ID F0ZHQ8_DICPU Unreviewed; 431 AA.
AC F0ZHQ8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 Name=PEX2 {ECO:0000313|EMBL:EGC36519.1};
GN ORFNames=DICPUDRAFT_150983 {ECO:0000313|EMBL:EGC36519.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC36519.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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; GL871024; EGC36519.1; -; Genomic_DNA.
DR RefSeq; XP_003286964.1; XM_003286916.1.
DR AlphaFoldDB; F0ZHQ8; -.
DR STRING; 5786.F0ZHQ8; -.
DR EnsemblProtists; EGC36519; EGC36519; DICPUDRAFT_150983.
DR GeneID; 10500456; -.
DR KEGG; dpp:DICPUDRAFT_150983; -.
DR eggNOG; KOG2879; Eukaryota.
DR InParanoid; F0ZHQ8; -.
DR OMA; YLICTVG; -.
DR OrthoDB; 64567at2759; -.
DR Proteomes; UP000001064; 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, ECO:0000256|SAM:Phobius};
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:UP000001064};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; 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 TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 376..417
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 49816 MW; 9EF80491F8743740 CRC64;
MTENVTINNN NTNNTNNNIN TNNNNTITNT VNNNINNVNS NINNNNNNGS SNNNNNINNK
EKIALSNSNV SRVESSSSVS YEHSDWNKVY NSEREKLLNI NKEIQSIKRP STTIVRVSQL
DSARLDEEIL DLLRSQFMKI FSFFKPNFIQ RFQPEINAIL KSIIFKLSIF NLGTTYGNQL
QNLTFRNEKA FDPNRGSDQL TKLTLRQKWL SGLINIGGEW LWTRLNRYSI KEGWSERPST
DFRKRLWNLM NFLESSYKAL SILNFLAFLY DGKYVTLVNR VLHMRLVYAH PTLSRNISFE
YMNRLLVWHG FTEFILFIMP LINIDRIKSF LYRVLIKNSF GSNTSSSSAS SSSSSLQQLQ
KQQLLIQQQQ MVLSKCPICM NDPISIPYTS DCGHLFCYYC IKTSCMIDSS FTCPRCNTLI
SNIKRFSITN N
//
