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Database: UniProt
Entry: W6YSA5_COCMI
LinkDB: W6YSA5_COCMI
Original site: W6YSA5_COCMI 
ID   W6YSA5_COCMI            Unreviewed;       385 AA.
AC   W6YSA5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=Peroxin-10 {ECO:0000256|ARBA:ARBA00041230};
GN   ORFNames=COCMIDRAFT_41169 {ECO:0000313|EMBL:EUC40510.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC40510.1};
RN   [1] {ECO:0000313|EMBL:EUC40510.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC40510.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel,
CC       composed of PEX2, PEX10 and PEX12. {ECO:0000256|ARBA:ARBA00034505}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Peroxisome
CC       membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004585}.
CC   -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family.
CC       {ECO:0000256|ARBA:ARBA00008704}.
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DR   EMBL; KI964159; EUC40510.1; -; Genomic_DNA.
DR   RefSeq; XP_007692969.1; XM_007694779.1.
DR   AlphaFoldDB; W6YSA5; -.
DR   STRING; 930090.W6YSA5; -.
DR   GeneID; 19124010; -.
DR   KEGG; bor:COCMIDRAFT_41169; -.
DR   eggNOG; KOG0317; Eukaryota.
DR   HOGENOM; CLU_041707_2_0_1; -.
DR   OrthoDB; 38742at2759; -.
DR   Proteomes; UP000054032; Unassembled WGS sequence.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IEA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR   CDD; cd16527; RING-HC_PEX10; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR025654; PEX2/10.
DR   InterPro; IPR006845; Pex_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23350; PEROXISOME ASSEMBLY PROTEIN 10; 1.
DR   PANTHER; PTHR23350:SF0; PEROXISOME BIOGENESIS FACTOR 10; 1.
DR   Pfam; PF04757; Pex2_Pex12; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Peroxisome biogenesis {ECO:0000256|ARBA:ARBA00022593};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          334..372
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   385 AA;  42341 MW;  DFB528C5CC2120C7 CRC64;
     MAPSPPFAYP FAASPDIIRS HQKDAYFSGV LLEHLSSLVR KLYGARTAHT YLSETRVIGE
     LLYLGLTTLI GNRTLGEEYT DIVQVESETG RLPALGRRAG YIVACILGPY VLGRALPAFR
     RRIRAKLEAN LRWYARQQAR AQMVAQEKGE KVQIRRPLGM RVQNYILQNL DTITSPSPVY
     AVSLATFYFS GSYYHLSKRL WGLRYIFTRQ VAEGDNRAGY EVLGVLLVLQ MAVQAYLHLH
     NTVTASSTAA AAAGGSGHPH GTSVIVGGGA EVSLDPNAYS ANNALLFDAA TPAVPTAAAS
     DVQKWTHTPP TDKPRYELGD EETMEWIGGG NRKCTLCLEE MKDPSVTTCG HVFCWTCIGD
     WAREKPECPL CRQACLVQHV LPLRG
//
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