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Conserved domains on  [gi|1907205764|ref|XP_036017960|]
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E3 ubiquitin-protein ligase HUWE1 isoform X8 [Mus musculus]

Protein Classification

DUF913 and HECTc domain-containing protein( domain architecture ID 11003809)

protein containing domains DUF913, UBA_HUWE1, DUF4414, and HECTc

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 ...
4014-4367 9.96e-161

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: 501.71  E-value: 9.96e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4014 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4093
Cdd:cd00078      3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4094 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4173
Cdd:cd00078     83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4174 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4252
Cdd:cd00078    163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4253 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4331
Cdd:cd00078    243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1907205764 4332 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4367
Cdd:cd00078    318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
431-814 1.71e-106

Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.


:

Pssm-ID: 461803  Cd Length: 369  Bit Score: 346.52  E-value: 1.71e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMDGVQC---IP-Q 503
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEYKSSVVdyeIPyY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  504 RAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNG 580
Cdd:pfam06025   67 RQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  581 LTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLG 660
Cdd:pfam06025  147 LSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLG 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  661 SAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEevqa 737
Cdd:pfam06025  221 SSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESS---- 296
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907205764  738 mQSFNSAQQNETEPNQQVVGTEERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 814
Cdd:pfam06025  297 -SDEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 super family cl20318
Domain of Unknown Function (DUF908);
92-367 1.30e-23

Domain of Unknown Function (DUF908);


The actual alignment was detected with superfamily member pfam06012:

Pssm-ID: 428721  Cd Length: 351  Bit Score: 105.88  E-value: 1.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764   92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012    5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  160 LTRLQHLAESWG------------------GKENGFGLAECCRDlQMLKYPPSATTLHFEFYADPGAEVKIEK------- 214
Cdd:pfam06012   85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKE-DSKVLPSEWGSVKFTYYPSSSSDEAPTSsksstss 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  215 ----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFTH 260
Cdd:pfam06012  164 nsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLHR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  261 IRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIVH 336
Cdd:pfam06012  242 IRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALAR 321
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1907205764  337 leRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  322 --HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
1308-1347 6.06e-15

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


:

Pssm-ID: 270474  Cd Length: 40  Bit Score: 71.28  E-value: 6.06e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907205764 1308 VNQQQLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHP 1347
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1608-1669 4.45e-14

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: 69.63  E-value: 4.45e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907205764 1608 WRWFDDRsGRWCSYSASNNSTIDSAWKSGETSV--RFTAGRRRYTVQFTTMVQVNEETGNRRPV 1669
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
3002-3035 1.10e-07

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


:

Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 50.58  E-value: 1.10e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907205764 3002 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3035
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2957-2984 2.20e-06

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


:

Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 46.73  E-value: 2.20e-06
                           10        20
                   ....*....|....*....|....*...
gi 1907205764 2957 PEGVDPSFLAALPDDIRREVLQNQLGIR 2984
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
4014-4367 9.96e-161

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: 501.71  E-value: 9.96e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4014 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4093
Cdd:cd00078      3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4094 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4173
Cdd:cd00078     83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4174 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4252
Cdd:cd00078    163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4253 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4331
Cdd:cd00078    243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1907205764 4332 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4367
Cdd:cd00078    318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
4038-4366 3.66e-159

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: 495.99  E-value: 3.66e-159
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  4038 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNR 4117
Cdd:smart00119    4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  4118 LLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYL-LENDVSTLgYDLTFSTEVQE-FGVCEVRDLKPNGANILVTE 4195
Cdd:smart00119   84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  4196 ENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQ 4274
Cdd:smart00119  163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  4275 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHM 4354
Cdd:smart00119  243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
                           330
                    ....*....|..
gi 1907205764  4355 LLLAIQECsEGF 4366
Cdd:smart00119  318 LLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3952-4369 2.04e-146

