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Conserved domains on  [gi|25143393|ref|NP_740776|]
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E3 ubiquitin-protein ligase wwp-1 [Caenorhabditis elegans]

Protein Classification

synaptotagmin family protein; RIM/PCLO family C2 domain-containing protein( domain architecture ID 13102327)

synaptotagmin family protein is a membrane-trafficking protein characterized by an N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains; similar to synaptotagmins 4 and 11, which do not bind calcium| RIM (Rab-3-interacting molecule)/PCLO (protein piccolo) family C2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HUL4 super family cl34867
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
251-792 4.32e-178

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5021:

Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 533.58  E-value: 4.32e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 251 STQPLPQGWEMRRDPRGRVYYVDHNTRTTTWQRPTADMLEAHEQWQSG--RDQAMLQWEQRFLLQQNNFSADDPL----- 323
Cdd:COG5021 295 SLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVvnNDDSSSIKDLPHQVGSNPFLEAHPEfsell 374

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 324 -----------GPLPEGWEKRQDPnTSRMYFVNHVNRTTQWEDPRTQG--------------------GSDQPLPDGWEM 372
Cdd:COG5021 375 knqsrgttrdfRNKPTGWSSSIED-LGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqraSREGPLLSGWKT 453

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 373 RFTEQGVPFFIDHQSKTTTYNDPRTGKPVGPLGVVGVQMaMEkSFRWKIAQFRYLCLSNsVPNHVKITVSRNNVFEDSFQ 452
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRI-KE-DKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYR 530

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 453 EIMRKNAVDLRRRLYIQFRGEEGLDYGGVAREWFFLLSHEVLNPMYCLFMYAGNNNYSLQINPASFVNPDHLKYFEYIGR 532
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 533 FIAMALFHGKFIYSGFTMPFYKKMLNKKIVLKDIEQVDSEIYNSLMWIKDNNIDECDMELYFVADYELLGELKTYELKEG 612
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 613 GTEIAVTEENKLEYIELLVEWRFNRGVEQQTKAFFTGFNSVFPLEWMQYFDERELELLLCGMQD-VDVDDWQRNTVYRHY 691
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 692 APQSKQVTWFWQWVRSLDQEKRARLLQFVTGTCRVPVGGFSELMGSTGPQLFCIERVG-KENWLPRSHTCFNRLDLPPYR 770
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYS 850

                       570       580
                ....*....|....*....|..
gi 25143393 771 SYDQLVEKLSMAIEMTEGFGNE 792
Cdd:COG5021 851 SKEKLRSKLLTAINEGAGFGLL 872
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 29-147 1.95e-31

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


The actual alignment was detected with superfamily member cd04021:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 125  Bit Score: 118.92  E-value: 1.95e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393  29 PSKVTVKVVNASFTKA-----ADCYVEITSDTSSaaPKKTTVKKKTMAPEWNEHLNVHANESSTISFRLLQKAKLFDDTC 103
Cdd:cd04021   1 KSQLQITVESAKLKSNsksfkPDPYVEVTVDGQP--PKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKADVL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 25143393 104 LGMAKLKLSSLTRNENGEFKNDINNISLLAKD---SSKIGTLNIIFS 147
Cdd:cd04021  79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENkgsSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 221-250 2.10e-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: 58.67  E-value: 2.10e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 25143393   221 LPDGWEMRFDQYGRKYYVDHTTKSTTWERP 250
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
251-792 4.32e-178

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 533.58  E-value: 4.32e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 251 STQPLPQGWEMRRDPRGRVYYVDHNTRTTTWQRPTADMLEAHEQWQSG--RDQAMLQWEQRFLLQQNNFSADDPL----- 323
Cdd:COG5021 295 SLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVvnNDDSSSIKDLPHQVGSNPFLEAHPEfsell 374

