 VVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLG----SETFIIWL--LNHYVFDSVVRYLKNKEMKPL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 321 THEDVLNEYLKIVNTIENDLQNKLNELRLRNYTRDRIARDNFKSLLREVPIKIKANTR--WSDIYPHIKSDPRFLHMLGR 398
Cdd:COG5104  325 DRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRmkWKNAYPLIKDDPRFLNLLGR 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 399 NGSSCLDLFLDF-VDEQRMYIFAQRSIAQQTLIDQNFEWNDADSDEITKQNIEKVLENDRKFDKVDKEDISLIVDGLIKQ 477
Cdd:COG5104  405 TGSSPLDLFFDFiVDLENMYGFARRSYERETRTGQISPTDRRAVDEIFEAIAEKKEEGEIKFDKVDKEDISLIVDGLIKQ 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 478 RNEKIQQKLQNERRILEQKKHYFWLLLQRTYTKTGKPKPSTWDLASKELGESLEYKALGDEDNIRRQIFEDFKPESSAPT 557
Cdd:COG5104  485 RNEKIQQKLQNERRILEQKKHYFWLLLQRTYTKTGKPKPSTWDLASKELGESLEYKALGDEDNIRRQIFEDFKPESSAPT 564
                        570       580
                 ....*....|....*....|....*.
gi 398364759 558 AESATANLTLTASKKRHLTPAVELDY 583
Cdd:COG5104  565 AESATANLTLTASKKRHLTPAVELDY 590
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
4-29 9.32e-10

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 425661 [Multi-domain]  Cd Length: 30  Bit Score: 53.66  E-value: 9.32e-10
                          10        20
                  ....*....|....*....|....*.
gi 398364759    4 WKEAKDASGRIYYYNTLTKKSTWEKP 29
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
4-31 2.47e-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: 52.53  E-value: 2.47e-09
                         10        20
                 ....*....|....*....|....*...
gi 398364759   4 WKEAKDASGRIYYYNTLTKKSTWEKPKE 31
Cdd:cd00201    4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
4-31 4.54e-09

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: 51.83  E-value: 4.54e-09
                           10        20
                   ....*....|....*....|....*...
gi 398364759     4 WKEAKDASGRIYYYNTLTKKSTWEKPKE 31
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
1-583 0e+00

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 846.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759   1 MSIWKEAKDASGRIYYYNTLTKKSTWEKPKELISQEELLLRENGWKAAKTADGKVYYYNPTTRETSWTIPAFEKKVEPIA 80
Cdd:COG5104   14 RSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759  81 EQKHDTVSHAQVNGNRIALTAGEKQEPGRTINEEESQYANNSKLLNVRRRTKEEAEKEFITMLKENQVDSTWSFSRIISE 160
Cdd:COG5104   94 EQKHDERSMIGGNGNDMAITDHETSEPKYLLGRLMSQYGITSTKDAVYRLTKEEAEKEFITMLKENQVDSTWPIFRAIEE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 161 LgtRDPRYWMVDDDPLWKKEMFEKYLSNRSADQLLKEHNETSKFKEAFQKMLQNNSHIKYYTRWPTAKRLIADEPIYKhS 240
Cdd:COG5104  174 L--RDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYS-S 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 241 VVNEKTKRQTFQDYIDTLIDTQKESKKKLKTQALKELREYLNGIIttssSETFITWQqlLNHYVFDKSKRYMANRHFKVL 320
Cdd:COG5104  251 VVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLG----SETFIIWL--LNHYVFDSVVRYLKNKEMKPL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 321 THEDVLNEYLKIVNTIENDLQNKLNELRLRNYTRDRIARDNFKSLLREVPIKIKANTR--WSDIYPHIKSDPRFLHMLGR 398
Cdd:COG5104  325 DRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRmkWKNAYPLIKDDPRFLNLLGR 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 399 NGSSCLDLFLDF-VDEQRMYIFAQRSIAQQTLIDQNFEWNDADSDEITKQNIEKVLENDRKFDKVDKEDISLIVDGLIKQ 477
Cdd:COG5104  405 TGSSPLDLFFDFiVDLENMYGFARRSYERETRTGQISPTDRRAVDEIFEAIAEKKEEGEIKFDKVDKEDISLIVDGLIKQ 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759 478 RNEKIQQKLQNERRILEQKKHYFWLLLQRTYTKTGKPKPSTWDLASKELGESLEYKALGDEDNIRRQIFEDFKPESSAPT 557
Cdd:COG5104  485 RNEKIQQKLQNERRILEQKKHYFWLLLQRTYTKTGKPKPSTWDLASKELGESLEYKALGDEDNIRRQIFEDFKPESSAPT 564
                        570       580
                 ....*....|....*....|....*.
gi 398364759 558 AESATANLTLTASKKRHLTPAVELDY 583
Cdd:COG5104  565 AESATANLTLTASKKRHLTPAVELDY 590
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
4-29 9.32e-10

