RN113_CAEEL
ID RN113_CAEEL Reviewed; 384 AA.
AC O17917;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable E3 ubiquitin-protein ligase rnf113;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O15541};
DE AltName: Full=RING finger protein 113 homolog;
GN Name=rnf-113; ORFNames=K01G5.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as E3 ubiquitin-protein ligase that catalyzes
CC the transfer of ubiquitin onto target proteins. May play a role in DNA
CC repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin
CC chains that recruit proteins involved in repair to sites of DNA damage
CC by alkylating agents. {ECO:0000250|UniProtKB:O15541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:O15541};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O15541}.
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DR EMBL; Z92803; CAB07242.2; -; Genomic_DNA.
DR EMBL; AF304126; AAG50239.1; -; mRNA.
DR PIR; T23197; T23197.
DR RefSeq; NP_499375.1; NM_066974.4.
DR AlphaFoldDB; O17917; -.
DR SMR; O17917; -.
DR BioGRID; 41694; 33.
DR IntAct; O17917; 1.
DR STRING; 6239.K01G5.1; -.
DR EPD; O17917; -.
DR PaxDb; O17917; -.
DR PeptideAtlas; O17917; -.
DR EnsemblMetazoa; K01G5.1.1; K01G5.1.1; WBGene00010476.
DR GeneID; 176507; -.
DR KEGG; cel:CELE_K01G5.1; -.
DR UCSC; K01G5.1.1; c. elegans.
DR CTD; 176507; -.
DR WormBase; K01G5.1; CE26718; WBGene00010476; rnf-113.
DR eggNOG; KOG1813; Eukaryota.
DR GeneTree; ENSGT00390000016292; -.
DR HOGENOM; CLU_050460_1_0_1; -.
DR InParanoid; O17917; -.
DR OMA; PEDCYIC; -.
DR OrthoDB; 1420266at2759; -.
DR PhylomeDB; O17917; -.
DR SignaLink; O17917; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O17917; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010476; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; HDA:WormBase.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:WormBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IDA:WormBase.
DR GO; GO:0034247; P:snoRNA splicing; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039971; CWC24-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12930; PTHR12930; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..384
FT /note="Probable E3 ubiquitin-protein ligase rnf113"
FT /id="PRO_0000056089"
FT ZN_FING 175..203
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 241..279
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..384
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 43428 MW; 308057FCC5051277 CRC64;
MDLFRKPKKR NAPVVRKKES SSDEDQDSEV KDVIQKRRRT NPMVQSTKQL DASTRRADNS
SDDSDDSDDN QDIAVATHSF AASGDAGPSG PRDQGATATL EVDTDYSHDA QAQFERVQQQ
LKEGVEKDGK ILYKGSALYG AKEAKDTAKG NAASGYNRVG PVRAPQFLRQ TVRWDFAPDI
CKDYKETGFC TFGDSCKFVH DRSDYKHGWE IDEEYEAGKY GAEDDANYEI HEGDDTFPED
CFICGNPFVD PIVTKCKHYF CTGCALKSFQ KSSKCPICQQ NTENIMNTAK ELLTYLKRKK
QQQKQEAEKQ EEEKDSDDDE KPHECDDHHH HDHEDEPEEP ENDSNVPEAE EKSDEEQEIM
MEDVEGLEGG ENDSESDDDD AEKD