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 324 -----------GPLPEGWEKRQDPnTSRMYFVNHVNRTTQWEDPRTQG--------------------GSDQPLPDGWEM 372
Cdd:COG5021 375 knqsrgttrdfRNKPTGWSSSIED-LGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqraSREGPLLSGWKT 453

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 373 RFTEQGVPFFIDHQSKTTTYNDPRTGKPVGPLGVVGVQMaMEkSFRWKIAQFRYLCLSNsVPNHVKITVSRNNVFEDSFQ 452
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRI-KE-DKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYR 530

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 453 EIMRKNAVDLRRRLYIQFRGEEGLDYGGVAREWFFLLSHEVLNPMYCLFMYAGNNNYSLQINPASFVNPDHLKYFEYIGR 532
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 533 FIAMALFHGKFIYSGFTMPFYKKMLNKKIVLKDIEQVDSEIYNSLMWIKDNNIDECDMELYFVADYELLGELKTYELKEG 612
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 613 GTEIAVTEENKLEYIELLVEWRFNRGVEQQTKAFFTGFNSVFPLEWMQYFDERELELLLCGMQD-VDVDDWQRNTVYRHY 691
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 692 APQSKQVTWFWQWVRSLDQEKRARLLQFVTGTCRVPVGGFSELMGSTGPQLFCIERVG-KENWLPRSHTCFNRLDLPPYR 770
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYS 850

                       570       580
                ....*....|....*....|..
gi 25143393 771 SYDQLVEKLSMAIEMTEGFGNE 792
Cdd:COG5021 851 SKEKLRSKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 438-790 4.60e-165

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 481.29  E-value: 4.60e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 438 KITVSRNNVFEDSFQEIMRKNAVDLRRRLYIQFRGEEGLDYGGVAREWFFLLSHEVLNPMYCLFMYAGNNNYSLQINPAS 517
Cdd:cd00078   2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 518 FVNPDHLKYFEYIGRFIAMALFHGKFIYSGFTMPFYKKMLNKKIVLKDIEQVDSEIYNSLMWIKDNNIDECDMELYFVAD 597
Cdd:cd00078  82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 598 Y-ELLGELKTYELKEGGTEIAVTEENKLEYIELLVEWRFNRGVEQQTKAFFTGFNSVFPLEWMQYFDERELELLLCGMQD 676
Cdd:cd00078 162 LdSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 677 VDVDDWQRNTVYRH-YAPQSKQVTWFWQWVRSLDQEKRARLLQFVTGTCRVPVGGFSELMgstgpQLFCIERVGK-ENWL 754
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 25143393 755 PRSHTCFNRLDLPPYRSYDQLVEKLSMAIEMTEGFG 790
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 461-789 8.50e-154

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 451.30  E-value: 8.50e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393    461 DLR-RRLYIQFRGEEGLDYGGVAREWFFLLSHEVLNPMYCLFMYAgNNNYSLQINPASFV-NPDHLKYFEYIGRFIAMAL 538
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393    539 FHGKFIYSGFTMPFYKKMLNKKIVLKDIEQVDSEIYNSLMWIKDNNIDECDMELYFVADY-ELLGELKTYELKEGGTEIA 617
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLtSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393    618 VTEENKLEYIELLVEWRFNRGVEQQTKAFFTGFNSVFPLEWMQYFDERELELLLCGMQDVDVDDWQRNTVYRH-YAPQSK 696
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393    697 QVTWFWQWVRSLDQEKRARLLQFVTGTCRVPVGGFSELMGStgpqlFCIERVG-KENWLPRSHTCFNRLDLPPYRSYDQL 775
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 25143393    776 VEKLSMAIEMTEGF 789
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 487-791 4.20e-122

