ID A0A0V0QG42_PSEPJ Unreviewed; 592 AA.
AC A0A0V0QG42;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PPERSA_00788 {ECO:0000313|EMBL:KRX01040.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX01040.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX01040.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX01040.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX01040.1}.
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DR EMBL; LDAU01000179; KRX01040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QG42; -.
DR EnsemblProtists; KRX01040; KRX01040; PPERSA_00788.
DR InParanoid; A0A0V0QG42; -.
DR OMA; HWILEND; -.
DR OrthoDB; 5471864at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
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:UP000054937};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 266..592
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 559
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 592 AA; 69381 MW; 70303F6BD53AA36A CRC64;
MEELMIVFKR SIKDIVNIWK DLQKKYQQIV NKLLEKQELL KKCLEFLKQT LEDYEYCWQT
QNEIPYAYTS FDIGFKQILH LYEFLYEKDL KRQKDNQQVK EGLNNQIDQF SKDENSEHQL
SEVLVKPELS KMVSKETHKQ GILLEGSKSS IDKDILSDQF DQDFCFSDLI DIIKKQFLLF
IYFSIENDRF NNLSKWENLC QMANKDNKSF QKLDIKSKLS QISAQAKFEA KRRLPKVQQN
KNFNIYLNID REYIWSDTIK EVSKKNGPQL ALSELNVKFK KEEGIDGGGL TREWLTLTLR
QIFNPDFGLF TLSSNQVTLR PSPLSYVIPS HLKYFEYAGR LVAKGLMEQI EVEVDFTVSF
LKHILKKNLI IQDLEDIDPE QAKNLHWILE NDINELDLTF SYDINKFGTI ETIELVENGS
NVIVTNDNKQ QFVKLMAHYK MTDEIKEQIQ KFIQGFYDVI PYKAIEHFDE KDFGMILSGI
KQIDINEMKQ FIGLQGYTQN SDQIEWLFDF LSQQDEQIKA LFLFYATGSF KVPYGGYSSL
GLEIVKVSNT KKLPVAHTCS KQIDLPPYES RQILEQKLLT AIQEGHKGFY IG
//
