ID DNJ20_CAEBR Reviewed; 382 AA.
AC Q626I7; A8WP80;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=DnaJ homolog dnj-20;
DE AltName: Full=DnaJ domain protein 20;
DE Flags: Precursor;
GN Name=dnj-20 {ECO:0000250|UniProtKB:Q8MPX3}; ORFNames=CBG00965;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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DR EMBL; HE600951; CAP22286.1; -; Genomic_DNA.
DR RefSeq; XP_002629733.1; XM_002629687.1.
DR AlphaFoldDB; Q626I7; -.
DR SMR; Q626I7; -.
DR STRING; 6238.Q626I7; -.
DR GeneID; 8573301; -.
DR KEGG; cbr:CBG_00965; -.
DR CTD; 8573301; -.
DR WormBase; CBG00965; CBP42204; WBGene00024268; Cbr-dnj-20.
DR eggNOG; KOG0713; Eukaryota.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q626I7; -.
DR OMA; FAGRDFY; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR44298; DNAJ HOMOLOG SUBFAMILY B MEMBER 11; 1.
DR PANTHER; PTHR44298:SF1; DNAJ HOMOLOG SUBFAMILY B MEMBER 11; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 2.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..382
FT /note="DnaJ homolog dnj-20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000270980"
FT DOMAIN 24..89
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
SQ SEQUENCE 382 AA; 42983 MW; 07458D9A33D2B62C CRC64;
MRILNVSLLV LTAFLVDFVE CGRDFYKILG VSKNANANQI KKAYRKQAKE LHPDRNPDDE
MANEKFQDLS AAYEVLSDKE KRAMYDRHGE EGVAKMGGGG GGGHDPFSSF FGDFFGGGGG
NGGDEGTPKG ADVTIDLFVT LEEAYNGHFV EIKRKKAVYK QTSGTRQCNC RHEMRTEQMG
QGRFQMFQVK VCDECPNVKL VQENKVLEVE VEVGADEGHT QIFHGEGEPH IEGDPGDLKF
KIRIQKHPRF LISVTGIEII ELKVDELVEL LLEGIRFERK GDDLYTNVTI SLQDALNGFE
MEILHLDGHM VKVQRDKVTW PGARLRKKDE GMPSMENNNK KGMLIVTFDV EFPKTELTDE
QKAQIIEILQ QQGIKPRAYN GL
//
