ID A0A2G5UU14_9PELO Unreviewed; 391 AA.
AC A0A2G5UU14;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000256|ARBA:ARBA00029536, ECO:0000256|PIRNR:PIRNR037880};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251, ECO:0000256|PIRNR:PIRNR037880};
GN Name=Cni-pdr-1 {ECO:0000313|EMBL:PIC42716.1};
GN Synonyms=Cnig_chr_III.g9702 {ECO:0000313|EMBL:PIC42716.1};
GN ORFNames=B9Z55_009702 {ECO:0000313|EMBL:PIC42716.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC42716.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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|ARBA:ARBA00004173, ECO:0000256|PIRNR:PIRNR037880}.
CC -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily.
CC {ECO:0000256|ARBA:ARBA00029442, 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:PIC42716.1}.
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DR EMBL; PDUG01000003; PIC42716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UU14; -.
DR STRING; 1611254.A0A2G5UU14; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000230233; Chromosome iii.
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; cd20357; Rcat_RBR_parkin; 1.
DR CDD; cd17039; Ubl_ubiquitin_like; 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; IPR047536; Rcat_RBR_parkin.
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; PF01485; IBR; 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; 2.
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|ARBA:ARBA00023006, 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|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR037880};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
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 10..82
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 192..391
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT ACT_SITE 360
FT /evidence="ECO:0000256|PIRSR:PIRSR037880-1"
SQ SEQUENCE 391 AA; 44786 MW; ED162DD330F0CB6A CRC64;
MLFSGMSNEV TVVLQDRKTG QRRNYTINVN NNENILELTK SVEKITKIPS EELEVVFCGK
KLSKSTIMKD LSLTPATQIM LLRPNSVVKT ATTSSPKLQT TDTSILGSFY VWCKSCDDVR
RGKLRVYCQN CESTSVLVKS EPQNWMDVLK SKRIPVTCEN CCRPGLYAEF KFKCLTCNDL
AAALTHVRGN WQMAECCICD GKEKIIFDLG CNHISCQSCF KDYLLSTLQE FHFENRPPYG
FTVSCVYPEC NRVVQDVHHF HVMGQSSYSE YQRKATERLI AIDDEGVTCP NPSCGQSFFW
EPYDDDGRSQ CPDCFYTFCR KCTERDCVCQ SEDDLTRTTI EATTRRCPKC NVATERNGGC
AHIHCTSCGM DWCFKCVTEW KEECQWDHWF N
//
