TIM50_CANGA
ID TIM50_CANGA Reviewed; 485 AA.
AC Q6FRX4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE Flags: Precursor;
GN Name=TIM50; OrderedLocusNames=CAGL0H05159g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380954; CAG59953.1; -; Genomic_DNA.
DR RefSeq; XP_447020.1; XM_447020.1.
DR AlphaFoldDB; Q6FRX4; -.
DR SMR; Q6FRX4; -.
DR STRING; 5478.XP_447020.1; -.
DR EnsemblFungi; CAG59953; CAG59953; CAGL0H05159g.
DR GeneID; 2888680; -.
DR KEGG; cgr:CAGL0H05159g; -.
DR CGD; CAL0130595; CAGL0H05159g.
DR VEuPathDB; FungiDB:CAGL0H05159g; -.
DR eggNOG; KOG2832; Eukaryota.
DR HOGENOM; CLU_023309_1_2_1; -.
DR InParanoid; Q6FRX4; -.
DR OMA; LGRNWDT; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..485
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM50"
FT /id="PRO_0000043128"
FT TOPO_DOM 36..120
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..485
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 193..336
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 76..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 57154 MW; 1788E9590739B623 CRC64;
MLSLFRCAVT RAPHIASKGI SVQISRNLAN SLIVQNKRRL NTKSYFLQEQ KKDDKKAQSI
LTDDLLFKAG IDVEEGKKEG QQKQHETEEG NEEQQSENSS NKKRKRRMTS ADKKKERYAN
YFYIFTFSSL AGLGLYMCRD WEENEDDEMK KDIDNGYTPD LMYKRFRARF NSVFTYFQEP
PFPDLLPPPP PAPYQRPLTL VITLEDFLVH SEWDQKHGWR TAKRPGADYF LGYLSQYYEI
VLFSSNYMMY AEKIAEKMDP IHAFISYNLF KEHCVYKDGV HIKDLSKLNR DLKKVMIIDT
DENSYKLQPE NAIPMDPWDG KADDKLLRLI PFLEYMATQQ VEDVRPILKS YHNKRELPAE
FEQRVQKLKN KFEQDQKKKN DSNWLLKLLG LAPVINGIGG GNKFPLDMIR EEGEKNYVRF
MKLIEEEKEK MRIQQEQMSG QTFTLKDYVE GNIPTPEEQM KMQLEKQKEI DALFEQKKKE
QQANK
