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TIM50_SCHPO
ID   TIM50_SCHPO             Reviewed;         452 AA.
AC   O13636; Q7LL08;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit tim50;
DE   Flags: Precursor;
GN   Name=tim50; ORFNames=pi044, SPBC17A3.01c, SPBC8D2.21c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; AB004537; BAA21424.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA17836.2; -; Genomic_DNA.
DR   PIR; T39693; T39693.
DR   RefSeq; NP_595583.2; NM_001021478.3.
DR   AlphaFoldDB; O13636; -.
DR   SMR; O13636; -.
DR   ComplexPortal; CPX-540; Mitochondrial inner membrane pre-sequence translocase complex.
DR   STRING; 4896.SPBC17A3.01c.1; -.
DR   MaxQB; O13636; -.
DR   PaxDb; O13636; -.
DR   EnsemblFungi; SPBC17A3.01c.1; SPBC17A3.01c.1:pep; SPBC17A3.01c.
DR   GeneID; 2539802; -.
DR   KEGG; spo:SPBC17A3.01c; -.
DR   PomBase; SPBC17A3.01c; tim50.
DR   VEuPathDB; FungiDB:SPBC17A3.01c; -.
DR   eggNOG; KOG2832; Eukaryota.
DR   HOGENOM; CLU_023309_1_0_1; -.
DR   InParanoid; O13636; -.
DR   OMA; LGRNWDT; -.
DR   PhylomeDB; O13636; -.
DR   PRO; PR:O13636; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0016021; C:integral component of membrane; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; ISS:PomBase.
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..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..452
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit tim50"
FT                   /id="PRO_0000043136"
FT   TOPO_DOM        28..99
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..452
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          172..316
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          30..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  52572 MW;  83E516CBED6271B3 CRC64;
     MLNRSLLFRN LRLARPRPFL PLVGKRFVTE KSQSQEEKDT SKITENAKEE VKRDTSSLAK
     ESLKLLDLNG LNDESYTGDP GKGPEYTSST MLKREKQARY AFWGFLGLTG GGLLYYGRRY
     GPDEKELEKQ YPAAGYSPSD WWNRVKARTN NFFSYYQEPA FEKLLPDPLP EPYNRPYTLV
     LSLDDLLIHS EWTRQHGWRT AKRPGLDYFL GYLSMYYEVV IFTRQYLATA KPIIDKIDPY
     HVSISAVLTR ESSKYEKGKV IKDLSYLNRD LSRVIMIDTN PESWSKQPDN AIAMAPWTGN
     PKDKELVGLI PLLEFIAIMD IKDVRPVLKS YQGKNIPLEY ARREEKLRTK LIEDWNEKKK
     KGSSFLFGGR SVSEEPPKLI IDIQRERQKA AYAEFKKYID ENGPKMLEEE KAREAEQKTS
     IFNLLFHPEE VQQQQLEQMQ QQQFSPETNA SK
 
 
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