ID G3VDH6_SARHA Unreviewed; 4250 AA.
AC G3VDH6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=HUWE1 {ECO:0000313|Ensembl:ENSSHAP00000001230.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000001230.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000001230.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000001230.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR STRING; 9305.ENSSHAP00000001230; -.
DR Ensembl; ENSSHAT00000001245.2; ENSSHAP00000001230.2; ENSSHAG00000001097.2.
DR eggNOG; KOG0939; Eukaryota.
DR GeneTree; ENSGT00940000156319; -.
DR HOGENOM; CLU_000058_0_0_1; -.
DR InParanoid; G3VDH6; -.
DR TreeFam; TF323417; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0140852; F:histone ubiquitin ligase activity; IEA:Ensembl.
DR GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IEA:Ensembl.
DR GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd14288; UBA_HUWE1; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 6.10.250.1630; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041918; UBA_HUWE1.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1345..1384
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1630..1709
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 3915..4225
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 479..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2300..2346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2391..2514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2733..2760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2780..2967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2994..3014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3036..3059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3350..3378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3464..3527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3701..3723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3771..3825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2053..2072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2300..2332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2421..2439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2443..2505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2733..2748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2838..2867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2908..2933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2998..3012
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3041..3059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3468..3511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3771..3788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3806..3825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4215
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4250 AA; 468426 MW; 893B31CF38B08C68 CRC64;
MSSVPELAGL SLKEFEREKM EKYEDCNDEQ LLLELQQIKT WNIGKCELYH WVDLLDRFDG
ILADAGQTVE NMAWMLMCDG PQKEHLKLLL LAVLNFTALL IEYSFSRHLY SSIEHLTTLL
ASSDMQVVLA VLNLLYVFSK RSNYITRLGS DKRTPLLSRL QHLAESWGGK ENGFGLAECC
RDLHMLKYPP SATTLHFEFY ADPGAEVKVE KRTPSNTLHY IHIEQLDKIS ESPSEIMESL
TKMYSIPKDK QMLLFTHIRL AHGFSNHKKR LQAVQARLHA ISILVYSNAL QESANSILYN
GLIEELVDVL QITDKQLMDI KAASLRTLTS IVHLERTPKL SSIIDCTGTA SYHGFLPVLV
RNCIQAMIDP SMDPYPHQFA TALFSFLYHL ASYDAGGEAL VSCGMMEALL KVIKFLGDEQ
DQITFVTRAV RVVDLITNLD MAAFQSHSGL SIFIYRLEHE VDLCRKECPF VIKPKIQRPS
TAHEGEEMET DTDVAMESSP GPSTASVDPR PDVETRSRAP SISGVQCIPQ RAALLKSMLN
FLKKAIQDPA FSDGIRHVMD GSLPTSLKHI ISNAEYYGPS LFLLATEVVT VFVFQEPSLL
SSLQDNGLTD VMLHALLIKD VPATREVLGS LPNVFSALCL NARGLQSFVQ CQPFERLFKV
LLSPDYLPAM RRRRSSDPLG DTASNLGSAV DELMRHQPTL KTDATTAIIK LLEEICNLGR
DPKYICQKPS IQKADGTSTA PPQRANHAAE EASSEDEEEE EVQAMQSFNP PAQSDTDSNQ
QVVGTEERVP IPLMDYILNV MKFVESILSN NTTDDHCQEF VNQKGLLPLV TILGLPNLPI
DFPTSAACQA VAGVCKSILT LSHEPKVLQE GLLQLDSILS SLEPLHRPIE APGGSVLLRE
LACAGNVADA TLSAQATPLL HSLTAAHAYI MMFVHTCRVG QSEIRAISVN QWGSQLGLSV
LSKLSQLYCS LVWESTVLLS LCTPNSLPSG CEFGQADMQK LVPKEEKAAT TTATHGTKRT
EGESDGTTAS VEASAQGLLE GIGLDGDTLA PMETDEPSTS DAKGKSKITP AMAARIKQIK
PLLSASSRLG RALAELFGLL VKLCVGSPVR QRRSHHATST TTAPTPAARS TASALTKLLT
KGLSWQPPPY TPTPRFRLTF FICSVGFTSP MLFDERKYPY HLMLQKFLCS GGHNALFETF
NWALSMGGKV PVSEGLEHPD LPDGTGEFLD AWLMLVEKMV NPTTVLESPH SLPAKLPGGQ
THPQFSALRF LVVTQKAAFT CIKNLWNRKP LKVYGGRMAE SMLAILCHIL RGEPVIRERL
SKDKEGTRGE EESGQEESGS RRDPQVNQQQ LQQLMDMGFT REHAMEALLN TSTMEQATEY
LLTHPPPLMG GVVRDLSMSE EDQMMRAIAM SLGQDIPMDQ RAESPEEAAC RKEEEERKAR
EKQEEEEAKC LEKFQDAEPL EQEELHGFTD TMLPGCFHLL DELPDTVYRV CDLIMTAIKR
NGADYRDMIL KQVVNQVWEA ADVLIKAALP LTTSDTKTVT EWINQMITLP QASNLATRIL
LLTLLFEELK LPCARVVETS GILNVLIKLL EVVQPCLLAA KEQKEIHTPK WITPVLLLID
FYEKTSISSK RRAQMNKYLH LSNNNWRWFD DRSGRWCSYS ASNNSTIDSA WRSGETSVRF
TAGRRRYTVQ FTTMVQVNEE TGNRRPVMLS LLRAPRVNKI PKESHEPELD KTLDETKEAE
SKPAEEEKTS SECPLAPESP ALEKEVVVQK EVVVQKEVQL GDILIQGLTG EMVTVLIRAC
VSMLGVPVDP DTLHATLRLC LRLTRDHKYA LMFAELKSTR MILNLTQSSG FNGFTPLVTL
LLRHIIEDPC TLQHTMEKVV RSAATSGAGS TTSGVVSGSL GSREINYILR VLGPAACRNP
NIFTEVTNGC IRIALPAPRG SGTASDDEFE NLRVKGPNAV QLVKTTPVKP SPLPLIPDTI
