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Conserved domains on  [gi|1135449794|ref|NP_001335258|]
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E3 ubiquitin-protein ligase TRIP12 isoform i [Homo sapiens]

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 ...
1666-2066 2.24e-128

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: 407.34  E-value: 2.24e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1666 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1742
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1743 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1822
Cdd:cd00078     67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1823 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1902
Cdd:cd00078    139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1903 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1982
Cdd:cd00078    197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1983 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 2062
Cdd:cd00078    275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                   ....
gi 1135449794 2063 QSFH 2066
Cdd:cd00078    349 AGFG 352
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
810-874 1.61e-23

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: 95.44  E-value: 1.61e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1135449794  810 IWQWRDDRGLWHPYNRIDSRIIEvAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 874
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIE-EAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
SRP1 super family cl34886
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
489-714 2.51e-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: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  489 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 567
Cdd:COG5064     75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  568 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 640
Cdd:COG5064    154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1135449794  641 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 714
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 ...
1666-2066 2.24e-128

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: 407.34  E-value: 2.24e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1666 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1742
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1743 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1822
Cdd:cd00078     67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1823 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1902
Cdd:cd00078    139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1903 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1982
Cdd:cd00078    197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1983 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 2062
Cdd:cd00078    275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                   ....
gi 1135449794 2063 QSFH 2066
Cdd:cd00078    349 AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1684-2062 4.06e-126

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: 399.69  E-value: 4.06e-126
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  1684 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 1762
Cdd:smart00119    1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  1763 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 1842
Cdd:smart00119   62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  1843 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFE 1922
Cdd:smart00119  128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  1923 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 2002
Cdd:smart00119  194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  2003 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQ 2062
Cdd:smart00119  272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1713-2068 1.31e-103

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 334.58  E-value: 1.31e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1713 LVSQELQRADLGLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 1792
Cdd:pfam00632    2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1793 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 1872
Cdd:pfam00632   63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1873 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDT 1949
Cdd:pfam00632  114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1950 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 2029
Cdd:pfam00632  192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1135449794 2030 PSVMTCVNYLKLPDYSSIEIMREKLLIAAREGqQSFHLS 2068
Cdd:pfam00632  267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1576-2067 6.39e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 284.35  E-value: 6.39e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1576 TSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGktcPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQD 1655
Cdd:COG5021    410 SSSTYEDLRREQLGRESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFI 482
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1656 SRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSRAM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLGLW 1726
Cdd:COG5021    483 SLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRRDRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTRE 562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1727 RgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KPAHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLR 1804
Cdd:COG5021    563 W--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNPEHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG 636
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1805 QetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKsqTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGG 1884
Cdd:COG5021    637 K--PVSLVDLESLDPELYRSL---------VWLLNNDI--DETIL-----DLTF---TVEDDSFGESRT----VELIPNG 691
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1885 KDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHG 1964
Cdd:COG5021    692 RNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHG 769
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1965 YTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDY 2044
Cdd:COG5021    770 YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEY 849
                          490       500
                   ....*....|....*....|...
gi 1135449794 2045 SSIEIMREKLLIAAREGQQSFHL 2067
Cdd:COG5021    850 SSKEKLRSKLLTAINEGAGFGLL 872
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
810-874 1.61e-23

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: 95.44  E-value: 1.61e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1135449794  810 IWQWRDDRGLWHPYNRIDSRIIEvAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 874
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIE-EAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
810-878 1.87e-19

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 84.31  E-value: 1.87e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1135449794   810 IWQWRDDRGLWHPYNRIDSRIIEvAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNP 878
Cdd:smart00678    2 VWEYEGRNGKWWPYDPRVSEDIE-EAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYS 69
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
489-714 2.51e-05

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  489 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 567
Cdd:COG5064     75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  568 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 640
Cdd:COG5064    154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1135449794  641 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 714
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 ...
1666-2066 2.24e-128

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: 407.34  E-value: 2.24e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1666 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1742
Cdd:cd00078      2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1743 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1822
Cdd:cd00078     67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1823 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1902
Cdd:cd00078    139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1903 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1982
Cdd:cd00078    197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1983 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 2062
Cdd:cd00078    275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                   ....
gi 1135449794 2063 QSFH 2066
Cdd:cd00078    349 AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1684-2062 4.06e-126

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: 399.69  E-value: 4.06e-126
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  1684 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 1762
Cdd:smart00119    1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  1763 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 1842
Cdd:smart00119   62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  1843 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFE 1922
Cdd:smart00119  128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  1923 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 2002
Cdd:smart00119  194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  2003 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQ 2062
Cdd:smart00119  272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1713-2068 1.31e-103

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 334.58  E-value: 1.31e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1713 LVSQELQRADLGLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 1792
Cdd:pfam00632    2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1793 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 1872
Cdd:pfam00632   63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1873 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDT 1949
Cdd:pfam00632  114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1950 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 2029
Cdd:pfam00632  192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1135449794 2030 PSVMTCVNYLKLPDYSSIEIMREKLLIAAREGqQSFHLS 2068
Cdd:pfam00632  267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1576-2067 6.39e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 284.35  E-value: 6.39e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1576 TSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGktcPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQD 1655
Cdd:COG5021    410 SSSTYEDLRREQLGRESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFI 482
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1656 SRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSRAM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLGLW 1726
Cdd:COG5021    483 SLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRRDRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTRE 562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1727 RgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KPAHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLR 1804
Cdd:COG5021    563 W--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNPEHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG 636
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1805 QetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKsqTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGG 1884
Cdd:COG5021    637 K--PVSLVDLESLDPELYRSL---------VWLLNNDI--DETIL-----DLTF---TVEDDSFGESRT----VELIPNG 691
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1885 KDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHG 1964
Cdd:COG5021    692 RNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHG 769
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794 1965 YTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDY 2044
Cdd:COG5021    770 YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEY 849
                          490       500
                   ....*....|....*....|...
gi 1135449794 2045 SSIEIMREKLLIAAREGQQSFHL 2067
Cdd:COG5021    850 SSKEKLRSKLLTAINEGAGFGLL 872
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
810-874 1.61e-23

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: 95.44  E-value: 1.61e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1135449794  810 IWQWRDDRGLWHPYNRIDSRIIEvAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 874
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIE-EAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
810-878 1.87e-19

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 84.31  E-value: 1.87e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1135449794   810 IWQWRDDRGLWHPYNRIDSRIIEvAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNP 878
Cdd:smart00678    2 VWEYEGRNGKWWPYDPRVSEDIE-EAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYS 69
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
489-714 2.51e-05

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  489 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 567
Cdd:COG5064     75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1135449794  568 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 640
Cdd:COG5064    154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1135449794  641 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 714
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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