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Conserved domains on  [gi|320541912|ref|NP_001188572|]
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hecw ubiquitin protein ligase, isoform E [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1065-1421 5.34e-155

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: 472.43  E-value: 5.34e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1065 LKLHIRRSHLLEDAFRRIMSANKKDLqRGRLAVLWDTEEGLDYGGPSREFFFLLSRELFNPYYGLFEYSANDTYTVQVSP 1144
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1145 LSAFVDNCHDWFRFSGRVLGLALVHQYLLDAFFTRPFYKALLRLPVALSDLESLDNEFHQSLQWIRDNDIGTGvDLGLTF 1224
Cdd:cd00078    80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDED-DLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1225 CV-TEELLGSVVDRELKPGGKNIIINEKNKKEYLERMIKWRLERGVQEQTESLVRGFYEVIDSRLVSVFDARELELVIAG 1303
Cdd:cd00078   159 TIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1304 TAEIDTNDWRLNTEYRSGYHDNHQVIVWFWQVIERFSNEQRLRLLQFVTGTSSIPYEGFSALRgstgpRRFCIEKWGKPN 1383
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPD 313
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 320541912 1384 A-LPRAHTCFNRLDLPPYPTPELLYEKLLLAVEETNTFG 1421
Cdd:cd00078   314 DrLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECW1_helix super family cl39772
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ...
735-791 1.31e-17

Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.


The actual alignment was detected with superfamily member pfam18436:

Pssm-ID: 465766  Cd Length: 67  Bit Score: 78.30  E-value: 1.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 320541912   735 LCRPDFYSLLHTNEAALAIYNRNAALKHMVMRIRRDPPCFQRYQYNKDLVALVNTFA 791
Cdd:pfam18436   11 ITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
635-664 2.92e-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: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 56.36  E-value: 2.92e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 320541912   635 LPPAWEARMDSHGRIFYIDHTTRTTSWQRP 664
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
PHA03247 super family cl33720
large tegument protein UL36; Provisional
408-559 1.03e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  408 PYLRQHRPLTRALSNGKASSSEEQASPRLllSPKRPRSPPSGCSTRSASPLDISLSPEQHSPTRGRGVGGALQDAVPPGT 487
Cdd:PHA03247 2875 PAAPARPPVRRLARPAVSRSTESFALPPD--QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541912  488 PTFHGQRPQQRLLKRVGGGAGAGATGGATGSPLVCPPTPTHHARRHARLQAVTA-NSSLASggAIPSDPPAVS 559
Cdd:PHA03247 2953 GEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwASSLAL--HEETDPPPVS 3023
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1065-1421 5.34e-155

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: 472.43  E-value: 5.34e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1065 LKLHIRRSHLLEDAFRRIMSANKKDLqRGRLAVLWDTEEGLDYGGPSREFFFLLSRELFNPYYGLFEYSANDTYTVQVSP 1144
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1145 LSAFVDNCHDWFRFSGRVLGLALVHQYLLDAFFTRPFYKALLRLPVALSDLESLDNEFHQSLQWIRDNDIGTGvDLGLTF 1224
Cdd:cd00078    80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDED-DLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1225 CV-TEELLGSVVDRELKPGGKNIIINEKNKKEYLERMIKWRLERGVQEQTESLVRGFYEVIDSRLVSVFDARELELVIAG 1303
Cdd:cd00078   159 TIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1304 TAEIDTNDWRLNTEYRSGYHDNHQVIVWFWQVIERFSNEQRLRLLQFVTGTSSIPYEGFSALRgstgpRRFCIEKWGKPN 1383
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPD 313
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 320541912 1384 A-LPRAHTCFNRLDLPPYPTPELLYEKLLLAVEETNTFG 1421
Cdd:cd00078   314 DrLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1089-1420 1.86e-145

