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Database: UniProt
Entry: A0A067C7M9_SAPPC
LinkDB: A0A067C7M9_SAPPC
Original site: A0A067C7M9_SAPPC 
ID   A0A067C7M9_SAPPC        Unreviewed;       323 AA.
AC   A0A067C7M9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=SPRG_11566 {ECO:0000313|EMBL:KDO22807.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO22807.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO22807.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO22807.1,
RC   ECO:0000313|Proteomes:UP000030745};
RX   PubMed=23785293;
RA   Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA   van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA   Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA   Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA   Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA   Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA   Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA   Russ C., Tyler B.M., van West P.;
RT   "Distinctive expansion of potential virulence genes in the genome of the
RT   oomycete fish pathogen Saprolegnia parasitica.";
RL   PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583262; KDO22807.1; -; Genomic_DNA.
DR   RefSeq; XP_012206478.1; XM_012351088.1.
DR   AlphaFoldDB; A0A067C7M9; -.
DR   STRING; 695850.A0A067C7M9; -.
DR   EnsemblProtists; KDO22807; KDO22807; SPRG_11566.
DR   GeneID; 24133592; -.
DR   KEGG; spar:SPRG_11566; -.
DR   VEuPathDB; FungiDB:SPRG_11566; -.
DR   OMA; SSEDIQC; -.
DR   OrthoDB; 5478214at2759; -.
DR   Proteomes; UP000030745; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF446; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 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:UP000030745};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1..323
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        290
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   323 AA;  35433 MW;  18396B65B7C6A88F CRC64;
     MLGESGVDAG GLQREWYSLV LAAVLAPSAG LFCINHKDDG AYMIDHNTSL EPTNLTLFRA
     VGRLLARAML DGQVLPQPLC VPLLKALVGA PLSVADIAYL DPTTSASLHY IATASSVDDL
     CLDFTVARGK TDLVPLLPNG QDIPVTLSNR AAYVDCMVQY LLFDRVQQPL TSLLHGFNEV
     MPADLVLPFD YQELGLLVAG SAADLDVDDW KRHTKMALAH AATTSATWFW ELLRDMTPTQ
     RRHLLQFTTG SSRVPIQGFQ GLTSFDGRLC PFTVEAIPFT RGVFPRAHAC FNRIDLPLYP
     TKELMRDGLH ALAQLEHAEF TIV
//
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