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Database: UniProt
Entry: A0A1A0HJ75_9ASCO
LinkDB: A0A1A0HJ75_9ASCO
Original site: A0A1A0HJ75_9ASCO 
ID   A0A1A0HJ75_9ASCO        Unreviewed;       326 AA.
AC   A0A1A0HJ75;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=METBIDRAFT_36392 {ECO:0000313|EMBL:OBA24051.1};
OS   Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX   NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA24051.1, ECO:0000313|Proteomes:UP000092555};
RN   [1] {ECO:0000313|EMBL:OBA24051.1, ECO:0000313|Proteomes:UP000092555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA24051.1,
RC   ECO:0000313|Proteomes:UP000092555};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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:OBA24051.1}.
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DR   EMBL; LXTC01000001; OBA24051.1; -; Genomic_DNA.
DR   RefSeq; XP_018714532.1; XM_018856734.1.
DR   AlphaFoldDB; A0A1A0HJ75; -.
DR   STRING; 869754.A0A1A0HJ75; -.
DR   GeneID; 30029710; -.
DR   OrthoDB; 38671at2759; -.
DR   Proteomes; UP000092555; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16489; mRING-CH-C4HC2H_ZNRF; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46661; E3 UBIQUITIN-PROTEIN LIGASE ZNRF1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR46661:SF4; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092555};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          7..80
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          280..322
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          119..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  35594 MW;  7AFB9764F22ED9CC CRC64;
     MPVWKADATA SKCYLCKARF TLFNRRHHCR KCGQLVCATC SSKQVRYFAN SYVLNSQNTP
     EKARSHVYYR TCDVCVDEIH MMRSALSPVP ATETASVLQG HRDEPPAAVG PSADVHMIPG
     ATSAANPLKT APNRAQHASS DPPEFTGSNE PHDADSDADL CPVCGVDLGK QFLEESLGGP
     LASSAAYETY KEAHVSRCLV TYDFASNHLR LSSPPDGLHA RNRMLVYNMP PIPEPSYETI
     SDGSPNAGAV AAKTDGEIPG LVRSTATFSG TEKDDMDAEC VICLEDLCPG DKVGRLECLC
     VFHYKCIKDW FNKKSYAECP VHYLHS
//
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