ID J7S4I1_NAUDC Unreviewed; 846 AA.
AC J7S4I1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=NDAI0G04830 {ECO:0000313|EMBL:CCK73466.1};
GN OrderedLocusNames=NDAI_0G04830 {ECO:0000313|EMBL:CCK73466.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCK73466.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCK73466.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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};
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DR EMBL; HE580273; CCK73466.1; -; Genomic_DNA.
DR RefSeq; XP_003980142.1; XM_003980093.1.
DR AlphaFoldDB; J7S4I1; -.
DR STRING; 1071378.J7S4I1; -.
DR GeneID; 13926944; -.
DR KEGG; ndi:NDAI_0G04830; -.
DR eggNOG; KOG0941; Eukaryota.
DR HOGENOM; CLU_002173_5_1_1; -.
DR OMA; YGNDWHI; -.
DR OrthoDB; 5471864at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; 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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 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:UP000000689};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 494..846
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 814
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 846 AA; 98683 MW; 018DE22CA96DE10E CRC64;
MGIFSRKNST KRDTAKAKEN ARIEIISRKA SLKRPSVEGK TVSRVGSLKQ NAEKRQCPCC
NSWIQVPPKI PKFRCSICQV TTYLKMDSSQ QSSTTSVKEN IVCNKFVLEK VINGCEKEVK
ERKLTSREDF AKVYDSVTIY LTNCFQDATI LNQSFCPENN LDTIDYLSLS EFYEIVMNLP
TRRPFYRLLC VSNELLRRSN IAMTSFKWIL IILNNPIVRQ ALTGRIPKKF ESVKIRTIAY
DLGKKCIGFL SNMPYKENSD KLIRYLKSLS VESTLQYIEL LNIYLTFQLH RIVRHETKTA
LEKYRPFYPG IGNGNTEAWI HDKYALGTNN DKTVVLRDFR FKPFQYEDDW HIKTVTELMR
KFYQVNVERC NQQGFSNSKK LNVSEFYNTM LDVIDYRKDF DIWRGYTGND QLSKFINQQS
WNTSSFTFCK YPFLLSLGLK ISIMEYEFKR IMEYEAENAF LTSLDKGKMV NVYFKIRVRR
NRITNDSLQC IQQHQGDLLK SLRIEFIDEP GIDAGGLRKE WFLLLTKSLF NPMNGLFVSV
EESNLSWIAI HDIQTLNKSS TFKNELFFLF GVVVALAIFN STILDLQFPR TFYKKLCNEP
LTFDDYREIY PVTAQNLMKM LQYENDDFEE VFGLTFETTY KDPLKYALDN EKSKGDGMVS
VELCKNGSKM KVTQANKQKF INLWVNFYLN ESIINQISQF RSGFDRVFAR TKSISLLNSE
ELERLLCGDE TQQSYDFKML RSVTKYSGGF SDDSRVVAWF WEIVEGWNYK LQRKLLSFIT
GSDRIPATGI STLNFKISRL GSKDKNNLPL SHTCFNELCL WEYSSRGKLE KKLLYAITES
EGFGFR
//