ID A0A1E3QJ67_9ASCO Unreviewed; 3222 AA.
AC A0A1E3QJ67;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=BABINDRAFT_163505 {ECO:0000313|EMBL:ODQ77494.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ77494.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KV454440; ODQ77494.1; -; Genomic_DNA.
DR RefSeq; XP_018982822.1; XM_019129949.1.
DR STRING; 984486.A0A1E3QJ67; -.
DR GeneID; 30147802; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000094336; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 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 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; PF14377; UBM; 2.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000094336};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 2886..3222
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 216..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2256..2284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1973..2025
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2048..2089
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2097..2115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2256..2280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3189
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3222 AA; 359930 MW; DD3BBCEC79854999 CRC64;
MIITKRDHAK LLERALPIKG LIEDLVSCDL ALLPSKLNAL TAWEKPKGDL CHWIPLLNRF
DSILEDLVKK YALDAEHVPL RELDRTDQTL STACLAYTAL LLRHCSNKHI YASTHHLYNL
VGSCSVPLRL ATLHVLVLVA ESACVTHSSK NAASAEVKAR ILALARFFPP ATHNHSGDDH
IGLYDCISNK KKIPSKWRAL DFEYFKTTAK TVPLFPKDQP LKHDVKSKKD APKDAKEDIA
GKHGNSLSDK TGDTPAGVEV SRKASKKKKK TQTHTIYTEG LAHFTLPQDE VRKLSLAQIY
DRAVSVPPAA WFQLGLKAPV AKAFNNQSFE ALQLRENLVQ IRCLAIAYIV CVNDTSLVTS
QLFEFDPYIF SYLVDLVSPA NSVSPPVYAA AVKALSCIAF RRTWSSDIVR ALSANVSHGV
LFQMLRVIYK AAKDEDPALD DAASAELLVE MLGRILETKS LAVSLTSAGL MTHLLDFLAL
RTTKRRISNA SLHLLDALIL SYPEMLDTFI DNEGFSRLVD AIVYEVNFAV ANPEFAGGKP
QGCIVHYEVS FRQAQYFKTL LKFVLHLLQT DTSDRMRNLF DSALLVALNE IVLRPQMFGP
TIITGTLNIL ATIIHNEPSS YAILQEAGCL DRVLANYATL FGPSSGLFTA MVEIVEAICL
NTVGLKKVID MGILPTFFQS FLVSDYSKDH VRAIDTSNTE QLGSLIEELG RHYPELRPII
VQEVIKLAAA VPRAASGLLP GTELYTSPQG AFYHSISEDV LNLEKGAEDL KEWEITEGSF
MVDRATLFLS SLVQESGMAR ALMEKMPFAR WLDFLAVANA PYDFVFSDSI LSITGVLKFL
DEEDRKYGLG DGSIIDALLA WLESVDAFLQ FDHAARGTSA FLAMARDGQI SAASSLLQNL
AHLSALLVVF MDIYCNPYNL FPVRITQLSQ IFAGAKGQRL MELLGCLFQS CALEEAFLRC
SMPDEATTLT SPPKNPDVPP LQFSHGELSL TPVKNDKNSA KYKNSVQIRF LTNRIQVAVA
