ID G0VBA6_NAUCC Unreviewed; 229 AA.
AC G0VBA6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 03-MAY-2023, entry version 48.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN Name=NCAS0B01460 {ECO:0000313|EMBL:CCC68230.1};
GN OrderedLocusNames=NCAS_0B01460 {ECO:0000313|EMBL:CCC68230.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC68230.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC68230.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the PAM complex, a complex required
CC for the translocation of transit peptide-containing proteins from the
CC inner membrane into the mitochondrial matrix in an ATP-dependent
CC manner. {ECO:0000256|RuleBase:RU000640}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU000640}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|RuleBase:RU004478}.
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DR EMBL; HE576753; CCC68230.1; -; Genomic_DNA.
DR RefSeq; XP_003674606.1; XM_003674558.1.
DR AlphaFoldDB; G0VBA6; -.
DR STRING; 1064592.G0VBA6; -.
DR GeneID; 11525233; -.
DR KEGG; ncs:NCAS_0B01460; -.
DR eggNOG; KOG3003; Eukaryota.
DR HOGENOM; CLU_057217_0_0_1; -.
DR InParanoid; G0VBA6; -.
DR OMA; YAYEKIA; -.
DR OrthoDB; 151932at2759; -.
DR Proteomes; UP000001640; Chromosome 2.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 1.
DR HAMAP; MF_01151; GrpE; 1.
DR InterPro; IPR000740; GrpE.
DR InterPro; IPR013805; GrpE_coiled_coil.
DR InterPro; IPR009012; GrpE_head.
DR PANTHER; PTHR21237; GRPE PROTEIN; 1.
DR PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000640};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Mitochondrion {ECO:0000256|RuleBase:RU000640};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640}.
FT COILED 47..88
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 229 AA; 26033 MW; 330D870D80BB2B6D CRC64;
MSALFTSATR SASRRLTIQT PTAMRSLALN RSATLPLNFR LYSDAAKDKE QKEEQKSDEN
LTEEQKKIKE LETKLETKSK EAVELKDSLL RSVADFRNLQ NVTKKDIQKA KDFALQKFAK
DLLESVDNFG HALSAFKEED LEKSKEISDL YTGVRMTRDV FEKTLKKHGI EKLDPIGETF
DPNKHEATFE LAQPDKEPGT VFHVQQIGFT LNDRVIRPAK VGIVKSTDE
//
