ID   A0A1V6RCD5_9EURO        Unreviewed;       277 AA.
AC   A0A1V6RCD5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=PENSOL_c008G03126 {ECO:0000313|EMBL:OQD98842.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD98842.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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}.
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:OQD98842.1}.
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DR   EMBL; MDYO01000008; OQD98842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6RCD5; -.
DR   STRING; 60172.A0A1V6RCD5; -.
DR   OrthoDB; 1278at2759; -.
DR   Proteomes; UP000191612; 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:UP000191612};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          149..185
FT                   /note="CHCH"
FT                   /evidence="ECO:0000259|Pfam:PF06747"
FT   REGION          193..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..277
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   277 AA;  29805 MW;  1EF5522BCC802E8E CRC64;
     MFRPAARALA RAPTVAARTP ANRRLISTGP TKSRSWKNTF LRLGLAGGAI YYYNTSSVFS
     EEPKFSILSS IRKQTGDDAN PQTLDSITPK IREERAAAQS QKSESAALEG GLNPQELQEE
     AGQEAAFNPE TGEINWDCPC LGGMAHGPCG EDFKAAFSCF VYSEEEPKGI DCVDKFKAMQ
     DCFRQHPEVY GAELEDDDEP QPQSDAPAPS EAPAIPEVTP TAAEVDASSP PTEKQTRAKE
     VTQVKAETAA AGENPEGDSL IPKAAHDTEE KNEATKA
//