MTG1_YEAST
ID MTG1_YEAST Reviewed; 367 AA.
AC Q03151; D6VZS0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mitochondrial GTPase 1;
DE Flags: Precursor;
GN Name=MTG1; OrderedLocusNames=YMR097C; ORFNames=YM6543.04C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12808030; DOI=10.1091/mbc.e02-10-0636;
RA Barrientos A., Korr D., Barwell K.J., Sjulsen C., Gajewski C.D.,
RA Manfredi G., Ackerman S., Tzagoloff A.;
RT "MTG1 codes for a conserved protein required for mitochondrial
RT translation.";
RL Mol. Biol. Cell 14:2292-2302(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Mitochondrial GTPase involved in assembly of the large
CC ribosomal subunit (PubMed:12808030). Plays a role in expression of the
CC mitochondrial translational machinery (PubMed:12808030).
CC {ECO:0000269|PubMed:12808030}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12808030, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12808030, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; Z49807; CAA89898.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09994.1; -; Genomic_DNA.
DR PIR; S55083; S55083.
DR RefSeq; NP_013815.1; NM_001182597.1.
DR AlphaFoldDB; Q03151; -.
DR SMR; Q03151; -.
DR BioGRID; 35272; 205.
DR DIP; DIP-4441N; -.
DR IntAct; Q03151; 3.
DR MINT; Q03151; -.
DR STRING; 4932.YMR097C; -.
DR MaxQB; Q03151; -.
DR PaxDb; Q03151; -.
DR PRIDE; Q03151; -.
DR EnsemblFungi; YMR097C_mRNA; YMR097C; YMR097C.
DR GeneID; 855122; -.
DR KEGG; sce:YMR097C; -.
DR SGD; S000004703; MTG1.
DR VEuPathDB; FungiDB:YMR097C; -.
DR eggNOG; KOG2485; Eukaryota.
DR GeneTree; ENSGT00500000044923; -.
DR HOGENOM; CLU_011106_0_1_1; -.
DR InParanoid; Q03151; -.
DR OMA; VYFVGMP; -.
DR BioCyc; YEAST:G3O-32797-MON; -.
DR PRO; PR:Q03151; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03151; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..367
FT /note="Mitochondrial GTPase 1"
FT /id="PRO_0000203287"
FT DOMAIN 42..228
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT BINDING 89..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 160..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 367 AA; 42144 MW; C8FFF830B65A9E49 CRC64;
MHINVRGTRK IISNVSSFTP RYEFPKYSMP LTDFKGHQVK ALKTFEKLLP QMNMIIELRD
IRAPLSTRNV VFDRIARKEH DVMKLVVYTR KDLMPGNKPY IGKLKNWHEE LGEKFILLDC
RNKTDVRNLL KILEWQNYEL ETNGGYLPMG YRALITGMPN VGKSTLINSL RTIFHNQVNM
GRKFKKVAKT GAEAGVTRAT SEVIRVTSRN TESRNEIYLI DTPGIGVPGR VSDHNRMLGL
ALCGSVKNNL VDPIFQADYL LYLMNLQNLN DGRTELYPGS TNSPTNDIYD VLRRLQVNKS
QNEKSTAIEW TNKWRLHGKG IIFDPEVLLN NDEFSYKNYV NDQLEKLGDL SYEGLSNKLK
GNPNQVF
