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Database: UniProt
Entry: A0A1L9S3S9_ASPWE
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ID   A0A1L9S3S9_ASPWE        Unreviewed;       264 AA.
AC   A0A1L9S3S9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-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=ASPWEDRAFT_101341 {ECO:0000313|EMBL:OJJ41804.1};
OS   Aspergillus wentii DTO 134E9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Cremei.
OX   NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ41804.1, ECO:0000313|Proteomes:UP000184383};
RN   [1] {ECO:0000313|Proteomes:UP000184383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(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}.
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DR   EMBL; KV878209; OJJ41804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9S3S9; -.
DR   STRING; 1073089.A0A1L9S3S9; -.
DR   VEuPathDB; FungiDB:ASPWEDRAFT_101341; -.
DR   OrthoDB; 1278at2759; -.
DR   Proteomes; UP000184383; 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; AU015836 PROTEIN-RELATED; 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:UP000184383};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          167..203
FT                   /note="CHCH"
FT                   /evidence="ECO:0000259|Pfam:PF06747"
FT   REGION          73..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  28498 MW;  B1C40FA14A8899B9 CRC64;
     MFRPASRALL RAPGVAARGP AGKRLISTTP SEPKSRSWKN TAVRFGLAIG AIYYYNTSSA
     FAKEPTFSFR SQNQTESVDE SSLPTLESVK SKIREREQKV AAPKAPETEV QPAADEQAQL
     SIESGEGAVK SPQELEEEAG QEAAFNPETG EINWDCPCLG GMAHGPCGED FKAAFSCFVF
     SEDEPKGIDC IDKFKAMQDC FRQHPEIYGA ELEDDEAPPA PEGQQAIEEP APAAQTEAAS
     NPETTAIPKE SHDTESKNEA PKSS
//
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