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 481.19  E-value: 2.04e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 3952 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRVLDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4027
Cdd:COG5021    454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4028 ELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4107
Cdd:COG5021    531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4108 IVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPN 4187
Cdd:COG5021    611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4188 GANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKSNTEYHKY 4266
Cdd:COG5021    691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4267 QSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4346
Cdd:COG5021    771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850
                          410       420
                   ....*....|....*....|...
gi 1907205764 4347 SFEKLRHMLLLAIQECSeGFGLA 4369
Cdd:COG5021    851 SKEKLRSKLLTAINEGA-GFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
4063-4369 2.02e-120

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 383.88  E-value: 2.02e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4063 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4140
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4141 MESEDYHFYQGLVYLLENDVSTLG-YDLTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLA 4219
Cdd:pfam00632   82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4220 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGT 4298
Cdd:pfam00632  160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907205764 4299 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFGLA 4369
Cdd:pfam00632  240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
431-814 1.71e-106

Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.


Pssm-ID: 461803  Cd Length: 369  Bit Score: 346.52  E-value: 1.71e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMDGVQC---IP-Q 503
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEYKSSVVdyeIPyY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  504 RAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNG 580
Cdd:pfam06025   67 RQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  581 LTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLG 660
Cdd:pfam06025  147 LSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLG 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  661 SAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEevqa 737
Cdd:pfam06025  221 SSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESS---- 296
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907205764  738 mQSFNSAQQNETEPNQQVVGTEERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 814
Cdd:pfam06025  297 -SDEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
92-367 1.30e-23

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 105.88  E-value: 1.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764   92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012    5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  160 LTRLQHLAESWG------------------GKENGFGLAECCRDlQMLKYPPSATTLHFEFYADPGAEVKIEK------- 214
Cdd:pfam06012   85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKE-DSKVLPSEWGSVKFTYYPSSSSDEAPTSsksstss 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  215 ----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFTH 260
Cdd:pfam06012  164 nsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLHR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  261 IRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIVH 336
Cdd:pfam06012  242 IRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALAR 321
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1907205764  337 leRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  322 --HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
1308-1347 6.06e-15

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


Pssm-ID: 270474  Cd Length: 40  Bit Score: 71.28  E-value: 6.06e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907205764 1308 VNQQQLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHP 1347
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1608-1669 4.45e-14

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: 69.63  E-value: 4.45e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907205764 1608 WRWFDDRsGRWCSYSASNNSTIDSAWKSGETSV--RFTAGRRRYTVQFTTMVQVNEETGNRRPV 1669
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1608-1669 9.45e-12

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 63.13  E-value: 9.45e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907205764  1608 WRW-FDDRSGRWCSYSASNNSTIDSAWKSGETSVRFTAGRRRYTVQFTTMVQVNEETGNRRPV 1669
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKV 63
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
3002-3035 1.10e-07

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 50.58  E-value: 1.10e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907205764 3002 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3035
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2957-2984 2.20e-06

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 46.73  E-value: 2.20e-06
                           10        20
                   ....*....|....*....|....*...
gi 1907205764 2957 PEGVDPSFLAALPDDIRREVLQNQLGIR 2984
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
2960-2978 9.72e-03

Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.


Pssm-ID: 412037  Cd Length: 36  Bit Score: 36.43  E-value: 9.72e-03
                           10
                   ....*....|....*....
gi 1907205764 2960 VDPSFLAALPDDIRREVLQ 2978
Cdd:cd19318     12 VDPSVLAALPPDLQEELEA 30
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
4014-4367 9.96e-161

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: 501.71  E-value: 9.96e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4014 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4093
Cdd:cd00078      3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4094 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4173
Cdd:cd00078     83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4174 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4252
Cdd:cd00078    163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4253 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4331
Cdd:cd00078    243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1907205764 4332 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4367
Cdd:cd00078    318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
4038-4366 3.66e-159

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: 495.99  E-value: 3.66e-159
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  4038 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNR 4117
Cdd:smart00119    4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  4118 LLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYL-LENDVSTLgYDLTFSTEVQE-FGVCEVRDLKPNGANILVTE 4195
Cdd:smart00119   84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  4196 ENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQ 4274
Cdd:smart00119  163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  4275 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHM 4354
Cdd:smart00119  243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
                           330
                    ....*....|..
gi 1907205764  4355 LLLAIQECsEGF 4366
Cdd:smart00119  318 LLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3952-4369 2.04e-146

