ID   TIM50_EMENI             Reviewed;         532 AA.
AC   Q5B4P0; C8V8E4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit tim50;
DE   Flags: Precursor;
GN   Name=tim50; ORFNames=AN4490;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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
CC       TIM23/timX, TIM17/timQ, tim50 and TIM21/timU. Interacts with
CC       preproteins in transit (By 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AACD01000078; EAA60833.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF77402.1; -; Genomic_DNA.
DR   RefSeq; XP_662094.1; XM_657002.1.
DR   AlphaFoldDB; Q5B4P0; -.
DR   SMR; Q5B4P0; -.
DR   STRING; 162425.CADANIAP00005955; -.
DR   EnsemblFungi; CBF77402; CBF77402; ANIA_04490.
DR   EnsemblFungi; EAA60833; EAA60833; AN4490.2.
DR   GeneID; 2872288; -.
DR   KEGG; ani:AN4490.2; -.
DR   VEuPathDB; FungiDB:AN4490; -.
DR   eggNOG; KOG2832; Eukaryota.
DR   HOGENOM; CLU_023309_0_0_1; -.
DR   InParanoid; Q5B4P0; -.
DR   OMA; LGRNWDT; -.
DR   OrthoDB; 1142452at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..532
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit tim50"
FT                   /id="PRO_0000043131"
FT   TOPO_DOM        33..175
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..532
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          247..390
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          26..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  60251 MW;  777EE885CEC77B8C CRC64;
     MLRRAILPLT RPSGLVSAPR LSALPVSHSR CYAKGSKPKT PYKLPESVKS SKPEQPAKPS
     QQEQYAAEQA EFETTSDPQA NTANTTSQAS SSPESSPSQS EQDAPQRPLP DLTQGIPSTL
     AAELEARSKK SGSGTLNLTE DPSRFEEDYS DDGRGDIPKG GYESSLDRKR ARMAKLMYAL
     FLLGSVGGMA YLGRNWDTVE EENAHPDVPS GWSFGLWYNR IKARMGDFTS YYKDPAFPKL
     LPDEDPNLRQ PYTLVLSLED LLVHSEWSRE HGWRVAKRPG VDYFLRYLNQ YYELVLFTSV
     PSMMADQVLR KLDPYRIIRW PLFREATRYK DGEYIKDLSY LNRDLSKVIL IDTKEEHARL
     QPENAIILDK WNGNPKDKTL VALIPFLEYL AGMGVDDVRT VLKSFEGQSI PIEFAKREKA
     MRERFEKELA EEQKKRPRSG MGSLASALGL KSSARTLDGE QLPSAGLQEG KMLWDQIRER
     GQKNYELIEK EIRENGEKWL AEMAAEEEKL RQEQMESMKG SLTGFFGGGK KE