ID   IF2P_HALMA              Reviewed;         601 AA.
AC   Q5UXU6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=rrnAC3203;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV47907.1; -; Genomic_DNA.
DR   RefSeq; WP_007189198.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UXU6; -.
DR   SMR; Q5UXU6; -.
DR   STRING; 272569.rrnAC3203; -.
DR   EnsemblBacteria; AAV47907; AAV47907; rrnAC3203.
DR   GeneID; 40154007; -.
DR   KEGG; hma:rrnAC3203; -.
DR   PATRIC; fig|272569.17.peg.3741; -.
DR   eggNOG; arCOG01560; Archaea.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   Proteomes; UP000001169; Chromosome I.
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..601
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_0000137299"
FT   DOMAIN          14..229
FT                   /note="tr-type G"
FT   REGION          23..30
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          48..52
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          85..88
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          139..142
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          207..209
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         23..30
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   601 AA;  65745 MW;  456314187D1BC5B2 CRC64;
     MSDTDPTTAT DDTLRTPIVA VLGHVDHGKT SLLDKIRGSA VTAGESGAIT QHIGATAVPL
     DVISEIAGDL VDPTDFDLPG LLFIDTPGHH SFSTLRSRGG ALADIAILVV DVNDGFQPQT
     LEAIDILKRT QTPFIVAANK IDTVPGWNPN EGQPVQQTMD AQSDRVQSDL NEKLYEIIGE
     LSDNGFSADM YWRVQNFQAN IGVVPVSAET SEGIPDLLTV MMGLSQRYMK EEMEIDTSGP
     GVGTVLEVKD TQGFGTTLDA IIYDGTIRND DTIVVGGLQG PIITDVRALL RPRPLEEIRT
     EQEFEQVDEV AAADGVKIAA PELGDAMAGA PIRVIRDRDR SEVIAEVEEE LAEIEVTTQE
     EGVVIKADTL GSLEALSSTL EEEEIPVMRA EVGAVAPRDV RVAETAGEST NQAILAFSVD
     VLDDARDLAE QEDVKLFEDD VIYQLVESYD DHVTAIEEAQ QEQILENITR PAKFRILQDH
     TFRQSDPAVV GVEILSGELR RNVNVVRWEN GEANRVGTLK TIQDEGEDVD SARAGERMAV
     SIQGPTVGRQ VEEGDDLWVE IPEKHAKILE QELKEDISVD EREALSMYLE KHRNRDPFWG
     K