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Conserved domains on  [gi|545746316|ref|NP_001271144|]
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E3 ubiquitin-protein ligase TRIP12 isoform b [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 ...
1623-2023 2.47e-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: 406.95  E-value: 2.47e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1623 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1699
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1700 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1779
Cdd:cd00078    67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1780 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1859
Cdd:cd00078   139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1860 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1939
Cdd:cd00078   197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1940 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 2019
Cdd:cd00078   275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                  ....
gi 545746316 2020 QSFH 2023
Cdd:cd00078   349 AGFG 352
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
768-831 3.76e-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: 3.76e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545746316   768 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 831
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
SRP1 super family cl34886
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
447-672 2.71e-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: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  447 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 525
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  526 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 598
Cdd:COG5064   154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545746316  599 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 672
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 ...
1623-2023 2.47e-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: 406.95  E-value: 2.47e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1623 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1699
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1700 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1779
Cdd:cd00078    67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1780 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1859
Cdd:cd00078   139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1860 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1939
Cdd:cd00078   197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1940 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 2019
Cdd:cd00078   275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                  ....
gi 545746316 2020 QSFH 2023
Cdd:cd00078   349 AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1641-2019 3.64e-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: 3.64e-126
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1641 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 1719
Cdd:smart00119    1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1720 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 1799
Cdd:smart00119   62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1800 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFE 1879
Cdd:smart00119  128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1880 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 1959
Cdd:smart00119  194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1960 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQ 2019
Cdd:smart00119  272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1670-2025 1.27e-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: 1.27e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  1670 LVSQELQRADLGLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 1749
Cdd:pfam00632    2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  1750 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 1829
Cdd:pfam00632   63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  1830 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDT 1906
Cdd:pfam00632  114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  1907 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 1986
Cdd:pfam00632  192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 545746316  1987 PSVMTCVNYLKLPDYSSIEIMREKLLIAAREGqQSFHLS 2025
Cdd:pfam00632  267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1533-2024 6.42e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 284.35  E-value: 6.42e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1533 TSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGktcPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQD 1612
Cdd:COG5021   410 SSSTYEDLRREQLGRESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFI 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1613 SRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSRAM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLGLW 1683
Cdd:COG5021   483 SLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRRDRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTRE 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1684 RgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KPAHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLR 1761
Cdd:COG5021   563 W--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNPEHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG 636
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1762 QetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKsqTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGG 1841
Cdd:COG5021   637 K--PVSLVDLESLDPELYRSL---------VWLLNNDI--DETIL-----DLTF---TVEDDSFGESRT----VELIPNG 691
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1842 KDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHG 1921
Cdd:COG5021   692 RNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHG 769
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1922 YTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDY 2001
Cdd:COG5021   770 YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEY 849
                         490       500
                  ....*....|....*....|...
gi 545746316 2002 SSIEIMREKLLIAAREGQQSFHL 2024
Cdd:COG5021   850 SSKEKLRSKLLTAINEGAGFGLL 872
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
768-831 3.76e-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: 3.76e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545746316   768 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 831
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
768-835 4.35e-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: 4.35e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545746316    768 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNP 835
Cdd:smart00678    2 VWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYS 69
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
447-672 2.71e-05

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  447 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 525
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  526 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 598
Cdd:COG5064   154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545746316  599 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 672
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 ...
1623-2023 2.47e-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: 406.95  E-value: 2.47e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1623 KRTVNREELLKQAESVMQDLGSS--RAMLEIQYENEVGTG-LGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqeg 1699
Cdd:cd00078     2 KITVRRDRILEDALRQLSKVSSSdlKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFR--------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1700 tkYIQNLQGLFALPfgrtAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQetSLTSHDLFDIDPVVA 1779
Cdd:cd00078    67 --YTPDDSGLLYPN----PSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGK--PLSLEDLEELDPELY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1780 RSVYHLEDIVRQKKRLEQdksqtkeslqyaleTLTMNgcsvedlgLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVI 1859
Cdd:cd00078   139 KSLKELLDNDGDEDDLEL--------------TFTIE--------LDSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1860 FWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSF 1939
Cdd:cd00078   197 DYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGS--EDIDLEDLKKNTEYKGGYSSDSPTIQWFWEVLESF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1940 DNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKtfestENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGq 2019
Cdd:cd00078   275 TNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRV-----GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG- 348

