ID M7WJ92_RHOT1 Unreviewed; 231 AA.
AC M7WJ92;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=RHTO_07058 {ECO:0000313|EMBL:EMS18086.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18086.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS18086.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS18086.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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; KB722692; EMS18086.1; -; Genomic_DNA.
DR RefSeq; XP_016269205.1; XM_016420717.1.
DR AlphaFoldDB; M7WJ92; -.
DR GeneID; 27371071; -.
DR eggNOG; KOG4149; Eukaryota.
DR HOGENOM; CLU_1001674_0_0_1; -.
DR OrthoDB; 1278at2759; -.
DR Proteomes; UP000016926; 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 Membrane {ECO:0000256|SAM:Phobius};
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..174
FT /note="CHCH"
FT /evidence="ECO:0000259|Pfam:PF06747"
FT REGION 69..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 24887 MW; 6CB83432CDC646A7 CRC64;
MFRASLRAVP RSLPARSYRQ QLRTATTSTA QRRFAVYQSQ TTNSFVYASV GLAALLGWTA
AILTVGGRGS KHGKKDAHAA KKGADAPVAE TATPQPDAAA APSAEEGQAA SQSAAFNPET
GEINWDCPCL GGMADGPCGE EFKAAFSCFV YSEAEPKGIN CVEKFRHMQE CFRKHPDIYG
DEDDDLHEEE EDFDLVSRAE AALALPDQHF LEEAAKEAPT RKEAEAASTL E
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