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 368.86  E-value: 4.20e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393   487 FLLSHEVLNPMYCLFMYAGNNNYSLQINPASFVNPDH--LKYFEYIGRFIAMALFHGKFIYSGFTMPFYKKMLNKKIVLK 564
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393   565 DIEQVDSEIYNSLMWIKD-NNIDECDMELYFVADYelLGELKTYELKEGGTEIAVTEENKLEYIELLVEWRFNRGVEQQT 643
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393   644 KAFFTGFNSVFPLEWMQYFDERELELLLCGMQDVDVDDWQRNTVYRH-YAPQSKQVTWFWQWVRSLDQEKRARLLQFVTG 722
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143393   723 TCRVPVGGFSELmgstgpQLFCIERVG--KENWLPRSHTCFNRLDLPPYRSYDQLVEKLSMAIEMTEGFGN 791
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 29-147 1.95e-31

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 118.92  E-value: 1.95e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393  29 PSKVTVKVVNASFTKA-----ADCYVEITSDTSSaaPKKTTVKKKTMAPEWNEHLNVHANESSTISFRLLQKAKLFDDTC 103
Cdd:cd04021   1 KSQLQITVESAKLKSNsksfkPDPYVEVTVDGQP--PKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKADVL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 25143393 104 LGMAKLKLSSLTRNENGEFKNDINNISLLAKD---SSKIGTLNIIFS 147
Cdd:cd04021  79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENkgsSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 221-250 2.10e-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: 58.67  E-value: 2.10e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 25143393   221 LPDGWEMRFDQYGRKYYVDHTTKSTTWERP 250
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 221-250 2.62e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 55.68  E-value: 2.62e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 25143393    221 LPDGWEMRFDQYGRKYYVDHTTKSTTWERP 250
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 222-250 5.28e-10

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: 54.84  E-value: 5.28e-10
                        10        20
                ....*....|....*....|....*....
gi 25143393 222 PDGWEMRFDQYGRKYYVDHTTKSTTWERP 250
Cdd:cd00201   1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
 
Name Accession Description Interval E-value
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
251-792 4.32e-178

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 533.58  E-value: 4.32e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 251 STQPLPQGWEMRRDPRGRVYYVDHNTRTTTWQRPTADMLEAHEQWQSG--RDQAMLQWEQRFLLQQNNFSADDPL----- 323
Cdd:COG5021 295 SLLRLNSLFSTRADSFGRTYYLDHDRILTQYSRPLLEETLGESTSFLVvnNDDSSSIKDLPHQVGSNPFLEAHPEfsell 374

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 324 -----------GPLPEGWEKRQDPnTSRMYFVNHVNRTTQWEDPRTQG--------------------GSDQPLPDGWEM 372
Cdd:COG5021 375 knqsrgttrdfRNKPTGWSSSIED-LGQFLFSDFLTSSSTYEDLRREQlgresdesfyvasnvqqqraSREGPLLSGWKT 453

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 373 RFTEQGVPFFIDHQSKTTTYNDPRTGKPVGPLGVVGVQMaMEkSFRWKIAQFRYLCLSNsVPNHVKITVSRNNVFEDSFQ 452
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNDSRLGSFISLNKLDIRRI-KE-DKRRKLFYSLKQKAKI-FDPYLHIKVRRDRVFEDSYR 530

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 453 EIMRKNAVDLRRRLYIQFRGEEGLDYGGVAREWFFLLSHEVLNPMYCLFMYAGNNNYSLQINPASFVNPDHLKYFEYIGR 532
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 533 FIAMALFHGKFIYSGFTMPFYKKMLNKKIVLKDIEQVDSEIYNSLMWIKDNNIDECDMELYFVADYELLGELKTYELKEG 612
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 613 GTEIAVTEENKLEYIELLVEWRFNRGVEQQTKAFFTGFNSVFPLEWMQYFDERELELLLCGMQD-VDVDDWQRNTVYRHY 691
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 692 APQSKQVTWFWQWVRSLDQEKRARLLQFVTGTCRVPVGGFSELMGSTGPQLFCIERVG-KENWLPRSHTCFNRLDLPPYR 770
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGtDDDRLPSAHTCFNRLKLPEYS 850

