IF2M_YEAST
ID IF2M_YEAST Reviewed; 676 AA.
AC P25038; D6W242; Q12693;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial;
DE Short=IF-2(Mt);
DE Short=IF-2Mt;
DE Short=IF2(mt);
DE Flags: Precursor;
GN Name=IFM1; OrderedLocusNames=YOL023W;
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].
RX PubMed=1935960; DOI=10.1111/j.1432-1033.1991.tb16325.x;
RA Vambutas A., Ackerman S.H., Tzagoloff A.;
RT "Mitochondrial translational-initiation and elongation factors in
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 201:643-652(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [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: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; X58379; CAA41268.1; -; Genomic_DNA.
DR EMBL; Z74765; CAA99023.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10758.1; -; Genomic_DNA.
DR PIR; S66706; S66706.
DR RefSeq; NP_014619.1; NM_001183277.1.
DR AlphaFoldDB; P25038; -.
DR SMR; P25038; -.
DR BioGRID; 34378; 291.
DR STRING; 4932.YOL023W; -.
DR MaxQB; P25038; -.
DR PaxDb; P25038; -.
DR PRIDE; P25038; -.
DR EnsemblFungi; YOL023W_mRNA; YOL023W; YOL023W.
DR GeneID; 854135; -.
DR KEGG; sce:YOL023W; -.
DR SGD; S000005383; IFM1.
DR VEuPathDB; FungiDB:YOL023W; -.
DR eggNOG; KOG1145; Eukaryota.
DR GeneTree; ENSGT00940000162583; -.
DR HOGENOM; CLU_006301_10_2_1; -.
DR InParanoid; P25038; -.
DR OMA; NRDNRTG; -.
DR BioCyc; YEAST:G3O-33439-MON; -.
DR PRO; PR:P25038; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P25038; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IMP: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; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR GO; GO:0070124; P:mitochondrial translational initiation; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; ISA:SGD.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Initiation factor; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..676
FT /note="Translation initiation factor IF-2, mitochondrial"
FT /id="PRO_0000014483"
FT DOMAIN 143..326
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 152..159
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 177..181
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 200..203
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 254..257
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 296..298
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 152..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 200..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254..257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 462
FT /note="H -> Y (in Ref. 1; CAA41268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 75657 MW; 947591278A31CB12 CRC64;
MLRRHGLFWL KTCPRLNVLL NQSIPIPHLL HSRDICQQRW YAKGKRRNQI SKKELKPLNF
SIPNYISVNK LANLLNCRVE RLIKDLTALG FENITTTYIL SKEYVELILQ EYNFALPNLS
TSTNLDNVYD ELKSPVNPKL LTKRAPVVTI MGHVDHGKTT IIDYLRKSSV VAQEHGGITQ
HIGAFQITAP KSGKKITFLD TPGHAAFLKM RERGANITDI IVLVVSVEDS LMPQTLEAIK
HAKNSGNEMI IAITKIDRIP QPKEREKKIE KVINDLIVQG IPVEKIGGDV QVIPISAKTG
ENMDLLEESI VLLSEVMDIR AENSPKTIAE GWIIESQVKK QVGNVATVLV KKGTLQKGKI
LICGNTFCKI KNLIDDKGIP ILKATPSYAT EVLGWKDVPH VGDEVIQVKS EAIAKKFISK
RQDLIEVQKN SSIVEKLNEE RALAKEQHLN KELEHENTVQ EHEQNTGPKL INYIIKCDVS
GSAEAVSESI SSLGNDEVRC NVISSSVGIP TESDLKMAQI TESTILCFNL GNLPSEVINN
RAGIKIKQYN VIYKLIEDVT ETLTENLKPI FEKKIVSTVD VRETFDFRLK KKIIRIAGCK
VNNGVIKKNS LVQVVRGPNE DVIFDGKIST LKHNKDDVAE VSKGHECGIT FESGFEGFKP
GDKILVYENV RVPRYL
