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Database: UniProt
Entry: G2YPR4_BOTF4
LinkDB: G2YPR4_BOTF4
Original site: G2YPR4_BOTF4 
ID   G2YPR4_BOTF4            Unreviewed;       575 AA.
AC   G2YPR4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50 {ECO:0000256|ARBA:ARBA00020799, ECO:0000256|RuleBase:RU365079};
GN   ORFNames=BofuT4_P136570.1 {ECO:0000313|EMBL:CCD53612.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD53612.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR   EMBL; FQ790347; CCD53612.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2YPR4; -.
DR   SMR; G2YPR4; -.
DR   STRING; 999810.G2YPR4; -.
DR   eggNOG; KOG2832; Eukaryota.
DR   HOGENOM; CLU_023309_0_0_1; -.
DR   InParanoid; G2YPR4; -.
DR   Proteomes; UP000008177; Unplaced contigs.
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:UP000008177};
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          286..429
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   REGION          1..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  63940 MW;  014CF554119B1BE3 CRC64;
     MLSRAIGRSL QTPALRNSST NFRITSSTSW TRSMASNRRQ PKKPTDYNRP SGTPTPSGPA
     GAQAAFTSPK SGLSSDKSGN PDFSKAQDEV SKGASSQRNT VPQSEGGGAG VPNPDARKGE
     SPDFSGKQDE FETIAADPAQ AEFENKPLPD LTQGIPSTLD FELANRKSKA SPLNLTEAAD
     PEEDASGGGK GRGELPASAY VSSSERKRNQ MANYMYLAFF ISAITGTVYM GRNWETEEEE
     KLHAETAPSG WSLTGMWNRV RARTGDQLGH YTEPAFTKLL PDPSPMFERP YTLVLSMEDL
     LIHSEWTREH GWRLAKRPGV DYFLRYLSQY YELVIFTTQP STLAEPVIRK FDPYHIVTWP
     LFREATLYEN GEYIKDLSYL NRDLSKVILI DTKAHHAKKQ PENAIILKPW MGDVQDKELV
     SLIPFLEYIP TMQYADVRKA LKSFEGTHIP TEFAKREAIA RKKFQEQLAE ERKKHGKRGG
     GVGLLGSALG IKPGGMMMTD PNEQSLADAL AQGKMLQDLA RERGQKNYEA FDKEIRENGA
     KWLKEEAEME EKAKEEGLKA MKSGMTGGWW GSSSS
//
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