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: 445.91  E-value: 1.86e-145
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912   1089 DLQRGRLAVLWDTEEGLDYGGPSREFFFLLSRELFNPYYGLFEYSANDtYTVQVSPLSAFVDNCH-DWFRFSGRVLGLAL 1167
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHlSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912   1168 VHQYLLDAFFTRPFYKALLRLPVALSDLESLDNEFHQSLQWIR-DNDIGTGVDLGLTFCVTEELlGSVVDRELKPGGKNI 1246
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLlNNDTSEELDLTFSIVLTSEF-GQVKVVELKPGGSNI 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912   1247 IINEKNKKEYLERMIKWRLERGVQEQTESLVRGFYEVIDSRLVSVFDARELELVIAGTAEIDTNDWRLNTEYRSGYHDNH 1326
Cdd:smart00119  159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANS 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912   1327 QVIVWFWQVIERFSNEQRLRLLQFVTGTSSIPYEGFSALRGStgprrFCIEKWGKP-NALPRAHTCFNRLDLPPYPTPEL 1405
Cdd:smart00119  239 QTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEI 313
                           330
                    ....*....|....*
gi 320541912   1406 LYEKLLLAVEETNTF 1420
Cdd:smart00119  314 LREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1039-1423 2.91e-129

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 422.25  E-value: 2.91e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1039 RRDFEAKLRSFYRKLeSKGYGQGPHKLKLHIRRSHLLEDAFRRIMSANKKDLqRGRLAVLWDTEEGLDYGGPSREFFFLL 1118
Cdd:COG5021   490 RRIKEDKRRKLFYSL-KQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDL-KKTLEIEFVGEEGIDAGGLTREWLFLL 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1119 SRELFNPYYGLFEYSANDTYTVQVSPLSAfVDNCH-DWFRFSGRVLGLALVHQYLLDAFFTRPFYKALLRLPVALSDLES 1197
Cdd:COG5021   568 SKEMFNPDYGLFEYITEDLYTLPINPLSS-INPEHlSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLES 646
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1198 LDNEFHQSLQWIRDNDIgTGVDLGLTFCVTEELLGSVVDRELKPGGKNIIINEKNKKEYLERMIKWRLERGVQEQTESLV 1277
Cdd:COG5021   647 LDPELYRSLVWLLNNDI-DETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFK 725
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1278 RGFYEVIDSRLVSVFDARELELVIAGTAE-IDTNDWRLNTEYRsGYHDNHQVIVWFWQVIERFSNEQRLRLLQFVTGTSS 1356
Cdd:COG5021   726 SGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSR 804
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541912 1357 IPYEGFSALRGSTGPRRFCIEKWGKP-NALPRAHTCFNRLDLPPYPTPELLYEKLLLAVEETNTFGIE 1423
Cdd:COG5021   805 IPINGFKDLQGSDGVRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1116-1422 2.51e-124

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 388.51  E-value: 2.51e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  1116 FLLSRELFNPYYGLFEYSANDTYTVQVSPLSAFVDNCH--DWFRFSGRVLGLALVHQYLLDAFFTRPFYKALLRLPVALS 1193
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLEllDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  1194 DLESLDNEFHQSLQWIRDNDIGTGVDLGLTFCVTEelLGSVVDRELKPGGKNIIINEKNKKEYLERMIKWRLERGVQEQT 1273
Cdd:pfam00632   81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  1274 ESLVRGFYEVIDSRLVSVFDARELELVIAGTAEIDTNDWRLNTEYRSGYHDNHQVIVWFWQVIERFSNEQRLRLLQFVTG 1353
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320541912  1354 TSSIPYEGFSALrgstgpRRFCIEKWG--KPNALPRAHTCFNRLDLPPYPTPELLYEKLLLAVEETNTFGI 1422
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECW1_helix pfam18436
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ...
735-791 1.31e-17

Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.


Pssm-ID: 465766  Cd Length: 67  Bit Score: 78.30  E-value: 1.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 320541912   735 LCRPDFYSLLHTNEAALAIYNRNAALKHMVMRIRRDPPCFQRYQYNKDLVALVNTFA 791
Cdd:pfam18436   11 ITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
635-664 2.92e-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: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 56.36  E-value: 2.92e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 320541912   635 LPPAWEARMDSHGRIFYIDHTTRTTSWQRP 664
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
634-664 1.75e-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: 54.14  E-value: 1.75e-09
                            10        20        30
                    ....*....|....*....|....*....|.
gi 320541912    634 PLPPAWEARMDSHGRIFYIDHTTRTTSWQRP 664
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
636-664 2.74e-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: 53.69  E-value: 2.74e-09
                          10        20
                  ....*....|....*....|....*....
gi 320541912  636 PPAWEARMDSHGRIFYIDHTTRTTSWQRP 664
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
408-559 1.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  408 PYLRQHRPLTRALSNGKASSSEEQASPRLllSPKRPRSPPSGCSTRSASPLDISLSPEQHSPTRGRGVGGALQDAVPPGT 487
Cdd:PHA03247 2875 PAAPARPPVRRLARPAVSRSTESFALPPD--QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541912  488 PTFHGQRPQQRLLKRVGGGAGAGATGGATGSPLVCPPTPTHHARRHARLQAVTA-NSSLASggAIPSDPPAVS 559
Cdd:PHA03247 2953 GEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwASSLAL--HEETDPPPVS 3023
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1065-1421 5.34e-155

