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Database: UniProt
Entry: A0A0A2J7V3_PENEN
LinkDB: A0A0A2J7V3_PENEN
Original site: A0A0A2J7V3_PENEN 
ID   A0A0A2J7V3_PENEN        Unreviewed;       376 AA.
AC   A0A0A2J7V3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=PEX2_015680 {ECO:0000313|EMBL:KGO61663.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO61663.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO61663.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO61663.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(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=2.3.2.27; 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}.
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:KGO61663.1}.
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DR   EMBL; JQFZ01000029; KGO61663.1; -; Genomic_DNA.
DR   RefSeq; XP_016602361.1; XM_016738844.1.
DR   AlphaFoldDB; A0A0A2J7V3; -.
DR   STRING; 27334.A0A0A2J7V3; -.
DR   GeneID; 27674263; -.
DR   HOGENOM; CLU_041707_2_0_1; -.
DR   OrthoDB; 38742at2759; -.
DR   PhylomeDB; A0A0A2J7V3; -.
DR   Proteomes; UP000030143; 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; PF13923; zf-C3HC4_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   Reference proteome {ECO:0000313|Proteomes:UP000030143};
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          325..363
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   376 AA;  42152 MW;  693E2B95123087A1 CRC64;
     MADDDSHLSL STPNSALGSS TSHFYPFATS PDIIRSHEKD AYLTGSLIQQ SQGIVRALRG
     ARYAHTHSDA IKHLTELLYF TLTTAIGNRT LGEEYCDLVQ LEDDTLQLPS IGRRVGYILS
     SILVPWTLQR LLPALRQRIR NKLERNIARQ QSRAVQQAGL LNKPQFSTTP TKRPLFTKLR
     IQQYILEHLD SITSLSPIYA LSIATFYFTG SYYHLSKRLW SLRYVFTKKI DDNEQRIGYE
     VLGVLLVLQI AVQGFLHARK IGASLNEDES QSADAGQSPG QGGAVLASIQ NPSTIPLLPA
     SVPLYDLEED PGAVSWIPEG QQRKCTLCLE MFKDPSVTTC GHVFCWICVR DWVREKPECP
     LCRQEVLLSK VLPLRG
//
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