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 425661 [Multi-domain]  Cd Length: 30  Bit Score: 53.66  E-value: 9.32e-10
                          10        20
                  ....*....|....*....|....*.
gi 398364759    4 WKEAKDASGRIYYYNTLTKKSTWEKP 29
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
134-185 2.00e-09

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: 53.23  E-value: 2.00e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398364759  134 EAEKEFITMLKENQVDSTWSFSRIISELGTrDPRYWMVdDDPLWKKEMFEKY 185
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIEN-DPRYKAL-LDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
4-31 2.47e-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: 52.53  E-value: 2.47e-09
                         10        20
                 ....*....|....*....|....*...
gi 398364759   4 WKEAKDASGRIYYYNTLTKKSTWEKPKE 31
Cdd:cd00201    4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
4-31 4.54e-09

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: 51.83  E-value: 4.54e-09
                           10        20
                   ....*....|....*....|....*...
gi 398364759     4 WKEAKDASGRIYYYNTLTKKSTWEKPKE 31
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
44-70 5.16e-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: 425661 [Multi-domain]  Cd Length: 30  Bit Score: 51.74  E-value: 5.16e-09
                          10        20
                  ....*....|....*....|....*..
gi 398364759   44 GWKAAKTADGKVYYYNPTTRETSWTIP 70
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
203-256 8.36e-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: 51.81  E-value: 8.36e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 398364759   203 KFKEAFQKMLQNNSHIKYYTRWPTAKRLIADEPIYKHsVVNEKTKRQTFQDYID 256
Cdd:smart00441   2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKA-LLSESEREQLFEDHIE 54
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
44-70 2.44e-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: 49.83  E-value: 2.44e-08
                         10        20
                 ....*....|....*....|....*..
gi 398364759  44 GWKAAKTADGKVYYYNPTTRETSWTIP 70
Cdd:cd00201    3 GWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
44-71 4.75e-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: 49.14  E-value: 4.75e-08
                           10        20
                   ....*....|....*....|....*...
gi 398364759    44 GWKAAKTADGKVYYYNPTTRETSWTIPA 71
Cdd:smart00456   5 GWEERKDPDGRPYYYNHETKETQWEKPR 32
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
358-410 2.33e-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: 2.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 398364759  358 ARDNFKSLLREvpIKIKANTRWSDIYPHIKSDPRFLHMlgRNGSSCLDLFLDF 410
Cdd:pfam01846   2 AREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
203-254 1.94e-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: 44.76  E-value: 1.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398364759  203 KFKEAFQKMLQNNsHIKYYTRWPTAKRLIADEPIYKhSVVNEKTKRQTFQDY 254
Cdd:pfam01846   1 KAREAFKELLKEH-KITPYSTWSEIKKKIENDPRYK-ALLDGSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
356-413 8.57e-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: 43.33  E-value: 8.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 398364759   356 RIARDNFKSLLREVPiKIKANTRWSDIYPHIKSDPRFLHMLGRngSSCLDLFLDFVDE 413
Cdd:smart00441   1 EEAKEAFKELLKEHE-VITPDTTWSEARKKLKNDPRYKALLSE--SEREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
494-552 1.67e-04

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: 39.48  E-value: 1.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 398364759   494 EQKKHYFWLLLQRTYTKTgkpKPSTWDLASKELGESLEYKALGDEDnIRRQIFEDFKPE 552
Cdd:smart00441   1 EEAKEAFKELLKEHEVIT---PDTTWSEARKKLKNDPRYKALLSES-EREQLFEDHIEE 55
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
133-188 6.70e-03

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: 34.86  E-value: 6.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364759   133 EEAEKEFITMLKENQV---DSTWSFSRIISELgtrDPRY-WMVDDDPlwKKEMFEKYLSN 188
Cdd:smart00441   1 EEAKEAFKELLKEHEVitpDTTWSEARKKLKN---DPRYkALLSESE--REQLFEDHIEE 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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