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: 472.43  E-value: 5.34e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1065 LKLHIRRSHLLEDAFRRIMSANKKDLqRGRLAVLWDTEEGLDYGGPSREFFFLLSRELFNPYYGLFEYSANDTYTVQVSP 1144
Cdd:cd00078     1 LKITVRRDRILEDALRQLSKVSSSDL-KKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1145 LSAFVDNCHDWFRFSGRVLGLALVHQYLLDAFFTRPFYKALLRLPVALSDLESLDNEFHQSLQWIRDNDIGTGvDLGLTF 1224
Cdd:cd00078    80 SSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDED-DLELTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1225 CV-TEELLGSVVDRELKPGGKNIIINEKNKKEYLERMIKWRLERGVQEQTESLVRGFYEVIDSRLVSVFDARELELVIAG 1303
Cdd:cd00078   159 TIeLDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1304 TAEIDTNDWRLNTEYRSGYHDNHQVIVWFWQVIERFSNEQRLRLLQFVTGTSSIPYEGFSALRgstgpRRFCIEKWGKPN 1383
Cdd:cd00078   239 SEDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPD 313
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 320541912 1384 A-LPRAHTCFNRLDLPPYPTPELLYEKLLLAVEETNTFG 1421
Cdd:cd00078   314 DrLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1089-1420 1.86e-145

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: 445.91  E-value: 1.86e-145
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912   1089 DLQRGRLAVLWDTEEGLDYGGPSREFFFLLSRELFNPYYGLFEYSANDtYTVQVSPLSAFVDNCH-DWFRFSGRVLGLAL 1167
Cdd:smart00119    1 DLKKRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPND-YLLYPNPRSGFANEEHlSYFRFIGRVLGKAL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912   1168 VHQYLLDAFFTRPFYKALLRLPVALSDLESLDNEFHQSLQWIR-DNDIGTGVDLGLTFCVTEELlGSVVDRELKPGGKNI 1246
Cdd:smart00119   80 YDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLlNNDTSEELDLTFSIVLTSEF-GQVKVVELKPGGSNI 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912   1247 IINEKNKKEYLERMIKWRLERGVQEQTESLVRGFYEVIDSRLVSVFDARELELVIAGTAEIDTNDWRLNTEYRSGYHDNH 1326
Cdd:smart00119  159 PVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANS 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912   1327 QVIVWFWQVIERFSNEQRLRLLQFVTGTSSIPYEGFSALRGStgprrFCIEKWGKP-NALPRAHTCFNRLDLPPYPTPEL 1405
Cdd:smart00119  239 QTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPK-----FTIRKAGSDdERLPTAHTCFNRLKLPPYSSKEI 313
                           330
                    ....*....|....*
gi 320541912   1406 LYEKLLLAVEETNTF 1420
Cdd:smart00119  314 LREKLLLAINEGKGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1039-1423 2.91e-129