KEVIYDMLNA LAAYHAPEEE KLDPKPGVTT QEVSQILQDM GDEVYQQYRT LTRQGSDFDA
QAGFAINAQV FATDSSSTET PQSGTPQGGA STPEESREGK KDKEGEKVSE ESKQKAKGSK
PLMPTSTILR LLAELVRSYV GIATLIANYN YAVGQSELIK EDCSVLAFVL DHLLPHTQNA
EDKDTPALAR LFLASLAAAG SGTDAQVALV NEVKAALSRA LAMAESTEKH ARLQAVMCII
STIMESCPST SSFYSSTTAK TQHNGMNNII RLFLKKGLVN DLARVPHSLD LSSPNMANTV
NAALKPLETL SRIVNQPSSL FGSKSASGKN KAEQDAQGVA QDASSNTQDP GEPGEAEVQE
EDHDAAQTEV ADGDIMDGEA ESDAVVIAGQ PQVLSTPEMQ VENELEDLID ELLERDGASG
NNAILVGRSG EDESQEDVLM DEAPSNLSQA STLQANREDS MNLLDAEDEE EHTQEEDSSG
SNEDEDESQD EEEEEEEDEE DDQEGEEGDE DDDDDGSEME LDEDYPDMNA SPLVRFERFD
REDDLIIEFD NMFSSATDIP PSPGNIPTTH PLMVRHADHS ALTLGSGSST TRITQGMSRS
QRTLRQLTAN TGHTIHVHYP GNRQPNPPLI LQRLLGPSAA ADILQLSSSL PLQSRGRARL
LVGNDDVHII ARSDDELLDD FFHDQSTATS QAGTLSSIPT ALTRWTEECK VLDAESMHDC
VCVVKVPVLN RLEFLRDEEL EERRDKRRQQ LLEGEAKSKE EKENKDQNPQ PKAPQTQTDP
CYSGTLLNSL FWQQLTLDQE LPGPASAPGP EAATQPLMPT EHKHLGSGQA GGETEAIQFS
LAPKITSLSP ERAEDSDALT AVSSQLEGSP MDTSSLASCN LEEGVGDGTT TSGAEAPEPA
PTTPGDAPQT GAETQGSGDE PGESPEESPQ QAEDSSPQGS SSESSSTRDS AVAISGADSR
GLLEEPLPST SSEEEDPLAG INLPEGVDPS FLAALPDDIR REVLQNQLGI RPPARVAPAA
TTPTPPPVVG NPNVTEVSPE FLAALPPAIQ EEVLAQQRAE QQRRELAQNS SSDTPMDPVT
FIQTLPSDLR RSVLEDMEDS VLAVMPPDIA AEAQALRREQ EARQRQLMHE RLFGHSSTSA
LSAILRSPAF TSRLSGNRAV QYTRLAVQRG GTFQMSGSSS HTRPSGSNVD SLLRLRGRLL
LDHEALSCLL VLLFVDEPKL NTSRLHRVLR NLCYHGQTRH WVIRSLLSIL QRSSESELCI
ETPKATASEE KGKKAAKVCP TGSHDSRPLD LLHKMESKSS SQLSWLSVSM DAALGCRTNI
FQIQRAAGRK HSGCGSTVHI HPQAAPVVCR HVLDTLIQLA KVFPSHFTQQ RTKETTCDSD
RERSNKQTCS PCPGQSTSSG ISTDFWDLLV KLDNMNVSRK GKNSVKSGPI NVGSEGESSL
YSLEASPLGQ LMNMLSHPVI RRSSLLTEKL LRLLSLISIA LPENKPPETV ANPSSSTGTP
STTTASSTSA ASTNTGVATP ATLTPTTAKS GKSPAKAGEG SSAGTMDSKM AASGLTENQL
QLSVEVLTSH SCSEEGLEDA ANVLLQLSRA RHLGYTLCKQ IGTLLAELRE YNLEQQRQAQ
CEILSPDGLP EEQPQATRLK GKMQSLRRAW SWASQASWGE TPLPSMSMLT SKTSTQKFFL
AFRYHPAPVP APRANKKGTK ARMRRRFAAC GLHVFVPLLL PPGSEGSQQS EKEKEERPPD
LPLLSEQLSL DELWDMLGEC LKELEESHDQ HAVLVLQPAV EAFFLVHATE RESKPPVRDT
RESQLAHIKD EPPPLSPAPL TPATPSSLDP FFSREPSSMH ISSSLPPDTQ KFLRFAETHR
TVLNQILRQS TTHLADGPFA VLVDYIRVLD FDVKRKYFRQ ELERLDEGLR KEDMAVHVRR
DHVFEDSYRE LHRKSPEEMK NRLYIVFEGE EGQDAGGLLR EWYMIISREM FNPMYALFRT
SPGDRVTYTI NPSSHCNPNH LSYFKFVGRI VAKAVYDNRL LECYFTRSFY KHILGKSVRY
TDMESEDYHF YQGLVYLLEN DVSTLGYDLT FSTEVQEFGV CEVRDLKPNG ANILVTEENK
KEYVHLVCQM RMTGAIRKQL AAFLEGFLWG FPKPSFPSSG QGLELSLSGP TFQMTSVQPR
GIHKYQSNSI QIQWFWRALR SFDQADRAKF LQFVTGTSKV PLRNFAARRG MNGIQKFQIH
RDDRSTDRLP SAHTCFNQLD LPGFTKLPPH AAKPSQGVGA HIKEATVGAW
//
