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Database: UniProt
Entry: A0A2I2FYA1_9EURO
LinkDB: A0A2I2FYA1_9EURO
Original site: A0A2I2FYA1_9EURO 
ID   A0A2I2FYA1_9EURO        Unreviewed;       523 AA.
AC   A0A2I2FYA1;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50 {ECO:0000256|ARBA:ARBA00020799, ECO:0000256|RuleBase:RU365079};
GN   ORFNames=P170DRAFT_389606 {ECO:0000313|EMBL:PLB45613.1};
OS   Aspergillus steynii IBT 23096.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB45613.1, ECO:0000313|Proteomes:UP000234275};
RN   [1] {ECO:0000313|EMBL:PLB45613.1, ECO:0000313|Proteomes:UP000234275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB45613.1,
RC   ECO:0000313|Proteomes:UP000234275};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|RuleBase:RU365079}.
CC   -!- SUBUNIT: Component of the TIM23 complex.
CC       {ECO:0000256|RuleBase:RU365079}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434,
CC       ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU365079}.
CC   -!- SIMILARITY: Belongs to the TIM50 family.
CC       {ECO:0000256|ARBA:ARBA00006344, ECO:0000256|RuleBase:RU365079}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PLB45613.1}.
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DR   EMBL; MSFO01000007; PLB45613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2FYA1; -.
DR   STRING; 1392250.A0A2I2FYA1; -.
DR   VEuPathDB; FungiDB:P170DRAFT_389606; -.
DR   OrthoDB; 11362at2759; -.
DR   Proteomes; UP000234275; Unassembled WGS sequence.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR12210:SF3; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM50; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU365079};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU365079};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU365079};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010,
KW   ECO:0000256|RuleBase:RU365079}; Transport {ECO:0000256|RuleBase:RU365079}.
FT   DOMAIN          239..382
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   REGION          36..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  59418 MW;  45B0CB47FF7FC7C1 CRC64;
     MLSRAVLPLT RPNVLASTLR VPALPVTHSR FYAKVGKPKA PYNIPESVKP SQPEQPTNSS
     QQEPSPEQAQ PDANTESQSS KHVESEPTPA QKQAPQKPLP DLTQGIPSTL AAELEARSKN
     RNQSPLNLTE AEDPSRSEEY TDDGRDGDIP KSGYESSLDR RRARMANLMY VLFLLAGAGG
     GAYLGRNWDT EEEEKAHPDV PSGWGFGLWY NRIKARYSDI TSYYKDPAFP SLLPDEDPMM
     RQPYTLVLSL EDLLVHSEWS REHGWRVAKR PGVDYFLRYL NQYYELVLFT SVPSMMADQV
     LRKLDPYRII RWPLFREATR YKDGEYIKDL SYLNRDLSKV ILIDTKEEHA RLQPENAIVL
     DKWHGDPKDK TLVALIPFLE YLAGMGVDDV RPVMKSFDGT SIPIEFAKRE KAMRERFEKE
     LAEEQKKKPK VGMGNLASAL GLKSTRTLDG EQSPSEGLAQ GKMLWDQIRE RGQKNYQMIE
     AEIRMNGEKW LAEMAAEEEK ARQEQMDAMK GSFTGMFGAG KKE
//
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