IF2P_HALSA
ID IF2P_HALSA Reviewed; 600 AA.
AC Q9HNQ2; O93625;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; Synonyms=hif2;
GN OrderedLocusNames=VNG_1997G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A9;
RX PubMed=9818089; DOI=10.1080/15216549800204022;
RA Hasegawa Y., Sawaoka N., Kado N., Ochi M., Itoh T.;
RT "Cloning and sequencing of the homologues of both the bacterial and
RT eukaryotic initiation factor genes (hIF-2 and heIF-2gamma) from archaeal
RT Halobacterium halobium.";
RL Biochem. Mol. Biol. Int. 46:495-507(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AB015763; BAA35081.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG20168.1; -; Genomic_DNA.
DR PIR; D84350; D84350.
DR PIR; T43849; T43849.
DR RefSeq; WP_010903469.1; NC_002607.1.
DR AlphaFoldDB; Q9HNQ2; -.
DR SMR; Q9HNQ2; -.
DR STRING; 64091.VNG_1997G; -.
DR PaxDb; Q9HNQ2; -.
DR PRIDE; Q9HNQ2; -.
DR EnsemblBacteria; AAG20168; AAG20168; VNG_1997G.
DR GeneID; 5953198; -.
DR GeneID; 62887326; -.
DR KEGG; hal:VNG_1997G; -.
DR PATRIC; fig|64091.14.peg.1525; -.
DR HOGENOM; CLU_002656_3_3_2; -.
DR InParanoid; Q9HNQ2; -.
DR OMA; FRQSKPA; -.
DR OrthoDB; 17053at2157; -.
DR PhylomeDB; Q9HNQ2; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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..600
FT /note="Probable translation initiation factor IF-2"
FT /id="PRO_0000137300"
FT DOMAIN 13..228
FT /note="tr-type G"
FT REGION 22..29
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 47..51
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 84..87
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 138..141
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 140..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..208
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 84..88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT CONFLICT 59..68
FT /note="LDTVSEVAGS -> AGHRLGGRRQ (in Ref. 1; BAA35081)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..97
FT /note="STLRSR -> FEHALG (in Ref. 1; BAA35081)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..114
FT /note="DG -> ER (in Ref. 1; BAA35081)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..164
FT /note="DR -> EP (in Ref. 1; BAA35081)"
FT /evidence="ECO:0000305"
FT CONFLICT 330..334
FT /note="PIRVV -> RSAWS (in Ref. 1; BAA35081)"
FT /evidence="ECO:0000305"
FT CONFLICT 580..600
FT /note="EREALKSYLDIMRKRDPFWGK -> GARR (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 64430 MW; 3D356AF39F01F5C9 CRC64;
MPDADTTDDP GDLRTPIVAV LGHVDHGKTS LLDKIRGSAV IEGEAGAITQ HIGATAVPLD
TVSEVAGSLV DPTEFDLPGL LFIDTPGHHS FSTLRSRGGA LADIAILVVD VNDGFQPQTE
EAIRILKDTG TPFVVAANKI DTTPGWNPNP DAPVQGTYDD QSDRVRSDLD DALYELIGEM
SDAGFSSDLY WRVQNFQKNV GVIPVSAETG EGVPDLLTVL MGLAQRYMKS EMEVTIDGPG
AGTVLEVKDE QGFGTTVDVI LYDGTIRSGD TVVVGAQPEP IVTDVRALLK PGDLAEMRTE
KRFGNVDRMQ AAAGLKVAAP DLDDAMAGAP IRVVGDRDVA DVVTEVEAEL AEVAVETGEE
GIVVKADTLG SLEALVSALE EAEIPVMSAE VGDVAPRDVA MATTVDSEKH RVLLGFNVDV
LPAAAENAER ESVRVFNSDV IYQLVEDYEA FVDAQEREQK EAVFDNIVRP ARFRILKDHV
FRQNDPAVVG VEVVSGTLKR NTPVGGIEGN DLDRAGIVKG IQDQGEDVDE ARAGNRVSVS
IDGPTVGRDI KEGDELWVDL PEKHAKVLDQ ELTSDLPADE REALKSYLDI MRKRDPFWGK
