ID A0A2V0NQA8_9CHLO Unreviewed; 498 AA.
AC A0A2V0NQA8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=Rsub_00434 {ECO:0000313|EMBL:GBF87723.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF87723.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF87723.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF87723.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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}.
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:GBF87723.1}.
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DR EMBL; BDRX01000002; GBF87723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0NQA8; -.
DR STRING; 307507.A0A2V0NQA8; -.
DR InParanoid; A0A2V0NQA8; -.
DR Proteomes; UP000247498; 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 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; 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:UP000247498};
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 433..474
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 52595 MW; 0906ADD0CC55735E CRC64;
MAAGSGAAAS APAPPGSGSG SGTDRVGGAA SAPAPRTAAP GAAADTTAEA WQLEYLQSLP
EQERLLSAAP PPWPLRVLRS TQLDALRLDA ELLSMLREQF ARVFAFFQPG RVADFEPELN
ALLALMIFRL SVWAGCATPG SELMNLRYRD EGAMEAAARA AARRGSGAAA GPSGRGAAQP
GWLHGGRSGV EGPGLSRRQR FLFAAGTIAL PYLWQRMHRL VAANDEWGTA PPAPWRSGSS
GRDEGSPQAR RRAALAAAWR ALRWLEGAYK VGVAANLLVF LYQGKYRTPL ERLLGARLVY
KQPEMSRVIS FEYLNRQLVW QELSDFLLFV LPLVNVARVK RAMLRAFPRL PLLTAGAAAG
GGAAAVAAGW TVAAKPDGGG GGGSGQSQQR RLGQGDCTSA PAAAAAAATA AAAAAAAAEG
ADAEDEYDPP GPCPICGLRE IVVPYVALPC RHVFCYYCLR AHCEADTAFE CPVDASRVAA
LQRFDGRAER RRRRGEVR
//