ACFSAMANLP MAKKQEAQVL KASLVATSNH LATTLIRLMD VTVDDPAAQG SYVAVVVNLL
CFVLTGKSRT GQEHLQTVLA ICFMQQGGFM RSRAVLVHHW QLLYTLDTER LRAAQNLKYL
PNTVECATLV IISQLLNLFT KVLNGDQIEK IPAVNHLYNN GIINAQEVSA NFVVQAKLLL
MGFLDTVMDG KYPFDEDIIT RLTPLAIHRF LEINRFVFTN NGELHVSHAG ALAQLDSARS
SSKVAYLRSL GMPEAVAVDF VKEHDVYDVP AHQPDDIDDD EWDGIVEKCL QKGYVKPEAH
LVSPQYREYR FLNELDDLRA KNRGRFLERW LLIPQFSPKS VFKVHEVVDG AFEKDPEDIP
HVVLEYLYSF DMADVGNKEK LASMLTLLSL FMSDSKVFYR ESTLELVDEF MGFFEDVLQP
EHLNQPWFSK ALLVFERILS YSDIPVAEEL AIEGKLRFPV VPGHPSISRE TYEGTFMRVL
ALDVEISDID TAISLTRILI LFGRRTENTS KMIEAGVVKR IVTSVAVFNA SDKFFILQES
LIALFRRCFE SPEVIRRTME AELRRVLATK GRFSPGTHKD INVVVKETSA MVVRAPEVYV
EVGSKEMRIH DCTKPLMTSL VELAVPPILE GPSAKPLDDP TGIMDLLLSE LMAAKKHNWF
EDPEPSEPFT SEQVAAKEAD QKAKDALSQF KGGITKNPHC AYACFLLQAM VELLASYKLA
KIEFVSYSKK HKAFGVAKAS STSMNFLLHQ VLPTHSLADG KADASERPKM VSRLAKMAIV
AFVSSPLGED GKKEDPDMQL IRKYTVESIA RVLQEAFVSS DVAKKRFGMI VDLVRLSESL
VLKEYRECLG KGLDKGSTEL DCYYIGRLML EKALPAQFSA VISDVDFNFP GAKEVINACI
GPLRTLCKLK IQFQDLFRSA GGEGEGEEEE ALSDDDKEDT PDLFKNSTLG MYDVEDSEEE
EDYDEMDYDE REPLEVVYSE DEVTDEELEE DSDDVDMEEP EAWSGEDVSM SEPDEITERG
FVEIETEDSS SEMSEESLQS EISFDDDFDD DEISVGSDDA LDEWMDNYAS DGEETGPTAF
LEDDDDEEED ELESDIDSAA GDYAIVESGI EHFANGGVGN RRGSRSGMIE DLMSAFGELS
RANGGSIFRE GGGINVPGSD AISILDRLFD KKKKDKLSLA PNFVIKSTLE SWKYVAAMFS
LSHESYAAAP AILNRIFDVS LELSVAKRAA EEQARAARTS KLQVKREERE RQRRESETAR
RNAPVVTPAV EPILMLIGGR EVDISGTDID PDFFEALPED MREEVFTQHI RERRAEATVA
GGDTREIDPQ FLDALPPQIR EEILQQEAMA NRFEETEELD NDEAIEGEEE EEEETDVVVP
KLKQRLFFTP LLDRAGVASL TKLMFLPQTF KERGAMHALM EYLCSSKQTR TEILGLLLSV
LEGTGGQKSL EKCYAQLCSR VKKGREAGEF PVGATPLVVA TQTLEALQYL LEADPHTRFY
FLVEHEAVRK GKKKFKDTID KAKKYPVNAL LAFVEKKLVQ NEPILMDLVS RVVQVATRPL
ALKGKTEMDK NNDGNATLGS MADHVPAALH ALAPLLSEAS LTHLVSILIA DECSSRTFQQ
VLGAMQNLSL VSNALTVFPR ELSLQASRLG GLIVGDLRDL ATDITSTPAA EELCGITINK
FVPPSSDQAK LLRVLTALDY LFGGTQTVEQ LSLLYTKIAL GPLWDALSSC LRVLEERAAL
TNVATVLLPL IEALMVVCKH SRVKDLQTKD VYTVRKDFLK EPIESLFFAF TDEHKKILNL
MVRVNPKLMS GPFAMLVKNP RVLEFDNKRN YFDRQLHKDG ERPTLNVSVG RDLVFLDSYR
ALFFKSKEEM KNAKLDIKFK GEDGVDAGGV TREWYLVLSR QMFNPDYALF APVASDKTTF
HPNRTSWVNP EHLSFFKFIG RIIGKAIYDG FFLDCHFSRA VYKQILGCPL SLKDMETLDL
EYFKSLIWML ENDITDIIIE DFSVETDDYG EHKVIDLIPD GRNVPVTQEN KQDYVRRVVA
YRLQTSIAEQ MDNFLQGFHD IIPRDLIAIF DEQELELLIS GLPDIDVDDW KNNSNYVNYS
GSSPQIQWFW RAVRSFDVEE RAKLLQFATG TSKVPLNGFK ELSGVNGIAK FSIHRDYGKT
DRLPSSHTCF NQIDLPEYDS YEQLRGSLLL ATTEGHEGFG LA
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