ID   A5DGV7_PICGU            Unreviewed;       974 AA.
AC   A5DGV7;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=PGUG_02508 {ECO:0000313|EMBL:EDK38410.2};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK38410.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK38410.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH408157; EDK38410.2; -; Genomic_DNA.
DR   RefSeq; XP_001484779.1; XM_001484729.1.
DR   AlphaFoldDB; A5DGV7; -.
DR   STRING; 294746.A5DGV7; -.
DR   GeneID; 5127301; -.
DR   KEGG; pgu:PGUG_02508; -.
DR   eggNOG; KOG0942; Eukaryota.
DR   HOGENOM; CLU_002173_2_3_1; -.
DR   InParanoid; A5DGV7; -.
DR   OMA; DCFELQM; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
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; IPR044611; E3A/B/C-like.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          626..974
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        942
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   974 AA;  112429 MW;  7A5C520ED7E6BCE6 CRC64;
     MLNFTGQTKK RVVNLGNKQS SAVNFLEQTR LQRQAREEQR QRERAANILQ GYVKWYLYLS
     RIAETIDLHQ ESNDVVDEYS FSRYLASFSF VCRWKRSLPR ERIISNITDL ATVLKVHDDL
     LKTLNKFQVE RIANNIMLVF HKTGNDTVIT EEALKILLII LQQEVANECL FPNVISGLQR
     LIPTTLSQEK LDTITNIIFA INVRDSPQAF ISFLCGRNLH LRTSDFRKSI LYSTIPNNIS
     IIQSLEPAQK VQLLLNILTL TPITSRKQIG PSDYIIIGTV LSTISFALSD RVRDEDDSDS
     TQEHNIIGVD NESIKEIKLL YSSAFIENAI EFFTNSQNES SKFVLYIFSS LLFLIPPEKK
     KLCMMITITP GSYKWFFNQL CHHELYVNFK TILARKDYLD SQDLNSVFQA LSPASVADFW
     KMLYTFEELY SYWLIVSNDT ESFSDDKLNL ESIVDFMEFS KGLCLTFIFS NGPICDNFDK
     IKSISISLLN QLYSKNTRLQ FLDSRFWETK NFNDNIDSLI EIIAEGHERS TMNDDMSDEE
     GSQPIFGSRT KITNDSQARL EVLAKMPFII PFKSRVRVFQ RLIELDRERN APVSYFGPRT
     TLKADIRREF ILEDAFNNFN NIGQNFKNPL SVTFFNEYGQ EAGIDGGGIT KEFLTSVVQE
     GFLPGGQFDL FKETATNNQL YPNDEIFKKL RMNYNVPEQK LKLEYLRFLG AIVGKCLYEN
     VLIDVSFAPF FINKWSNVAH LMKSSINDLR SLDEELFSNL LKLNSMSDQE LVELDLNFMI
     EEQVSGKKFI YDLMPPNGRN TQVNHNNRLN YIHQVSNFKL NQSLHLQTKY FVEGLFEMIS
     AAWLTMFDPI ELQMLISGGE QDINIDDWKD NVEYGGYFDD DLTIVYFWEV VKEMSPQERF
     KLVKFVTSVS RAPLLGFQSL TPKFGIRNSG REIDRLPTAS TCVNLLKLPD YQDKELIRSK
     LLYAINMGAG FDLS
//