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Database: UniProt
Entry: A0A067C940_SAPPC
LinkDB: A0A067C940_SAPPC
Original site: A0A067C940_SAPPC 
ID   A0A067C940_SAPPC        Unreviewed;       325 AA.
AC   A0A067C940;
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=RING-type E3 ubiquitin transferase (cysteine targeting) {ECO:0000256|ARBA:ARBA00034523};
DE            EC=2.3.2.36 {ECO:0000256|ARBA:ARBA00034523};
DE   AltName: Full=Peroxin-2 {ECO:0000256|ARBA:ARBA00032511};
GN   ORFNames=SPRG_07518 {ECO:0000313|EMBL:KDO27269.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO27269.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO27269.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO27269.1,
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=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.; EC=2.3.2.36;
CC         Evidence={ECO:0000256|ARBA:ARBA00034438};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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; KK583218; KDO27269.1; -; Genomic_DNA.
DR   RefSeq; XP_012202045.1; XM_012346655.1.
DR   AlphaFoldDB; A0A067C940; -.
DR   STRING; 695850.A0A067C940; -.
DR   EnsemblProtists; KDO27269; KDO27269; SPRG_07518.
DR   GeneID; 24129789; -.
DR   KEGG; spar:SPRG_07518; -.
DR   VEuPathDB; FungiDB:SPRG_07518; -.
DR   OMA; YLICTVG; -.
DR   OrthoDB; 64567at2759; -.
DR   Proteomes; UP000030745; 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:0016558; P:protein import into peroxisome matrix; IEA:InterPro.
DR   CDD; cd16526; RING-HC_PEX2; 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; IPR045859; RING-HC_PEX2.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR48178; PEROXISOME BIOGENESIS FACTOR 2; 1.
DR   PANTHER; PTHR48178:SF1; PEROXISOME BIOGENESIS FACTOR 2; 1.
DR   Pfam; PF04757; Pex2_Pex12; 1.
DR   Pfam; PF00097; zf-C3HC4; 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   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030745};
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          263..303
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   325 AA;  36558 MW;  B9B6EE1B7DF23686 CRC64;
     MWADGSVAEL ARLRGVLARA PSLAPTHASA NLRVNKWDSL VLDSEILALM KHPIKSMFAL
     FQPGLMEKYQ PEIDGVTYAM LFALSVGMHQ PTPGMKLQNL QFAKECLTWK KTLPLFLLSV
     GLPYAWNRIH RALLSYRWRE DRSTEAEDQY QHFLNLVHRV STVASILKLA NHLAFWKQGE
     YRSVPERLVG MKLAPLTRSV APRAITFEYM NRQLVWDGFV EFCYFALPLI NWQRAGLWLK
     QRGKQLLGPD VNSDDHASGV GPCALCNATP AKTPYITTCG HQYCYYCLQT AVATDPTFVC
     ATCGDVFDAS ERLSAAHVSP ALLHM
//
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