ID   BAG1_CAEBR              Reviewed;         209 AA.
AC   Q61D31; A8XG96;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=BAG family molecular chaperone regulator 1;
GN   Name=bag-1; ORFNames=CBG12655;
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).
CC   -!- FUNCTION: May inhibit the chaperone activity of HSP70/HSC70 by
CC       promoting substrate release in an ATP-dependent manner. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
CC   -!- DOMAIN: The BAG domain probably mediates direct interaction with HSP70.
CC       {ECO:0000250}.
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DR   EMBL; HE600940; CAP31602.1; -; Genomic_DNA.
DR   RefSeq; XP_002640155.1; XM_002640109.1.
DR   AlphaFoldDB; Q61D31; -.
DR   SMR; Q61D31; -.
DR   STRING; 6238.CBG12655; -.
DR   EnsemblMetazoa; CBG12655.1; CBG12655.1; WBGene00033572.
DR   GeneID; 8582151; -.
DR   KEGG; cbr:CBG_12655; -.
DR   CTD; 8582151; -.
DR   WormBase; CBG12655; CBP17556; WBGene00033572; Cbr-bag-1.
DR   eggNOG; ENOG502S5YF; Eukaryota.
DR   HOGENOM; CLU_1316430_0_0_1; -.
DR   InParanoid; Q61D31; -.
DR   OMA; AGFKMLM; -.
DR   OrthoDB; 1262293at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:EnsemblMetazoa.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   Gene3D; 1.20.58.120; -; 1.
DR   InterPro; IPR017093; BAG-1.
DR   InterPro; IPR039773; BAG_chaperone_regulator.
DR   InterPro; IPR036533; BAG_dom_sf.
DR   InterPro; IPR003103; BAG_domain.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR12329; PTHR12329; 1.
DR   PANTHER; PTHR12329:SF16; PTHR12329:SF16; 1.
DR   Pfam; PF02179; BAG; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PIRSF; PIRSF037029; BAG_1; 1.
DR   SMART; SM00264; BAG; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF63491; SSF63491; 1.
DR   PROSITE; PS51035; BAG; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Chaperone; Reference proteome.
FT   CHAIN           1..209
FT                   /note="BAG family molecular chaperone regulator 1"
FT                   /id="PRO_0000088876"
FT   DOMAIN          7..84
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          107..193
FT                   /note="BAG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
SQ   SEQUENCE   209 AA;  23732 MW;  4A88A89841926656 CRC64;
     MKLVVSCSSV QTIVDILDES EGENSISTLG QLRERIAADN DVDAETMKLL HRGKFLQGEA
     DVSLSTINFK ENDKIIVMGG KNAMADDAGF KMLMQYEKHN LSNLQKTYDV NLKDVADLER
     GFLEKPKQVE MGKKLEKKVK FFNEEAERHL ETLDGMNIIT DATPDNQAKR NREKRKTLIN
     GIQTLLNQND ALLRRLEQYM SILNGDILE