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Conserved domains on  [gi|56971359|gb|AAH88304|]
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Trip12 protein, partial [Rattus norvegicus]

Protein Classification

HECT domain-containing protein( domain architecture ID 12189884)

HECT domain-containing protein may function as an E3 ubiquitin-protein ligase that catalyzes the attachment of ubiquitin chains to target proteins

CATH:  3.30.2410.10
EC:  2.3.2.26
Gene Ontology:  GO:0004842
PubMed:  22389392|29016349
SCOP:  4002196

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
78-456 2.33e-130

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: 380.04  E-value: 2.33e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359     78 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 156
Cdd:smart00119   1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    157 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 236
Cdd:smart00119  62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    237 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFE 316
Cdd:smart00119 128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    317 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 396
Cdd:smart00119 194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    397 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGQ 456
Cdd:smart00119 272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
78-456 2.33e-130

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: 380.04  E-value: 2.33e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359     78 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 156
Cdd:smart00119   1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    157 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 236
Cdd:smart00119  62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    237 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFE 316
Cdd:smart00119 128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    317 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 396
Cdd:smart00119 194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    397 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGQ 456
Cdd:smart00119 272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
60-460 2.33e-130

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: 380.76  E-value: 2.33e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359  60 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 136
Cdd:cd00078   2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 137 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 216
Cdd:cd00078  67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 217 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 296
Cdd:cd00078 139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 297 FWALNEGVCRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 376
Cdd:cd00078 197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 377 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGq 456
Cdd:cd00078 275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                ....
gi 56971359 457 QSFH 460
Cdd:cd00078 349 AGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
107-462 9.50e-105

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 313.78  E-value: 9.50e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   107 LVSQELQRADLGLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 186
Cdd:pfam00632   2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   187 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 266
Cdd:pfam00632  63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   267 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDT 343
Cdd:pfam00632 114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   344 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 423
Cdd:pfam00632 192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 56971359   424 PSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGqQSFHLS 462
Cdd:pfam00632 267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
9-461 2.68e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 266.25  E-value: 2.68e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   9 PFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQDSRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSR 83
Cdd:COG5021 446 PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRR 521
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359  84 AM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLGLWRgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KP 157
Cdd:COG5021 522 DRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTREW--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNP 599
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 158 AHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKs 237
Cdd:COG5021 600 EHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGK--PVSLVDLESLDPELYRSL---------VWLLNNDI- 663
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 238 qTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFES 317
Cdd:COG5021 664 -DETIL-----DLTF---TVEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSE 730
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 318 VFPLSHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVG 397
Cdd:COG5021 731 IIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPIN 808
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56971359 398 GFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGQQSFHL 461
Cdd:COG5021 809 GFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
78-456 2.33e-130

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: 380.04  E-value: 2.33e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359     78 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 156
Cdd:smart00119   1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    157 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 236
Cdd:smart00119  62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    237 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFE 316
Cdd:smart00119 128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    317 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 396
Cdd:smart00119 194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359    397 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGQ 456
Cdd:smart00119 272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
60-460 2.33e-130

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: 380.76  E-value: 2.33e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359  60 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 136
Cdd:cd00078   2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 137 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 216
Cdd:cd00078  67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 217 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 296
Cdd:cd00078 139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 297 FWALNEGVCRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 376
Cdd:cd00078 197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 377 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGq 456
Cdd:cd00078 275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                ....
gi 56971359 457 QSFH 460
Cdd:cd00078 349 AGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
107-462 9.50e-105

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 313.78  E-value: 9.50e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   107 LVSQELQRADLGLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 186
Cdd:pfam00632   2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   187 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 266
Cdd:pfam00632  63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   267 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDT 343
Cdd:pfam00632 114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   344 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 423
Cdd:pfam00632 192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 56971359   424 PSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGqQSFHLS 462
Cdd:pfam00632 267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
9-461 2.68e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 266.25  E-value: 2.68e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359   9 PFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQDSRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSR 83
Cdd:COG5021 446 PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFISLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRR 521
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359  84 AM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLGLWRgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KP 157
Cdd:COG5021 522 DRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTREW--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNP 599
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 158 AHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKs 237
Cdd:COG5021 600 EHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGK--PVSLVDLESLDPELYRSL---------VWLLNNDI- 663
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 238 qTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFES 317
Cdd:COG5021 664 -DETIL-----DLTF---TVEDDSFGESRT----VELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSE 730
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56971359 318 VFPLSHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVG 397
Cdd:COG5021 731 IIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPIN 808
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56971359 398 GFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGQQSFHL 461
Cdd:COG5021 809 GFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAGFGLL 872
 
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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