JID1_ASHGO
ID JID1_ASHGO Reviewed; 305 AA.
AC Q75BG6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=J domain-containing protein 1;
GN Name=JID1; OrderedLocusNames=ADL327W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Probable chaperone. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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DR EMBL; AE016817; AAS51593.1; -; Genomic_DNA.
DR RefSeq; NP_983769.1; NM_209122.1.
DR AlphaFoldDB; Q75BG6; -.
DR SMR; Q75BG6; -.
DR STRING; 33169.AAS51593; -.
DR EnsemblFungi; AAS51593; AAS51593; AGOS_ADL327W.
DR GeneID; 4619904; -.
DR KEGG; ago:AGOS_ADL327W; -.
DR eggNOG; ENOG502RYTK; Eukaryota.
DR HOGENOM; CLU_074165_0_0_1; -.
DR InParanoid; Q75BG6; -.
DR OMA; NAGTWED; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone; Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..305
FT /note="J domain-containing protein 1"
FT /id="PRO_0000240377"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 91..163
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
SQ SEQUENCE 305 AA; 34206 MW; 161DE21CC323A29E CRC64;
MAKRANWSLD GQQSSGGGAA SWICACTDKI SIAKALTRSL SVMLSRPTAL LRTGARWRVS
LTASGRSTVR CASTVAGWQG GLSWPQGKQP TPYEVLGLVK TGVDARQLKK RYHELAKLYH
PDTAGAAQQG LGEHERLRRF KLVNEAYALL SDASRRRMYD MYATGWAHGP APMAPAMAHG
AYHERYAYYN AGTWEDMQDL NSDRQQVQFS AWGMVVWALC MLAGFQVMAF LIRLEERTSK
SAHTHEEAEH ALLLAHLNYG LDQDRVSRVR RFLWFRSWGL YRTKAELDEA ARTNEALVRQ
LEGGK