                       570       580
                ....*....|....*....|..
gi 25143393 771 SYDQLVEKLSMAIEMTEGFGNE 792
Cdd:COG5021 851 SKEKLRSKLLTAINEGAGFGLL 872
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 438-790 4.60e-165

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 481.29  E-value: 4.60e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 438 KITVSRNNVFEDSFQEIMRKNAVDLRRRLYIQFRGEEGLDYGGVAREWFFLLSHEVLNPMYCLFMYAGNNNYSLQINPAS 517
Cdd:cd00078   2 KITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 518 FVNPDHLKYFEYIGRFIAMALFHGKFIYSGFTMPFYKKMLNKKIVLKDIEQVDSEIYNSLMWIKDNNIDECDMELYFVAD 597
Cdd:cd00078  82 FADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 598 Y-ELLGELKTYELKEGGTEIAVTEENKLEYIELLVEWRFNRGVEQQTKAFFTGFNSVFPLEWMQYFDERELELLLCGMQD 676
Cdd:cd00078 162 LdSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSED 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393 677 VDVDDWQRNTVYRH-YAPQSKQVTWFWQWVRSLDQEKRARLLQFVTGTCRVPVGGFSELMgstgpQLFCIERVGK-ENWL 754
Cdd:cd00078 242 IDLEDLKKNTEYKGgYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSpDDRL 316

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 25143393 755 PRSHTCFNRLDLPPYRSYDQLVEKLSMAIEMTEGFG 790
Cdd:cd00078 317 PTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 461-789 8.50e-154

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 451.30  E-value: 8.50e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393    461 DLR-RRLYIQFRGEEGLDYGGVAREWFFLLSHEVLNPMYCLFMYAgNNNYSLQINPASFV-NPDHLKYFEYIGRFIAMAL 538
Cdd:smart00119   1 DLKkRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYS-PNDYLLYPNPRSGFaNEEHLSYFRFIGRVLGKAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393    539 FHGKFIYSGFTMPFYKKMLNKKIVLKDIEQVDSEIYNSLMWIKDNNIDECDMELYFVADY-ELLGELKTYELKEGGTEIA 617
Cdd:smart00119  80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEELDLTFSIVLtSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393    618 VTEENKLEYIELLVEWRFNRGVEQQTKAFFTGFNSVFPLEWMQYFDERELELLLCGMQDVDVDDWQRNTVYRH-YAPQSK 696
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGgYSANSQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393    697 QVTWFWQWVRSLDQEKRARLLQFVTGTCRVPVGGFSELMGStgpqlFCIERVG-KENWLPRSHTCFNRLDLPPYRSYDQL 775
Cdd:smart00119 240 TIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGsDDERLPTAHTCFNRLKLPPYSSKEIL 314

                          330
                   ....*....|....
gi 25143393    776 VEKLSMAIEMTEGF 789
Cdd:smart00119 315 REKLLLAINEGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 487-791 4.20e-122

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 368.86  E-value: 4.20e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393   487 FLLSHEVLNPMYCLFMYAGNNNYSLQINPASFVNPDH--LKYFEYIGRFIAMALFHGKFIYSGFTMPFYKKMLNKKIVLK 564
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393   565 DIEQVDSEIYNSLMWIKD-NNIDECDMELYFVADYelLGELKTYELKEGGTEIAVTEENKLEYIELLVEWRFNRGVEQQT 643
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNmDNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393   644 KAFFTGFNSVFPLEWMQYFDERELELLLCGMQDVDVDDWQRNTVYRH-YAPQSKQVTWFWQWVRSLDQEKRARLLQFVTG 722
Cdd:pfam00632 159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143393   723 TCRVPVGGFSELmgstgpQLFCIERVG--KENWLPRSHTCFNRLDLPPYRSYDQLVEKLSMAIEMTEGFGN 791
Cdd:pfam00632 239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 29-147 1.95e-31

