ID   A0A1V9ZN74_9STRA        Unreviewed;       855 AA.
AC   A0A1V9ZN74;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=ACHHYP_06936 {ECO:0000313|EMBL:OQR99391.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR99391.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR99391.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR99391.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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:OQR99391.1}.
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; JNBR01000070; OQR99391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9ZN74; -.
DR   STRING; 1202772.A0A1V9ZN74; -.
DR   OrthoDB; 5478214at2759; -.
DR   Proteomes; UP000243579; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR001876; Znf_RanBP2.
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.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:OQR99391.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        684..705
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          315..673
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   DOMAIN          744..773
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          787..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        640
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   855 AA;  95466 MW;  4A8E2F1A8CE160A9 CRC64;
     MLSSVTVVFI VIAVVIVGVC IANCIYMKRH PATGELGEGL LNRNFLDFMP GLNRRDVQEQ
     TLEMERWECS VCAFLNIATK PMCKYRLIEM YSESVPSESP SLSVSHRASK TFQRQTSKSL
     QRLSSFFHKA ILPEDLNPRQ RSARMRKQWT RQMDAKGRVV WARHFLDTEE FPASFVIQMG
     PIHTGGNYTD DSTSVTVIIH DSTTLASADG YSPPTDFTKT IAWVPIEAVH ADAAVTGARL
     ALSMWTSLLA ISRLPFSLKY AWFLHQIEDL IVPYGELCAL FLIASAHPSP ISHVQTKVDR
     ARVFEEALEN LMLIKEQGLC AIIRYTFLGE SGLDAGAIQR EWYMLVAQAL LHEDSGLFAI
     SNREDNSYFI NPNSAHATRT LFVLASRDTS FTRVHRNVAL PHLDLYRAAG RFIGRALLDG
     QVLPIHLNPV LFKALLGVPM TLDDIEALDR TTYKSLQYLV QNDKVDELSL TFSVTQPLGD
     GYVEVDLVPH GSDIAVTDAN KHEYIELMVR HLVFGRVEPQ LLAIIKGLYD VIPSELLTAF
     DHKELELILC GLNEIDVADW QANTVTSSNL EKAAVLEWFW DVVAGLSVHD QAKLLQYATG
     ASRVPVQGFK GLTSYDGKIC YFTLKGIVYA PGMYPVAHAC YNRIDLPLYP ERALLEEAIA
     TLLLSDPTGF NIEYGASDGG NRTLWFFGLC ASVVLFVLFL GIVNYCYSKR YGSPTPPGPA
     VNNQNFHEFM PGIKRGDVEE LLAKVDRWEC SICAFQSVVQ KQSCSLCGTP KDARLVEVST
     EQVVPRKTRS SSVMRRSSMA GPYRHRSKSG LPRPSMRRLS LLFQKAILPE DLNARQRSAR
     CVSAAHHFGT HCSAL
//