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 481.19  E-value: 2.04e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 3952 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRVLDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4027
Cdd:COG5021    454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4028 ELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4107
Cdd:COG5021    531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4108 IVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPN 4187
Cdd:COG5021    611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4188 GANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKSNTEYHKY 4266
Cdd:COG5021    691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4267 QSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4346
Cdd:COG5021    771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850
                          410       420
                   ....*....|....*....|...
gi 1907205764 4347 SFEKLRHMLLLAIQECSeGFGLA 4369
Cdd:COG5021    851 SKEKLRSKLLTAINEGA-GFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
4063-4369 2.02e-120

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 383.88  E-value: 2.02e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4063 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4140
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4141 MESEDYHFYQGLVYLLENDVSTLG-YDLTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLA 4219
Cdd:pfam00632   82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764 4220 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGT 4298
Cdd:pfam00632  160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907205764 4299 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFGLA 4369
Cdd:pfam00632  240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
431-814 1.71e-106

Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.


Pssm-ID: 461803  Cd Length: 369  Bit Score: 346.52  E-value: 1.71e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMDGVQC---IP-Q 503
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEYKSSVVdyeIPyY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  504 RAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNG 580
Cdd:pfam06025   67 RQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  581 LTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLG 660
Cdd:pfam06025  147 LSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLG 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  661 SAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEevqa 737
Cdd:pfam06025  221 SSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESS---- 296
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907205764  738 mQSFNSAQQNETEPNQQVVGTEERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 814
Cdd:pfam06025  297 -SDEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
92-367 1.30e-23

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 105.88  E-value: 1.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764   92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012    5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  160 LTRLQHLAESWG------------------GKENGFGLAECCRDlQMLKYPPSATTLHFEFYADPGAEVKIEK------- 214
Cdd:pfam06012   85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKE-DSKVLPSEWGSVKFTYYPSSSSDEAPTSsksstss 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  215 ----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFTH 260
Cdd:pfam06012  164 nsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLHR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907205764  261 IRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIVH 336
Cdd:pfam06012  242 IRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALAR 321
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1907205764  337 leRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  322 --HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
1308-1347 6.06e-15

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


Pssm-ID: 270474  Cd Length: 40  Bit Score: 71.28  E-value: 6.06e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907205764 1308 VNQQQLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHP 1347
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1608-1669 4.45e-14

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: 69.63  E-value: 4.45e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907205764 1608 WRWFDDRsGRWCSYSASNNSTIDSAWKSGETSV--RFTAGRRRYTVQFTTMVQVNEETGNRRPV 1669
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1608-1669 9.45e-12

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 63.13  E-value: 9.45e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907205764  1608 WRW-FDDRSGRWCSYSASNNSTIDSAWKSGETSVRFTAGRRRYTVQFTTMVQVNEETGNRRPV 1669
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKV 63
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
3002-3035 1.10e-07

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 50.58  E-value: 1.10e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907205764 3002 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3035
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2957-2984 2.20e-06

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 46.73  E-value: 2.20e-06
                           10        20
                   ....*....|....*....|....*...
gi 1907205764 2957 PEGVDPSFLAALPDDIRREVLQNQLGIR 2984
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
1317-1346 2.48e-04

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 41.13  E-value: 2.48e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907205764 1317 MDMGFTREHAMEAL--LNTSTMEQATEYLLTH 1346
Cdd:cd14327      7 VEMGFSRERAEEALraVGTNSVELAMEWLFTN 38
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
2960-2978 9.72e-03

Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.


Pssm-ID: 412037  Cd Length: 36  Bit Score: 36.43  E-value: 9.72e-03
                           10
                   ....*....|....*....
gi 1907205764 2960 VDPSFLAALPDDIRREVLQ 2978
Cdd:cd19318     12 VDPSVLAALPPDLQEELEA 30
 
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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