ID A0A1G4KAU1_9SACH Unreviewed; 3239 AA.
AC A0A1G4KAU1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=LAMI_0G10814G {ECO:0000313|EMBL:SCV01331.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV01331.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCV01331.1, ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCV01331.1};
RA Devillers H.;
RL Submitted (MAR-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; LT598469; SCV01331.1; -; Genomic_DNA.
DR STRING; 1230905.A0A1G4KAU1; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000191024; Chromosome g.
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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
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:UP000191024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 2903..3239
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1952..2019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2031..2096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2276..2301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2392..2419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1986..2006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2031..2049
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2276..2300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3206
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3239 AA; 368774 MW; B2F3655A964890DE CRC64;
MVTLTKLEKL RKDEQAKGFK PLMDELTQCS GEEFVEKLKG LIEWDRSKDD LYTWIPVLNR
IDAMLGKLVE NYSYKGSDPK KQPVRLTVMK AADEDVAVGL MGFTCRLLNN SSNRPLYSSL
DVMADLLNCP NYRIKLAATK VIATFGECQV ISRQKIDSKS AIGTPDVKRK ILDLALAIPS
SSADDSMNHF ALSDLFFDKK AFPSKWSRVA FSYYIESSKK THNASSSGRQ ANTSLRRFIL
GPDELKSMTL QQIFDKGMAE IPPDRWYDFS LQASVAKAFS DNTFDNLQLR IVIIQTKFNA
IAFTNIVYIP PQVSSKLFEV DPYAFNNLAD FLSLSEQKIP RDLRLDALFA LECISLKHIW
CSDIMRNLGG NMSHGLLFQI LRYISKVLRD DTNAEIDNEY NVRFSYLISN IADVKSLQES
LIGAGLISNL LEVISIRDCP HKRTLSSAAH LLEVVVDDAD AATEFITNNG FNVLIESLND
EVHYALDHPE MAKPPKYSTV YYSISFRQLT YIRSLLKLVL KLLKTDSGDR IRNLIDSPIL
QALNRILANR PTFGYTLVTY SLDVIQTVIN TEPTIYSVLV ESETIPYIID HFEEFLGPSG
ELLCLLPEVI SALSLNADGL KRVREKHLID CLFQITTTPE YAKLLSWDDN AFDLGSSIDE
LARHYPDLKP DIEAAFHKTI KALPKILKFD HPYVYKSSTG KGEFYLSKNE EVIDNEEGSK
EIESGEVQVA AAVADCFSAI FYGMTLENVS WAGLAEKVDI KELLSVVILE KPPYDYVGSQ
TLLNFSDILK MFDDERRNYA LPALLERLSQ SLESVREFLD FGFERSYVLS TPYDKLEETL
RELSIINVIL YIITDTYVNI ASLFPIRVLQ ILEFFEQHDF SLIRNLRLLF QRCALEEMFI
RDRLPPSVVA ETAVRPIGNT PPILIHAAKP TKDEAKDDKT SAKFKNTLQD RHLFIQIQSW
