IF2P_SULTO
ID IF2P_SULTO Reviewed; 602 AA.
AC Q976A1;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=STK_02790;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
CC -!- FUNCTION: Function in general translation initiation by promoting the
CC binding of the formylmethionine-tRNA to ribosomes. Seems to function
CC along with eIF-2. {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}.
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DR EMBL; BA000023; BAB65247.1; -; Genomic_DNA.
DR RefSeq; WP_010978230.1; NC_003106.2.
DR AlphaFoldDB; Q976A1; -.
DR SMR; Q976A1; -.
DR STRING; 273063.STK_02790; -.
DR EnsemblBacteria; BAB65247; BAB65247; STK_02790.
DR GeneID; 1458181; -.
DR KEGG; sto:STK_02790; -.
DR PATRIC; fig|273063.9.peg.331; -.
DR eggNOG; arCOG01560; Archaea.
DR OMA; FRQSKPA; -.
DR OrthoDB; 17053at2157; -.
DR Proteomes; UP000001015; Chromosome.
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 Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_A; IF_2_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR004544; TF_aIF-2_arc.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00491; aIF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..602
FT /note="Probable translation initiation factor IF-2"
FT /id="PRO_0000137309"
FT DOMAIN 10..227
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 44..48
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 83..86
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 137..140
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 205..207
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 602 AA; 67130 MW; 99E13842DF30BDC6 CRC64;
MSQQLQSRRL RQPIVVVLGH VDHGKTTLLD KIRGTAVVKK EPGEMTQEVG ASFVPTSVIE
KIAEPLKKTF PIKLEIPGLL FIDTPGHELF SNLRRRGGSV ADIAILVVDV VEGFQKQTYE
SLEILRSRKV PFLVAANKID RIPGWKPIDT YSFLESIKSQ RKDVQTQLDN YVYRLVGQLA
ELGFNADRFD RIRDFTKTVA IVPVSAKTGE GIAELLALLA GLTQNYMKTK LRFAEGPAKG
VILEVKELQG LGYTIDVIIY DGILKKNDTI IIGGLNGPIV TKVRSILVPK PLQDIKVVKT
DLTQIDEVYA AAGVKIYAPE LENALAGSPL FVAENEQQIE EYKKIIQEEI ASVKYYNANI
AGIVVKADSL GSLEAIVEGL KQKNIPIRLA DIGPITKKDI TEAELTLQEA KEYGIIAAFR
VKPLQGIEVP NNIKLIYSEI IYQLIDDIEK YITEVRESEK RRTLDSLILP GKFRLIPGYV
FRRSDPVIVG VEVLGGIIRP KFPVMKKDGK RVGEILQIQD NKKSVDRATK GMEVAVSIKG
NIMVGRQIDE GEILYTDVPK EDLEILLTKY KDIITDDMKE VIKEIINIKR VNDPTYALGL
KV