                  ....
gi 545746316 2020 QSFH 2023
Cdd:cd00078   349 AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
1641-2019 3.64e-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: 3.64e-126
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1641 DLGSSRamLEIQYENEVG-TGLGPTLEFYALVSQELQRADLGLWRgeevtlsnpkgsqegtkYIQNLQGLFALPFGRTAK 1719
Cdd:smart00119    1 DLKKRV--LEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFR-----------------YSPNDYLLYPNPRSGFAN 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1720 PAHIakvkMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRqeTSLTSHDLFDIDPVVARSVYHLedivrqkkRLEQDK 1799
Cdd:smart00119   62 EEHL----SYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLG--KPVTLHDLESLDPELYKSLKWL--------LLNNDT 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1800 SqtkeslqYALETltmngcsVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFE 1879
Cdd:smart00119  128 S-------EELDL-------TFSIVLTSEFGQVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFS 193
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1880 SVFPLSHLQYFYPEELDQLLCGSKadTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPV 1959
Cdd:smart00119  194 EVIPENLLKLFDPEELELLICGSP--EIDVDDLKSNTEYKGGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPV 271
                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316   1960 GGFRSLNPPLTIVRKTFEstenpDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQ 2019
Cdd:smart00119  272 GGFAALSPKFTIRKAGSD-----DERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEGK 326
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
1670-2025 1.27e-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: 1.27e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  1670 LVSQELQRADLGLWRGEevtlsnpkgsQEGTKYIqnlqglfalPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDL 1749
Cdd:pfam00632    2 LLSKELFDPNYGLFEYE----------TEDDRTY---------WFNPSSSESPDLELLDYFKFLGKLLGKAIYNGILLDL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  1750 PLGLPFYKWMLRQEtsLTSHDLFDIDPVVARSVYHLedivrqkkrleqdksqtkeslqyaletLTMNGCSVEDLGLDFTL 1829
Cdd:pfam00632   63 PFPPFFYKKLLGEP--LTLEDLESIDPELYKSLKSL---------------------------LNMDNDDDEDLGLTFTI 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  1830 PGF---PNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkaDT 1906
Cdd:pfam00632  114 PVFgesKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGS--PE 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  1907 WDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLnPPLTIVRKTFesteNPDDFL 1986
Cdd:pfam00632  192 IDVEDLKKNTEYDGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVGGFKSL-PKFTIVRKGG----DDDDRL 266
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 545746316  1987 PSVMTCVNYLKLPDYSSIEIMREKLLIAAREGqQSFHLS 2025
Cdd:pfam00632  267 PTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
1533-2024 6.42e-80

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 284.35  E-value: 6.42e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1533 TSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGktcPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPeinqSDSQD 1612
Cdd:COG5021   410 SSSTYEDLRREQLGRESDESFYVASNVQQQRASREG---PLLSGWKTRLNNLYRFYFVEHRKKTLTKNDSR----LGSFI 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1613 SRVAPRLDRKKRTVNREELLKQAESVM-----QDLGSSRAM----LEIQYENEVGTGLGPTLEFYALVSQELQRADLGLW 1683
Cdd:COG5021   483 SLNKLDIRRIKEDKRRKLFYSLKQKAKifdpyLHIKVRRDRvfedSYREIMDESGDDLKKTLEIEFVGEEGIDAGGLTRE 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1684 RgeEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTA--KPAHIAKvkmkFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLR 1761
Cdd:COG5021   563 W--LFLLSKEMFNPDYGLFEYITEDLYTLPINPLSsiNPEHLSY----FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLG 636
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1762 QetSLTSHDLFDIDPVVARSVyhledivrqKKRLEQDKsqTKESLqyaleTLTMngcSVEDLGLDFTLPgfpnIELKKGG 1841
Cdd:COG5021   637 K--PVSLVDLESLDPELYRSL---------VWLLNNDI--DETIL-----DLTF---TVEDDSFGESRT----VELIPNG 691
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1842 KDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSkADTWDAKTLMECCRpDHG 1921
Cdd:COG5021   692 RNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGI-PEDIDIDDWKSNTA-YHG 769
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316 1922 YTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDY 2001
Cdd:COG5021   770 YTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEY 849
                         490       500
                  ....*....|....*....|...
gi 545746316 2002 SSIEIMREKLLIAAREGQQSFHL 2024
Cdd:COG5021   850 SSKEKLRSKLLTAINEGAGFGLL 872
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
768-831 3.76e-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: 3.76e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545746316   768 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLS--TLGRVYTIDFNSMQQINEDTGTARAIQR 831
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEVSSLIEEAYQKGKPSVDLSitTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
768-835 4.35e-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: 4.35e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545746316    768 IWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNP 835
Cdd:smart00678    2 VWEYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYS 69
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
447-672 2.71e-05

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 49.12  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  447 QLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQmEHNFDIMN-HACRALTYMMEALPRSSAVV 525
Cdd:COG5064    75 QLTQQLFSDDIEQQLQAVYKFRKLLSKETSPPIQPVIDAGVVPRFVEFMD-EIQRDMLQfEAAWALTNIASGTTQQTKVV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746316  526 VD--AIPVFLEKLQVIQcIDVAEQALTALEML---SRRHSKAILQAGGLADCLLYLEFFSINAQ--RNALAIAANCCQSI 598
Cdd:COG5064   154 VDagAVPLFIQLLSSTE-DDVREQAVWALGNIagdSEGCRDYVLQCGALEPLLGLLLSSAIHISmlRNATWTLSNLCRGK 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545746316  599 TPD-EFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASK----DLLTNvQQLLVVTPPILSSG 672
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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