IF2_VESOH
ID IF2_VESOH Reviewed; 815 AA.
AC A5CXX6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=COSY_0059;
OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Vesicomyosocius.
OX NCBI_TaxID=412965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA;
RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA Kato C., Kitagawa M., Kato I., Maruyama T.;
RT "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT clam, Calyptogena okutanii.";
RL Curr. Biol. 17:881-886(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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009247; BAF61196.1; -; Genomic_DNA.
DR RefSeq; WP_011929466.1; NC_009465.1.
DR AlphaFoldDB; A5CXX6; -.
DR SMR; A5CXX6; -.
DR STRING; 412965.COSY_0059; -.
DR PRIDE; A5CXX6; -.
DR EnsemblBacteria; BAF61196; BAF61196; COSY_0059.
DR KEGG; vok:COSY_0059; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 139681at2; -.
DR Proteomes; UP000000247; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..815
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335519"
FT DOMAIN 315..482
FT /note="tr-type G"
FT REGION 153..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..331
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 349..353
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 370..373
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 424..427
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 460..462
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 153..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 324..331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 370..374
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 424..427
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 815 AA; 89129 MW; 0E3695EA9A4A63F8 CRC64;
MAHTVQTLSK LLKKTPDEVV TILANAGVDG KNSDSVISAE ERKILMSSLS KRPIRRSSMS
VFRKAGTKSN AVSVSDVKVK VRSKRLTQPI TMIDEQSKVV ANEMARAALA ALDAGRNADE
ILLAQDARRL EMVRLQKAQV EVVEIQKETV KKVQEKEAEK KVEKLKTADK PKEGNKPKRL
RNTSSDNNTR KQLHVARHNP NRRLKKKDRT HLSQKIQAEQ AQHAFQKPIE KVIHEVAIVG
NIKVTELAQK MATKAGEVLK VLMGMGVMVT LNDVIDQDTA LLVVEEMGHK GIISVEETIE
DVLIEQLKYN EHESARPPIV TIMGHVDHGK TSLLDYIRQA KVAHGEVGGI TQHIGAYQVQ
SNGNIITFID TPGHAAFSKM RFRGANVTDI VILVVAADDG VMPQTIESIK HTQIVGVPMI
VAINKIDKEG TDVDKIKQVL STYDVISEDW GGDVIMVPVS AHTGEGVDAL LDAISLTAEI
LEFSAVSEGP AHGTVLEARL EKGRGKVTTI LVQSGTLNKG DIMIAGFEYG KVKQIVDDKG
KILKLAMPSM PVEVLGLSGV PNSGDEVIVV GSERKAREVA DFRKSKDREV QLQKQQASKM
ENFLMKMEKG DISTVNVLLK ADVRGSAQAL IEALEELSTD EVRVKVVSSG VGGINNTDIT
LAATSSALVL GFNVRADAVA RKTADNEGVR VEYYSIIYNL INDVKAIMSG LLSPELSENI
IGIASVKNIF KSQKMGDIAG CMVDEGMVKR DSLIRVLRDS VVIFDGKLES LRRFKDDVNE
VKSGTECGIG VLNYTDVQPG DQIEIFERVE RARIL
