TIM50_DEBHA
ID TIM50_DEBHA Reviewed; 471 AA.
AC Q6BVY9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE Flags: Precursor;
GN Name=TIM50; OrderedLocusNames=DEHA2B15642g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Essential component of the TIM23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane. Required to direct preproteins
CC in transit and direct them to the channel protein TIM23, and possibly
CC facilitates transfer of the translocating proteins from the TOM complex
CC to the TIM23 complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the TIM23 complex, at least composed of TIM23,
CC TIM17, TIM50 and TIM21. Interacts with preproteins in transit (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TIM50 family. {ECO:0000305}.
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DR EMBL; CR382134; CAG85644.1; -; Genomic_DNA.
DR RefSeq; XP_457630.1; XM_457630.1.
DR AlphaFoldDB; Q6BVY9; -.
DR SMR; Q6BVY9; -.
DR STRING; 4959.XP_457630.1; -.
DR EnsemblFungi; CAG85644; CAG85644; DEHA2B15642g.
DR GeneID; 2913605; -.
DR KEGG; dha:DEHA2B15642g; -.
DR VEuPathDB; FungiDB:DEHA2B15642g; -.
DR eggNOG; KOG2832; Eukaryota.
DR HOGENOM; CLU_023309_1_2_1; -.
DR InParanoid; Q6BVY9; -.
DR OMA; LGRNWDT; -.
DR OrthoDB; 1142452at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027111; Tim50.
DR PANTHER; PTHR12210:SF3; PTHR12210:SF3; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW Reference proteome; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..104
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 105..471
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM50"
FT /id="PRO_0000043130"
FT TOPO_DOM 105..110
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..471
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 185..328
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 29..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 54195 MW; 255F18EF824D58B5 CRC64;
MLRNTRLLTR TISSSLRFAA TKNTRLPTQH KFYSKKTDKK AEEPQSILTD DLLAKAGFED
PNEPKEKSEQ QESENGEPSE EEKSNGQEQR SRRKRRAQTS KDIQRERYAN MFYLATLVGG
IAGVGYMCRD WDSEDEQTKL EGKDIDNGFA PNLMYGRLNK RLGSLFTFFS EPVFENLLPP
PAPEAYRRPL TLVVTLDDLL IHSDWDTKHG WRTGKRPGLD YFLGYLSQYY EIVIFGSNYQ
MYSENTVGKL DPFHAYVSYA LFREACRYKD GKLVKDLSLL NRDLGKTVLI DVEEDSWSMQ
PDNAIPMKPW DGSYDDTLVK LIPFLEYLAT QPVKDVRPIL NSFKDKSNIV QEFAEREAKL
REQWKKDNKH LFDSANRPNA GNFLASLMGV PTSSVNKEPK MPLDIIREHG QLQYEHFQKY
LKENAPKFLE EEQKLKDEFG KVSLNKLITE GAPSADDIAK VQAERAAAQQ Q