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 422.25  E-value: 2.91e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1039 RRDFEAKLRSFYRKLeSKGYGQGPHKLKLHIRRSHLLEDAFRRIMSANKKDLqRGRLAVLWDTEEGLDYGGPSREFFFLL 1118
Cdd:COG5021   490 RRIKEDKRRKLFYSL-KQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDL-KKTLEIEFVGEEGIDAGGLTREWLFLL 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1119 SRELFNPYYGLFEYSANDTYTVQVSPLSAfVDNCH-DWFRFSGRVLGLALVHQYLLDAFFTRPFYKALLRLPVALSDLES 1197
Cdd:COG5021   568 SKEMFNPDYGLFEYITEDLYTLPINPLSS-INPEHlSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLES 646
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1198 LDNEFHQSLQWIRDNDIgTGVDLGLTFCVTEELLGSVVDRELKPGGKNIIINEKNKKEYLERMIKWRLERGVQEQTESLV 1277
Cdd:COG5021   647 LDPELYRSLVWLLNNDI-DETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFK 725
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912 1278 RGFYEVIDSRLVSVFDARELELVIAGTAE-IDTNDWRLNTEYRsGYHDNHQVIVWFWQVIERFSNEQRLRLLQFVTGTSS 1356
Cdd:COG5021   726 SGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYH-GYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSR 804
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541912 1357 IPYEGFSALRGSTGPRRFCIEKWGKP-NALPRAHTCFNRLDLPPYPTPELLYEKLLLAVEETNTFGIE 1423
Cdd:COG5021   805 IPINGFKDLQGSDGVRKFTIEKGGTDdDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1116-1422 2.51e-124

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 388.51  E-value: 2.51e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  1116 FLLSRELFNPYYGLFEYSANDTYTVQVSPLSAFVDNCH--DWFRFSGRVLGLALVHQYLLDAFFTRPFYKALLRLPVALS 1193
Cdd:pfam00632    1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLEllDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  1194 DLESLDNEFHQSLQWIRDNDIGTGVDLGLTFCVTEelLGSVVDRELKPGGKNIIINEKNKKEYLERMIKWRLERGVQEQT 1273
Cdd:pfam00632   81 DLESIDPELYKSLKSLLNMDNDDDEDLGLTFTIPV--FGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  1274 ESLVRGFYEVIDSRLVSVFDARELELVIAGTAEIDTNDWRLNTEYRSGYHDNHQVIVWFWQVIERFSNEQRLRLLQFVTG 1353
Cdd:pfam00632  159 EAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTG 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320541912  1354 TSSIPYEGFSALrgstgpRRFCIEKWG--KPNALPRAHTCFNRLDLPPYPTPELLYEKLLLAVEETNTFGI 1422
Cdd:pfam00632  239 SSRLPVGGFKSL------PKFTIVRKGgdDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEGEGFGL 303
HECW1_helix pfam18436
Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids ...
735-791 1.31e-17

Helical box domain of E3 ubiquitin-protein ligase HECW1; This is a region of 109 amino acids found in HECW1 proteins in Eukaryotes.Polymorphisms in the same region in the C.elegans homolog affects C. elegans behavioural avoidance of a lawn of Pseudomonas aeruginosa.


Pssm-ID: 465766  Cd Length: 67  Bit Score: 78.30  E-value: 1.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 320541912   735 LCRPDFYSLLHTNEAALAIYNRNAALKHMVMRIRRDPPCFQRYQYNKDLVALVNTFA 791
Cdd:pfam18436   11 ITRPDFFSVLHNNYSAYRMFTNNTCLKHMISKVRRDPRHFERYQHNRDLVNFLNLFA 67
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
635-664 2.92e-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: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 56.36  E-value: 2.92e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 320541912   635 LPPAWEARMDSHGRIFYIDHTTRTTSWQRP 664
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
634-664 1.75e-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: 54.14  E-value: 1.75e-09
                            10        20        30
                    ....*....|....*....|....*....|.
gi 320541912    634 PLPPAWEARMDSHGRIFYIDHTTRTTSWQRP 664
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
636-664 2.74e-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: 53.69  E-value: 2.74e-09
                          10        20
                  ....*....|....*....|....*....
gi 320541912  636 PPAWEARMDSHGRIFYIDHTTRTTSWQRP 664
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
408-559 1.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541912  408 PYLRQHRPLTRALSNGKASSSEEQASPRLllSPKRPRSPPSGCSTRSASPLDISLSPEQHSPTRGRGVGGALQDAVPPGT 487
Cdd:PHA03247 2875 PAAPARPPVRRLARPAVSRSTESFALPPD--QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541912  488 PTFHGQRPQQRLLKRVGGGAGAGATGGATGSPLVCPPTPTHHARRHARLQAVTA-NSSLASggAIPSDPPAVS 559
Cdd:PHA03247 2953 GEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwASSLAL--HEETDPPPVS 3023
 
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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