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TIM50_YARLI
ID   TIM50_YARLI             Reviewed;         466 AA.
AC   Q6CDV7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE   Flags: Precursor;
GN   Name=TIM50; OrderedLocusNames=YALI0B20856g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382128; CAG83408.1; -; Genomic_DNA.
DR   RefSeq; XP_501155.1; XM_501155.1.
DR   AlphaFoldDB; Q6CDV7; -.
DR   SMR; Q6CDV7; -.
DR   STRING; 4952.CAG83408; -.
DR   EnsemblFungi; CAG83408; CAG83408; YALI0_B20856g.
DR   GeneID; 2907093; -.
DR   KEGG; yli:YALI0B20856g; -.
DR   VEuPathDB; FungiDB:YALI0_B20856g; -.
DR   HOGENOM; CLU_023309_1_2_1; -.
DR   InParanoid; Q6CDV7; -.
DR   OMA; LGRNWDT; -.
DR   Proteomes; UP000001300; Chromosome B.
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..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..466
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM50"
FT                   /id="PRO_0000043138"
FT   TOPO_DOM        30..112
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..466
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          188..332
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          52..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  52853 MW;  40ACEBFAAD2F4A69 CRC64;
     MHSLLRAAQI ARVARPGVKR AMTPAVRFYS DKKTEKSDQP FQSSLLNDDL LAQAGMDVDE
     SKGKSKPAAE GKSEGAAEGA TEDDVTDEQR ARWAGTAKKS TDQTSKQESR ERIAGYGYYA
     FFAGSAAFAA YLARDWDNEE DKKKHDTIGQ GYTPMLMWAR LKARIGDTFS FYRDPVAPVL
     LPDPPAPPYQ RPLTLVIALD DLLVHQEWSR EHGWRVAKRP GVDYFLGYLG QYYEIVLFSS
     QYMANCEKLI MKLDPYHAWF SHVLTREHTT YEDGKLVKDL SLMNRDMGKI IIIDPDTGCT
     MKQPENSIPI EPWKGTPGDK ELVKLIPFLE WLVSQNVNDV RPILKAFDGT YLPDEFTRRE
     AIAREKFEKD WYAKHGKDGQ WASKFLGVSE PKQQKPLMPH DVMRREGQKQ YQKFLEYLAV
     EGPKLKAEEE RMIAEQKAMG PKNLSEAVSS IGSLPPVPQQ PTEPKA
 
 
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