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TIM50_CRYNB
ID   TIM50_CRYNB             Reviewed;         516 AA.
AC   P0CN67; Q55ZJ2; Q5KNV7;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE   Flags: Precursor;
GN   Name=TIM50; OrderedLocusNames=CNBA4980;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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 and TIM50. Interacts with preproteins in transit (By similarity).
CC       {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; AAEY01000003; EAL23153.1; -; Genomic_DNA.
DR   RefSeq; XP_777800.1; XM_772707.1.
DR   AlphaFoldDB; P0CN67; -.
DR   SMR; P0CN67; -.
DR   EnsemblFungi; AAW40998; AAW40998; CNA05150.
DR   EnsemblFungi; EAL23153; EAL23153; CNBA4980.
DR   GeneID; 4933760; -.
DR   KEGG; cnb:CNBA4980; -.
DR   VEuPathDB; FungiDB:CNBA4980; -.
DR   HOGENOM; CLU_023309_1_1_1; -.
DR   Proteomes; UP000001435; Chromosome 1.
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:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   Transit peptide; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..516
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM50"
FT                   /id="PRO_0000410088"
FT   TOPO_DOM        18..166
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..516
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          231..375
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  56881 MW;  D6DDBEA5917935A5 CRC64;
     MLRQATSRFL SSTHRSIRPL STTAPSFIRI RSQASEPSPA ERPPPVPENV NPSQPFEPEV
     SKSEGTAKAA ETQQAEEPAS AGTPLTPPQP EVVFGNTHSA ASTTPETEPN VENPDYSKLP
     SLDIDQEAAA ISEPATGKDQ EVEGGERKKT GAGKKEYVSS QEKSRRMWIR AGYGALAVGA
     VGAVLAMGND ETTGKKQGGF VETFQNNMLE LFDFFNKPAF QTLLPDPLPP PHQRPYTLCI
     DLEGLLVHSS WDRTHGWRTA KRPGVDYFLG YLSQFYEIVL FSSQPLYTAA PIAEKIDPYQ
     AFMPYRLFRE STRSVKGKVV KDISFLNRDP SKVIVLDVNP EHVALQPENG IVLQPWNGSP
     GDKGLVDMIP FLESIGIFNP ADVRPILQAY AGKDIPIEYA KKEAEAKAKA IEEWERAHPT
     AITGAGSGFL SSIFGSVAAP GSSRPNQPMT YLEQKRAQAQ RIYQEEQKYW AEHADEFKKL
     IEEDKQRQLA EMKGSILGYL GAPKMQDGPK EEVLKA
 
 
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