ID A7TLH4_VANPO Unreviewed; 684 AA.
AC A7TLH4;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=Kpol_1024p13 {ECO:0000313|EMBL:EDO16860.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO16860.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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. {ECO:0000256|ARBA:ARBA00025162}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733}.
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DR EMBL; DS480415; EDO16860.1; -; Genomic_DNA.
DR RefSeq; XP_001644718.1; XM_001644668.1.
DR AlphaFoldDB; A7TLH4; -.
DR STRING; 436907.A7TLH4; -.
DR GeneID; 5545043; -.
DR KEGG; vpo:Kpol_1024p13; -.
DR eggNOG; KOG1145; Eukaryota.
DR HOGENOM; CLU_006301_10_2_1; -.
DR InParanoid; A7TLH4; -.
DR OMA; RYYNVIY; -.
DR OrthoDB; 169393at2759; -.
DR PhylomeDB; A7TLH4; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF20; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT DOMAIN 147..326
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 684 AA; 76452 MW; 2C7D279F0B125CA3 CRC64;
MWKRSTPQIF SILRGRATKS CPLITISSPV WTRSISYSNV IQAPKGNRGK KTKKSSEKPK
PVNFIIPNYL SVDKLSNLLN CRVTDLIKDL GKLGFKDVTN KYILTKEYIE LILQEYNYEL
PNSNLELNSS NVYDSLKQAA NPNNLEKRPP VVTIMGHIDH GKTTIIDHLR KSSVVDQEHG
GITQHIGAFQ VITPISKKKI TFLDTPGHAA FLKMRERGAN ITDIIILVVS IEDSIMPQTI
EAIKHIKNSG NELIVAITKI DKATTPRERE RMLEKVTNDL IAQEIPVEKI GGDVQVIPIS
ARTGENMDLL EESIIALSDL MDIRSENSKS TMVEGWVLES QVKKMMGNVG TVLVKKGTLR
KGDILVCGNT YCKVKNMLTE SHNQTNEALP SQAITVLGWK DLPIAGDEVI QVPNESIAKK
SISRRLTLIK SENDMQTVLK LNEQNAQEKL EKEKNDIDED EDEDDIDEHV VEETGPKKIN
FIIKADVSGS AEAIKDSLTG LGNNEVESYI VSTSVGNPNE SDLKMAKITD SKILCFNLGS
LPSDIVNNKE GIEIRQYNVI YKLIEDVTEI LTNNLAPIYE NKNTATVEIR EIFNYSLKKK
QLKVAGCKVI NGKITRNSLV KVVRGDEQNQ VYDGRLSTLK QGKDDTAEVS KGKECGITFQ
KNFDSYQPGD KIIAYEKVKV QRYL
//
