MTG2_YEAST
ID MTG2_YEAST Reviewed; 518 AA.
AC P38860; D3DLB7; Q6DUF2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=GTPase MTG2, mitochondrial;
DE AltName: Full=Mitochondrial GTPase 2;
DE Flags: Precursor;
GN Name=MTG2; OrderedLocusNames=YHR168W;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RC STRAIN=CRY1;
RX PubMed=15591131; DOI=10.1091/mbc.e04-07-0622;
RA Datta K., Fuentes J.L., Maddock J.R.;
RT "The yeast GTPase Mtg2p is required for mitochondrial translation and
RT partially suppresses an rRNA methyltransferase mutant, mrm2.";
RL Mol. Biol. Cell 16:954-963(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 498.
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 [4]
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).
CC -!- FUNCTION: Required for mitochondrial protein synthesis. May be involved
CC in mitochondrial ribosome biogenesis. {ECO:0000269|PubMed:15591131}.
CC -!- SUBUNIT: Interacts with the mitochondrial 54S large ribosomal subunit.
CC {ECO:0000269|PubMed:15591131}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15591131}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15591131}; Matrix side
CC {ECO:0000269|PubMed:15591131}.
CC -!- MISCELLANEOUS: Present with 189 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|PROSITE-ProRule:PRU01047}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68013.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY643812; AAT65075.1; -; Genomic_DNA.
DR EMBL; U00027; AAB68013.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006934; DAA06861.2; -; Genomic_DNA.
DR PIR; S48907; S48907.
DR RefSeq; NP_012038.2; NM_001179299.2.
DR AlphaFoldDB; P38860; -.
DR SMR; P38860; -.
DR BioGRID; 36602; 74.
DR DIP; DIP-3928N; -.
DR IntAct; P38860; 1.
DR STRING; 4932.YHR168W; -.
DR MaxQB; P38860; -.
DR PaxDb; P38860; -.
DR PRIDE; P38860; -.
DR EnsemblFungi; YHR168W_mRNA; YHR168W; YHR168W.
DR GeneID; 856573; -.
DR KEGG; sce:YHR168W; -.
DR SGD; S000001211; MTG2.
DR VEuPathDB; FungiDB:YHR168W; -.
DR eggNOG; KOG1489; Eukaryota.
DR GeneTree; ENSGT00940000157379; -.
DR HOGENOM; CLU_011747_2_6_1; -.
DR InParanoid; P38860; -.
DR OMA; PRVGHWE; -.
DR BioCyc; YEAST:G3O-31202-MON; -.
DR PRO; PR:P38860; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38860; protein.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR CDD; cd01898; Obg; 1.
DR Gene3D; 2.70.210.12; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR InterPro; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF01018; GTP1_OBG; 2.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..518
FT /note="GTPase MTG2, mitochondrial"
FT /id="PRO_0000122468"
FT DOMAIN 89..339
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 340..512
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 346..353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 394..398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 460..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
SQ SEQUENCE 518 AA; 57847 MW; 191FCDBA5294B107 CRC64;
MSIAWSSVFK RELRLERFLP RVYSTKVPDN APRAADNEQW LETLRPITHP EQKKSDHDVS
YTRHINVPLG EVTSVNYLQR YNKHKHSQGN FVDVRIVKCK SGAGGSGAVS FFRDAGRSIG
PPDGGDGGAG GSVYIQAVAG LGSLAKMKTT YTAEDGEAGA ARQLDGMRGR DVLIQVPVGT
VVKWCLPPQK VRELVEREMR KDNNATLRSI LGSTAVNLSV SSGSHRKKIQ LYRHEMAESW
LFKDKAKEYH ENKDWFKDLH KKMEAYDHSL EQSELFNDQF PLAGLDLNQP MTKPVCLLKG
GQGGLGNMHF LTNLIRNPRF SKPGRNGLEQ HFLFELKSIA DLGLIGLPNA GKSTILNKIS
NAKPKIGHWQ FTTLSPTIGT VSLGFGQDVF TVADIPGIIQ GASLDKGMGL EFLRHIERSN
GWVFVLDLSN KNPLNDLQLL IEEVGTLEKV KTKNILIVCN KVDIDAEKSE SFAKYLQVEK
FSKSQEWDCV PISALREENI DVLKKKMFKC ARQSEFDK
