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IF2P_SULAC
ID   IF2P_SULAC              Reviewed;         602 AA.
AC   P95691; Q4JAV4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Probable translation initiation factor IF-2;
GN   Name=infB; OrderedLocusNames=Saci_0695;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-552.
RA   Keeling P.J., Baldauf S.L., Doolittle W.F., Zillig W., Klenk H.-P.;
RT   "An infB-homologue in Sulfolobus acidocaldarius.";
RL   Syst. Appl. Microbiol. 19:312-321(1996).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000077; AAY80075.1; -; Genomic_DNA.
DR   EMBL; U43413; AAB41057.1; -; Genomic_DNA.
DR   RefSeq; WP_011277577.1; NC_007181.1.
DR   AlphaFoldDB; P95691; -.
DR   SMR; P95691; -.
DR   STRING; 330779.Saci_0695; -.
DR   EnsemblBacteria; AAY80075; AAY80075; Saci_0695.
DR   GeneID; 3472541; -.
DR   KEGG; sai:Saci_0695; -.
DR   PATRIC; fig|330779.12.peg.663; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   Proteomes; UP000001018; 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_0000137307"
FT   DOMAIN          9..229
FT                   /note="tr-type G"
FT   REGION          18..25
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          43..47
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          82..85
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          204..206
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        150
FT                   /note="Y -> H (in Ref. 2; AAB41057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="K -> R (in Ref. 2; AAB41057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200
FT                   /note="I -> V (in Ref. 2; AAB41057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="K -> E (in Ref. 2; AAB41057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        524..534
FT                   /note="VDRASKGMEVA -> LVSCYYERNKP (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   602 AA;  67020 MW;  6EBA0BBB4CD75685 CRC64;
     MTTQVPKRLR QPIVVVLGHV DHGKTTLLDK IRGTAVVKKE PGEMTQEVGA SFVPTSVIEK
     ISEPLKKSFP IKLEIPGLLF IDTPGHELFS NLRKRGGSVA DIAILVVDIV EGIQKQTLES
     IEILKSRKVP FIVAANKIDR INGWKAQDTY SFLESINKQE QRVRDNLDKQ VYNLVIQLAE
     QGFNAERFDR IRDFTKTVAI IPVSAKTGEG IAEVLAILAG LTQNYMKNKL KFAEGPAKGV
     ILEVKELQGL GYTADVVIYE GILRKNDIIV LAGIDGPIVT KVRAILVPRP LQDIKLAKSD
     LAQIDEVYAA SGVKVYAQNL ETALAGSPIY VAENNEEVEK YKKIIQEEVS AVRYYNSSVY
     GIIVKADSLG SLEAIVSSLE RRNIPIRLAD IGPISKRDIT EAEIVAEKAK EYGIIAAFRV
     KPLSGIEIPE KIKLISDDII YQLMDNIEKY IEDIKESEKR KTLETIVLPG KIKIIPGYVF
     RRSDPVIVGV EVLGGIIRPK YGLIKKDGRR VGEVLQIQDN KKSVDRASKG MEVAVSIKGN
     IMVGRQVEEG EVLYTDVPKE DLQILMEKYK DIVTDDMIEV IKEIIRIKRT QDATYGLGLQ
     FQ
 
 
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