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Database: UniProt
Entry: C5PBS5_COCP7
LinkDB: C5PBS5_COCP7
Original site: C5PBS5_COCP7 
ID   C5PBS5_COCP7            Unreviewed;       295 AA.
AC   C5PBS5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=CPC735_065020 {ECO:0000313|EMBL:EER25402.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER25402.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER25402.1, ECO:0000313|Proteomes:UP000009084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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:EER25402.1}.
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DR   EMBL; ACFW01000041; EER25402.1; -; Genomic_DNA.
DR   RefSeq; XP_003067547.1; XM_003067501.1.
DR   AlphaFoldDB; C5PBS5; -.
DR   GeneID; 9693030; -.
DR   KEGG; cpw:CPC735_065020; -.
DR   VEuPathDB; FungiDB:CPC735_065020; -.
DR   HOGENOM; CLU_054990_0_0_1; -.
DR   OrthoDB; 1278at2759; -.
DR   Proteomes; UP000009084; 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   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          185..220
FT                   /note="CHCH"
FT                   /evidence="ECO:0000259|Pfam:PF06747"
FT   REGION          72..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  32412 MW;  6BA53AECFF959BB8 CRC64;
     MFRSASRTVL RQTHRLRLAQ RQAGRRFVST VPPSQKSRSW KSTVARWGLA AAAVYYYNTS
     TVFAEQPSLA LKPASESEDE ESSLPTIESV AAAKKRKSAS RTPAPSSPPS PKSDSKPEES
     SEPPAPELSG AITETEESAP ADVQPLQLSA SELEQEADQE GAFNPETGEI NWDCPCLGGM
     AHGPCGPEFR EAFSCFVYST EEPKGMDCID KFKNMQDCFR LHPDVYGSEL EEDEVDEQLK
     EHIAAEEAQK SQSLSDAPVD AAVAESQENR ETELEKIQQI PVTEEKITKD KASEQ
//
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