ID   A0A136IW33_9PEZI        Unreviewed;       340 AA.
AC   A0A136IW33;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Mitochondrial intermembrane space import and assembly protein 40 {ECO:0000256|ARBA:ARBA00013714};
DE   AltName: Full=Mitochondrial import inner membrane translocase TIM40 {ECO:0000256|ARBA:ARBA00033150};
GN   ORFNames=Micbo1qcDRAFT_235454 {ECO:0000313|EMBL:KXJ89111.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ89111.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the import and folding of small cysteine-
CC       containing proteins (small Tim) in the mitochondrial intermembrane
CC       space (IMS). Forms a redox cycle with ERV1 that involves a disulfide
CC       relay system. Precursor proteins to be imported into the IMS are
CC       translocated in their reduced form into the mitochondria. The oxidized
CC       form of MIA40 forms a transient intermolecular disulfide bridge with
CC       the reduced precursor protein, resulting in oxidation of the precursor
CC       protein that now contains an intramolecular disulfide bond and is able
CC       to undergo folding in the IMS. {ECO:0000256|ARBA:ARBA00024980}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004164}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004164}; Intermembrane side
CC       {ECO:0000256|ARBA:ARBA00004164}.
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DR   EMBL; KQ964256; KXJ89111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136IW33; -.
DR   STRING; 196109.A0A136IW33; -.
DR   InParanoid; A0A136IW33; -.
DR   OrthoDB; 1278at2759; -.
DR   Proteomes; UP000070501; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IEA:InterPro.
DR   Gene3D; 1.10.287.2900; -; 1.
DR   InterPro; IPR010625; CHCH.
DR   InterPro; IPR039289; CHCHD4.
DR   PANTHER; PTHR21622:SF0; CHCH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR21622; COILED-COIL-HELIX-COILED-COIL-HELIX DOMAIN CONTAINING 4; 1.
DR   Pfam; PF06747; CHCH; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          179..214
FT                   /note="CHCH"
FT                   /evidence="ECO:0000259|Pfam:PF06747"
FT   REGION          98..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   340 AA;  35545 MW;  75E93379BE86F80A CRC64;
     MYRSALRATP RIPHAVRSST LRSAAPRRFA STVPADKSRS WKSSAARWGL AIGALYYYNT
     STAFAEEPQS STIPVPAHFS DDDMPTVDAI VAQKRKEAEA RQLKAASDAT AKSSAPATTQ
     ATHDESAAAA PPSSSSPPPA AGSPEALEAE ANQQGAFNPE TGEINWDCPC LGGMADGPCG
     EDFKAAFSCF VYSTEEPKGM DCIDKFQAMQ DCFRLHPEIY GEELADAEDA GEDAPSSEEP
     AELDAAKPSP KAADVSARTA NGDSNTKDAA NTPADDPAPS ATKPAGKPTE KASKKPAEKA
     AEKAAEPVLT PAQTPTGSLA QESDEAKRDP RFDATSAPAK
//