ID   IF2P_METBF              Reviewed;         591 AA.
AC   Q466D5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=Mbar_A3384;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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}.
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; CP000099; AAZ72257.1; -; Genomic_DNA.
DR   RefSeq; WP_011308296.1; NC_007355.1.
DR   AlphaFoldDB; Q466D5; -.
DR   SMR; Q466D5; -.
DR   STRING; 269797.Mbar_A3384; -.
DR   EnsemblBacteria; AAZ72257; AAZ72257; Mbar_A3384.
DR   GeneID; 3624821; -.
DR   KEGG; mba:Mbar_A3384; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   OrthoDB; 17053at2157; -.
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.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..591
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_0000228266"
FT   DOMAIN          7..223
FT                   /note="tr-type G"
FT   REGION          16..23
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          41..45
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          78..81
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          132..135
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          200..202
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         78..82
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         132..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   591 AA;  64938 MW;  DBE03A08D9B911BB CRC64;
     MADKKNLRTP IVCVMGHVDH GKTTLLDKIR GTAIVSGEAG AITQHIGATE VPIDVIINKL
     GDPRLRDRFI VPGLLFIDTP GHHAFTTLRS RGGALADLAI VVVDINEGFK PQTYESLQIL
     KRFKTPFVVV ANKIDRIGGW VSQKDLPFAV TFKKQSEDVQ ARLETKLYEV IGELYNQGFA
     AERYDRVTNF QKTLGVVPVS AMTGEGIPDV LMVLLGLAQK FLEANLHYSA KGPGVGTVLE
     VKEEKGLGAT LDVILYDGTL KKGDTVVIGS LGKPIQTKVR ALLKPRELSE MRYESKFKQV
     NKVTAAVGVK ISAPGLEGAL AGSPIRVANE DTLDEIVDQI KSEIDEVRID TGAVGIMIKA
     DTLGSLEALV HEFQKDEVSI RKAEVGDISH RDAIEASTVE DPLYSVIIGF NVKVHPDARD
     FLQESTVKVF TSDVIYRLVE DYQKYVKEQQ EQAEKRIFET IIRPGKFKIL PGCIFRQSKP
     AVVGIRVLGG VVRTNADVML ENGNVVGKIK GLQIEGENIP SAGVGKEVAM AIEGATVGRQ
     IKEEDVLYVN VPERHAKVLE HEIYDSLSTD EKETLDIFLS LKRKDNPFWA K