ID A0A0B1TRQ4_OESDE Unreviewed; 388 AA.
AC A0A0B1TRQ4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000256|PIRNR:PIRNR037880};
DE EC=2.3.2.31 {ECO:0000256|PIRNR:PIRNR037880};
GN ORFNames=OESDEN_01955 {ECO:0000313|EMBL:KHJ98065.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ98065.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ98065.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ98065.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex,
CC catalyzing the covalent attachment of ubiquitin moieties onto substrate
CC proteins. {ECO:0000256|PIRNR:PIRNR037880}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798,
CC ECO:0000256|PIRNR:PIRNR037880};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR037880}.
CC -!- SUBUNIT: Forms an E3 ubiquitin ligase complex.
CC {ECO:0000256|PIRNR:PIRNR037880}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion
CC {ECO:0000256|PIRNR:PIRNR037880}.
CC -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily.
CC {ECO:0000256|PIRNR:PIRNR037880}.
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DR EMBL; KN549362; KHJ98065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1TRQ4; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053660; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd20336; Rcat_RBR; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR003977; Parkin.
DR InterPro; IPR041565; Parkin_Znf-RING.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR041170; Znf-RING_14.
DR PANTHER; PTHR11685:SF449; E3 UBIQUITIN-PROTEIN LIGASE PARKIN; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF17976; zf-RING_12; 1.
DR Pfam; PF17978; zf-RING_14; 1.
DR PIRSF; PIRSF037880; Parkin; 3.
DR PRINTS; PR01475; PARKIN.
DR SMART; SM00647; IBR; 1.
DR SUPFAM; SSF57850; RING/U-box; 4.
DR PROSITE; PS51873; TRIAD; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|PIRNR:PIRNR037880};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR037880};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR037880};
KW Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843,
KW ECO:0000256|PIRNR:PIRNR037880};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR037880};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037880};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 128..388
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR037880-1"
SQ SEQUENCE 388 AA; 43704 MW; 66578B22268BB5A1 CRC64;
MYGFMSRSLI VFVENRQPFA CSAKATSTAG EPEPAVARAT PEIGSFYVWC KSCSDIRRGK
LRVYCSACSS SAVLVKTEPS CWKDVTRSNQ IEVTCAECKS THYAVFRFKC IKCNEVGAVL
SHIRGNWEHV QCSVCLDEHT TYLFDFGCHH MVCRQCFVEC LTLALEESRF IFRPPFGYTI
TCPYPGCERC VADVHHFHVL GDEKYQRYQK LATEKLVAMD DQGVFCPYPD CNASFFWEVE
DDDGKTLCPE CLRLFCRLCK SADCVCGVDD PTEVTIKATT KKCPGCGANT ERNEGCAHIH
CIVCKMDWCF GHSPFLFRLC KSADCVCGVD DPTEVTIKAT TKKCPGCGAN TERNEGCAHI
HCIVCKMDWC FVCVAPWTED CQWNHWFS
//