SSMLFRCFLR LTHARKMSIE SNDRALEIRV FETTVDEIIN MLDLRYLETH MGYFLVVFNF
VTFAFTFPNV TTSAGGTIQT IPALLFCQNG GFKIYFEAVK KLFDYLETLK SVEKLEKIEY
IKDSPDVLAV TSLINLLSFI NKCVQLDSME NIKNTSEYYP YDEIQYNITI SLMVSVKILS
LGLISEITEE YELFQNDERR LPYSVFKQLL SLLKNIYNNS FEDESYEAYQ LHWDLIPPSQ
RKVAMLQECG ISEDVARGYL EEEKDDLPIY ERPDVFSETE WEKYLELKRS GNWKTDLELL
DSQYKDNSNV DDLSKMRIEF YQGGGMLDRM LELLPLYPKL VNAISHTLLQ MLKEMHESPT
NVLENLLVMM KETDLESASS LASVIHLFGI LLNNKEIYEV AEAEIKEFVS YLTKSLRPEY
VNTAWFSKAL YVYEIIFAKS ESPKVEQLSG DWKECANSPF PSTFNAIDIS HQAKEEVFDV
LIRVNEISDF YSALAVSRIL ILYARNESFA QEVAKSGVLA TLLKVIGLHQ KSEKINYLES
SFLLLARRCF ENSDIVKSLI RHELNRAFTS RAIADNKEKS RDLAGLLSEK ASVVLREPNL
FINCLSETTR FENFLNPKKL DNLSVKRYPS ECDVEMQDAF ASSEEKVTLK NRTGIVHLLF
TQLMAAFKKD WANDPSSNEE LVDDLHKKDG QNVSRNPVCG YMIFLLKVLI ELVGSYKESK
FEFLTFNKRN LYAEAPKPRT TALNFILYQL LDTDDRNQEK ASAERREVIS KLARDLIVSF
ASSVQDERTQ RGDPKIVDPD MTFIRKFTIE SIGKAFREAT KTPKTLESNV GKLYGWFHLL
SSLLGNDVNY LHSVLDPNKV FVDRYQIGKL MIEMGIPCSI TDCIASLDLN YPFSKKLFNA
SIEPLNAINE VRSRFSALFK LENIDDEEEV DDESEKEENA DMFRNSALGM YDVDDIEEDD
DDDASLIGED EDIAFVEGDD DGLEVVFSED DLDGEQDSDD LGSDHSLGSE DVDDSDGEMD
YNIAGPIQVS LSSQESSFGS REVSDTDESS YFTDEEGPMN MIEIDEYGSD SAMDENFDDI
SDIDESDWES GLSELSGSDE DNSEGSIHEG VPPSDRWLAD ENDVDDESDG NGRGVSSFQW
VFAPDQQPFR VHDRSASARR GSHHHHLGRR SGFSMVSPSI SILNGGRRAQ SILLNPLGPS
GLEEVENGIV NQLNEVGIPG RSRTDATHLS DVLFGGEFFD EKTSAGIYLK STTARWNDIF
EMFYDSKIYV NNCLPTIFSR IFEPSSVLYI KKREEALQKQ SEQRFRREEE LKKQMDAKKR
KLEDMQNEPE IADSQHEETT QHEPIIVSIG GEDVDIAGTD IDPEFLNALP DEMRAEVFAQ
HVRERRAEAQ HHPLSSREID SDFLEAIPEN IREEILEQEA AESRFSRLVG ALDEREPEEG
ESDGEHDEVI EDGEQPKSKA SERCYFSPLV DRAGIAAIMR SVFIAQPYLA REAHHELFFR
LCSSKQNRND VVNYLLLILT EGITDTHSLE KVYNLISSKA VGPNKGGPPT RQLPIDCTPL
SVANQTIEIL QNLVETGNKL KFFFITEHEN LLVNRSSLKN KKDLFTKNMK WPINHLFGLL
DKKIITDEAV LLDFLTRTLQ ICTKPISTIA KSLQENAQRK FLLPEIEEKH LESIVSIIKY
DSCNTKVFQQ TLNVMLNLLV MANAQEKFTQ ELSHLAQPAV RILSDDVNTL SKKITDVENG
SEINYEIIQK FTVPSSEQAK LLKVLTATDY IHANKKHLTE IEVEKLMKLY DSMKLGNLWS
ALSNCLTQFE ERPNITSSAS ILLPLIESLM VVCKHSKVRD SKELLRYESK KSDFAQIAAE
NTFFAFTDLH KKILNQMIRS NPKLMNGPFA LLVRNPRILD FDNKRYYFVA RIKSGGQERP
KLSISVRRNE VFLDSYRALF FKSNDEIKSS KLEITFKGEA GVDAGGVTRE WYQVLSRQMF
NPDYALFLPV ASDKTTFHPN RTSGVNPEHL SFFKFIGMII GKAISDQCFL DCHFSREVYK
NILGKPVSLK DMESLDLDYY KSLIWILEND ITGIIEETFS VETDDYGEHK IIDLIPDGRD
IAVTEDCKQE YVQKIVEYKL HTSVKEQMDN FLLGFYAVIP KELIAIFDEQ ELELLISGLP
DIDVDDWKNN TVYVNYTATC KQISHFWRAV RSFDTEERAK LLQFVTGTSK VPLNGFRELS
GVNGISKFSI HRDYGSTERL PSSHTCFNQL DLPAYSSYET LRGSLLLAIN EGHEGFGIA
//
