TIM10_GIBZE
ID TIM10_GIBZE Reviewed; 95 AA.
AC Q4IPZ1; A0A0E0RN84; V6QUE0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM10;
GN Name=TIM10; ORFNames=FGRRES_00717, FGSG_00717;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. Also required for the transfer of beta-
CC barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIM9 and 3 copies of
CC TIM10, named soluble 70 kDa complex. Associates directly with the TIM22
CC complex, whose core is composed of TIM22 and TIM54. Interacts with the
CC transmembrane regions of multi-pass transmembrane proteins in transit
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}.
CC -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC 2 disulfide bonds in the mitochondrial intermembrane space. However,
CC during the transit of TIM10 from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; DS231663; ESU05938.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF72709.1; -; Genomic_DNA.
DR RefSeq; XP_011316423.1; XM_011318121.1.
DR AlphaFoldDB; Q4IPZ1; -.
DR SMR; Q4IPZ1; -.
DR STRING; 5518.FGSG_00717P0; -.
DR EnsemblFungi; ESU05938; ESU05938; FGSG_00717.
DR GeneID; 23548194; -.
DR KEGG; fgr:FGSG_00717; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G01817; -.
DR eggNOG; KOG3480; Eukaryota.
DR HOGENOM; CLU_162151_1_0_1; -.
DR InParanoid; Q4IPZ1; -.
DR PHI-base; PHI:1564; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IEA:InterPro.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR027100; Tim10.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR PANTHER; PTHR11038:SF16; PTHR11038:SF16; 1.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 3: Inferred from homology;
KW Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..95
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM10"
FT /id="PRO_0000228063"
FT MOTIF 38..63
FT /note="Twin CX3C motif"
FT DISULFID 38..63
FT /evidence="ECO:0000250"
FT DISULFID 42..59
FT /evidence="ECO:0000250"
SQ SEQUENCE 95 AA; 10504 MW; 88E1E97DE89BD629 CRC64;
MSFLGMGRPQ PTSEQKIAAV ESEMRMMADT YNRLQQSCQK KCVPNDYREG ELNKGESVCL
DRCTAKFLDT SMKVSEIMQQ QGQALGGQQG GGGMF
