TIM50_ASHGO
ID TIM50_ASHGO Reviewed; 476 AA.
AC Q75A73;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE Flags: Precursor;
GN Name=TIM50; OrderedLocusNames=ADR045W;
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, AND SEQUENCE REVISION TO 183-184; 186; 204; 210;
RP 215-216; 223; 229; 233; 237 AND 245.
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: Essential component of the TIM23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane. Required to direct preproteins
CC in transit and direct them to the channel protein TIM23, and possibly
CC facilitates transfer of the translocating proteins from the TOM complex
CC to the TIM23 complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the TIM23 complex, at least composed of TIM23,
CC TIM17, TIM50 and TIM21. Interacts with preproteins in transit (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TIM50 family. {ECO:0000305}.
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DR EMBL; AE016817; AAS51965.2; -; Genomic_DNA.
DR RefSeq; NP_984141.2; NM_209494.2.
DR AlphaFoldDB; Q75A73; -.
DR SMR; Q75A73; -.
DR STRING; 33169.AAS51965; -.
DR EnsemblFungi; AAS51965; AAS51965; AGOS_ADR045W.
DR GeneID; 4620290; -.
DR KEGG; ago:AGOS_ADR045W; -.
DR eggNOG; KOG2832; Eukaryota.
DR HOGENOM; CLU_023309_1_2_1; -.
DR InParanoid; Q75A73; -.
DR OMA; LGRNWDT; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IEA:EnsemblFungi.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027111; Tim50.
DR PANTHER; PTHR12210:SF3; PTHR12210:SF3; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW Reference proteome; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..9
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 10..476
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM50"
FT /id="PRO_0000043125"
FT TOPO_DOM 10..110
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..476
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 186..329
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 40..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 54798 MW; 909B64ED2275893D CRC64;
MLHVIRRSRA TSARQLPRVA GLLAGAAAVR SRTYIGTRIL HEEQKPKKPE PPNSILTEDM
LARAGVDAER GPETEKAPAE DKAGESTETG SGAGKKKRAR KTTTEIKRER YANLFYLFSL
TGLAGGAVYM SRDWDADEPE EERKGIENGY TPGLMYRRFK ARFDSLFTFF QEPPYPDLLP
PPPPPPYQRP LTLVLPLEDF FVHSEWTQQH GWRTAKRPGA DYFLGYLSQY YEIVLFSSNY
MVYSEKVVEK LDPIRAFITY NLFKDHCVYK DGIHIKDLSH LNRDLGKTLI IDTDPNSVKL
QMENAILAEP WDGKADDALL RYIPFLEYLV TQPINDVRPI LNSFKDRHHI PEEFAERVEK
LRAKFNADQK AKAGSGLSFL LNPGMASKPA KFPLDLIREE GEKNYVRFMK LIEEEKEKLK
LQQEHMSAPT FTLKDMAEGN MPTPEEQMKM QLQKQKEFEE LYEKEKQKMQ QQTKGQ
