ID A0A016SL06_9BILA Unreviewed; 405 AA.
AC A0A016SL06;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000256|PIRNR:PIRNR037880};
DE EC=2.3.2.31 {ECO:0000256|PIRNR:PIRNR037880};
GN Name=Acey_s0206.g1971 {ECO:0000313|EMBL:EYB91398.1};
GN Synonyms=Acey-pdr-1 {ECO:0000313|EMBL:EYB91398.1};
GN ORFNames=Y032_0206g1971 {ECO:0000313|EMBL:EYB91398.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB91398.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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|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: Mitochondrion {ECO:0000256|PIRNR:PIRNR037880}.
CC -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily.
CC {ECO:0000256|PIRNR:PIRNR037880}.
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:EYB91398.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JARK01001542; EYB91398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SL06; -.
DR STRING; 53326.A0A016SL06; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd17039; Ubl_ubiquitin_like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR003977; Parkin.
DR InterPro; IPR041565; Parkin_Znf-RING.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
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; PF00240; ubiquitin; 1.
DR Pfam; PF17976; zf-RING_12; 1.
DR Pfam; PF17978; zf-RING_14; 1.
DR PIRSF; PIRSF037880; Parkin; 2.
DR PRINTS; PR01475; PARKIN.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|PIRNR:PIRNR037880};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR037880};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR037880};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
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 4..77
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 189..405
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT ACT_SITE 374
FT /evidence="ECO:0000256|PIRSR:PIRSR037880-1"
SQ SEQUENCE 405 AA; 45909 MW; 2C95DB4155C231B2 CRC64;
MDELVVVVHN RADRSKRSLL VPFDQNDTVR SFEQRISEKT GIPSRKLKVV LCGHALEETT
FLKDLLLGPT TSLIVFVDNE HTSTCDTKEG STADAHLTRT TPEIGSFYVW CKTCCDIQRG
KLRVYCSRCS SSAVLVKTEP SCWKDVTRSR QIEVVCADCK STQHAVFKFK CVTCNEVGAV
LSHIRGNWEH VECSVCLDEH NTYLFDLGCH HMVCRQCFVE CLAIALKEAQ FVFRPPFGYT
ITCPHPGCDR CVTDVHHFRV LGDESYEKYQ KIATEKLVAM DDQGVFCPYP DCNASFFWEV
EDDDGIISCP ECLRLFCRYF FNFTIHITSA PTHLRLCKSA NCVCGIDDPT TTTIKATTKK
CPGCGANTER NEGCAHIHCI VCKMDWCFVC VAPWTEDCQW NHWFS
//