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 118.92  E-value: 1.95e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143393  29 PSKVTVKVVNASFTKA-----ADCYVEITSDTSSaaPKKTTVKKKTMAPEWNEHLNVHANESSTISFRLLQKAKLFDDTC 103
Cdd:cd04021   1 KSQLQITVESAKLKSNsksfkPDPYVEVTVDGQP--PKKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKADVL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 25143393 104 LGMAKLKLSSLTRNENGEFKNDINNISLLAKD---SSKIGTLNIIFS 147
Cdd:cd04021  79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENkgsSVKVGELTVILD 125
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 255-284 1.80e-12

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: 61.75  E-value: 1.80e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 25143393   255 LPQGWEMRRDPRGRVYYVDHNTRTTTWQRP 284
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 221-250 2.10e-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: 58.67  E-value: 2.10e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 25143393   221 LPDGWEMRFDQYGRKYYVDHTTKSTTWERP 250
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 254-285 2.49e-11

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: 58.77  E-value: 2.49e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 25143393    254 PLPQGWEMRRDPRGRVYYVDHNTRTTTWQRPT 285
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 256-285 4.73e-11

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 57.92  E-value: 4.73e-11
                        10        20        30
                ....*....|....*....|....*....|
gi 25143393 256 PQGWEMRRDPRGRVYYVDHNTRTTTWQRPT 285
Cdd:cd00201   1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 221-250 2.62e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 55.68  E-value: 2.62e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 25143393    221 LPDGWEMRFDQYGRKYYVDHTTKSTTWERP 250
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 222-250 5.28e-10

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: 54.84  E-value: 5.28e-10
                        10        20
                ....*....|....*....|....*....
gi 25143393 222 PDGWEMRFDQYGRKYYVDHTTKSTTWERP 250
Cdd:cd00201   1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 325-357 1.39e-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: 53.76  E-value: 1.39e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 25143393    325 PLPEGWEKRQDPNtSRMYFVNHVNRTTQWEDPR 357
Cdd:smart00456   1 PLPPGWEERKDPD-GRPYYYNHETKETQWEKPR 32
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 326-356 9.46e-09

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


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 51.35  E-value: 9.46e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 25143393   326 LPEGWEKRQDPNtSRMYFVNHVNRTTQWEDP 356
Cdd:pfam00397   1 LPPGWEERWDPD-GRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 327-357 1.28e-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: 50.99  E-value: 1.28e-08
                        10        20        30
                ....*....|....*....|....*....|.
gi 25143393 327 PEGWEKRQDPNtSRMYFVNHVNRTTQWEDPR 357
Cdd:cd00201   1 PPGWEERWDPD-GRVYYYNHNTKETQWEDPR 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 365-396 2.67e-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: 2.67e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 25143393    365 PLPDGWEMRFTEQGVPFFIDHQSKTTTYNDPR 396
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPR 32
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 367-396 6.06e-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: 49.06  E-value: 6.06e-08
                        10        20        30
                ....*....|....*....|....*....|
gi 25143393 367 PDGWEMRFTEQGVPFFIDHQSKTTTYNDPR 396
Cdd:cd00201   1 PPGWEERWDPDGRVYYYNHNTKETQWEDPR 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 366-395 7.36e-07

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: 45.96  E-value: 7.36e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 25143393   366 LPDGWEMRFTEQGVPFFIDHQSKTTTYNDP 395
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
PRP40 COG5104
Splicing factor [RNA processing and modification];
225-284 3.42e-06

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 50.46  E-value: 3.42e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143393 225 WEMRFDQYGRKYYVDHTTKSTTWERP------STQPLPQ-GWEMRRDPRGRVYYVDHNTRTTTWQRP 284
Cdd:COG5104  17 WEELKAPDGRIYYYNKRTGKSSWEKPkellkgSEEDLDVdPWKECRTADGKVYYYNSITRESRWKIP 83
 
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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