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Conserved domains on  [gi|1907067363|ref|XP_036017235|]
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E3 ubiquitin-protein ligase TRIP12 isoform X32 [Mus musculus]

Protein Classification

E3 ubiquitin-protein ligase TRIP12 family protein( domain architecture ID 13416587)

E3 ubiquitin-protein ligase TRIP12 (thyroid hormone receptor interactor 12) family protein is involved in a broad range of physiological processes such as mouse embryogenesis; TRIP12 displays a HECT domain, a WW (tryptophan-tryptophan) protein-protein interaction motif and an ARM domain (armadillo/beta-catenin-like repeats)

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 ...
1594-1994 2.94e-125

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: 398.09  E-value: 2.94e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1594 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLCLWRgeevtlsnpkgsqeg 1670
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1671 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1750
Cdd:cd00078     67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1751 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1830
Cdd:cd00078    139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1831 FWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1910
Cdd:cd00078    197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1911 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGq 1990
Cdd:cd00078    275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                   ....
gi 1907067363 1991 QSFH 1994
Cdd:cd00078    349 AGFG 352
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
739-802 3.71e-25

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


:

Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 100.06  E-value: 3.71e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067363  739 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 802
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
SRP1 super family cl34886
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
418-643 2.39e-05

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


The actual alignment was detected with superfamily member COG5064:

Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  418 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 496
Cdd:COG5064     75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  497 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 569
Cdd:COG5064    154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067363  570 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 643
Cdd:COG5064    233 NPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTPALRSVG 310
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1594-1994 2.94e-125

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: 398.09  E-value: 2.94e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1594 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLCLWRgeevtlsnpkgsqeg 1670
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1671 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1750
Cdd:cd00078     67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1751 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1830
Cdd:cd00078    139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1831 FWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1910
Cdd:cd00078    197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1911 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGq 1990
Cdd:cd00078    275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                   ....
gi 1907067363 1991 QSFH 1994
Cdd:cd00078    349 AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1612-1990 3.83e-123

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: 391.21  E-value: 3.83e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1612 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLCLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 1690
Cdd:smart00119    1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1691 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 1770
Cdd:smart00119   62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1771 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFE 1850
Cdd:smart00119  128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1851 SVFPLCHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 1930
Cdd:smart00119  194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1931 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGQ 1990
Cdd:smart00119  272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1641-1996 9.21e-100

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 323.41  E-value: 9.21e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1641 LVSQELQRADLCLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 1720
Cdd:pfam00632    2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1721 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 1800
Cdd:pfam00632   63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1801 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSkaDT 1877
Cdd:pfam00632  114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1878 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 1957
Cdd:pfam00632  192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1907067363 1958 PSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGqQSFHLS 1996
Cdd:pfam00632  267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1504-1995 9.42e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 283.97  E-value: 9.42e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1504 TSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGktcPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQD 1583
Cdd:COG5021    410 SSSTYEDLRREQLGRESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFI 482
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1584 SRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSRAM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLCLW 1654
Cdd:COG5021    483 SLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRRDRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTRE 562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1655 RgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KPAHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLR 1732
Cdd:COG5021    563 W--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNPEHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG 636
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1733 QetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKsqTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGG 1812
Cdd:COG5021    637 K--PVSLVDLESLDPELYRSL---------VWLLNNDI--DETIL-----DLTF---TVEDDSFGESRT----VELIPNG 691
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1813 KDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHG 1892
Cdd:COG5021    692 RNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHG 769
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1893 YTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDY 1972
Cdd:COG5021    770 YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEY 849
                          490       500
                   ....*....|....*....|...
gi 1907067363 1973 SSIDIMRDKLLIAAREGQQSFHL 1995
Cdd:COG5021    850 SSKEKLRSKLLTAINEGAGFGLL 872
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
739-802 3.71e-25

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 100.06  E-value: 3.71e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067363  739 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 802
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
739-806 4.29e-21

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 88.94  E-value: 4.29e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067363   739 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNP 806
Cdd:smart00678    2 VWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYS 69
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
418-643 2.39e-05

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  418 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 496
Cdd:COG5064     75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  497 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 569
Cdd:COG5064    154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067363  570 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 643
Cdd:COG5064    233 NPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTPALRSVG 310
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
1594-1994 2.94e-125

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: 398.09  E-value: 2.94e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1594 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLCLWRgeevtlsnpkgsqeg 1670
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1671 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1750
Cdd:cd00078     67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1751 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1830
Cdd:cd00078    139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1831 FWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1910
Cdd:cd00078    197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1911 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGq 1990
Cdd:cd00078    275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                   ....
gi 1907067363 1991 QSFH 1994
Cdd:cd00078    349 AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1612-1990 3.83e-123

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: 391.21  E-value: 3.83e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1612 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLCLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 1690
Cdd:smart00119    1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1691 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 1770
Cdd:smart00119   62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1771 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFE 1850
Cdd:smart00119  128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1851 SVFPLCHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 1930
Cdd:smart00119  194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  1931 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGQ 1990
Cdd:smart00119  272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1641-1996 9.21e-100

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 323.41  E-value: 9.21e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1641 LVSQELQRADLCLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 1720
Cdd:pfam00632    2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1721 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 1800
Cdd:pfam00632   63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1801 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSkaDT 1877
Cdd:pfam00632  114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1878 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 1957
Cdd:pfam00632  192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1907067363 1958 PSVMTCVNYLKLPDYSSIDIMRDKLLIAAREGqQSFHLS 1996
Cdd:pfam00632  267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1504-1995 9.42e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 283.97  E-value: 9.42e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1504 TSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGktcPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQD 1583
Cdd:COG5021    410 SSSTYEDLRREQLGRESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFI 482
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1584 SRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSRAM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLCLW 1654
Cdd:COG5021    483 SLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRRDRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTRE 562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1655 RgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KPAHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLR 1732
Cdd:COG5021    563 W--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNPEHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG 636
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1733 QetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKsqTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGG 1812
Cdd:COG5021    637 K--PVSLVDLESLDPELYRSL---------VWLLNNDI--DETIL-----DLTF---TVEDDSFGESRT----VELIPNG 691
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1813 KDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLCHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHG 1892
Cdd:COG5021    692 RNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHG 769
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363 1893 YTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDY 1972
Cdd:COG5021    770 YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEY 849
                          490       500
                   ....*....|....*....|...
gi 1907067363 1973 SSIDIMRDKLLIAAREGQQSFHL 1995
Cdd:COG5021    850 SSKEKLRSKLLTAINEGAGFGLL 872
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
739-802 3.71e-25

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 100.06  E-value: 3.71e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067363  739 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 802
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
739-806 4.29e-21

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 88.94  E-value: 4.29e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067363   739 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNP 806
Cdd:smart00678    2 VWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYS 69
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
418-643 2.39e-05

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  418 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 496
Cdd:COG5064     75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067363  497 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 569
Cdd:COG5064    154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067363  570 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 643
Cdd:COG5064    233 NPPpDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSDGPNEKIQAVLDVGIPgrlvELLSH-ESAKIQTPALRSVG 310
 
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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