IF2P_NATPD
ID IF2P_NATPD Reviewed; 602 AA.
AC Q3IMS5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=NP_4982A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI50582.1; -; Genomic_DNA.
DR RefSeq; WP_011324193.1; NC_007426.1.
DR AlphaFoldDB; Q3IMS5; -.
DR SMR; Q3IMS5; -.
DR STRING; 348780.NP_4982A; -.
DR PRIDE; Q3IMS5; -.
DR EnsemblBacteria; CAI50582; CAI50582; NP_4982A.
DR GeneID; 3703271; -.
DR KEGG; nph:NP_4982A; -.
DR eggNOG; arCOG01560; Archaea.
DR HOGENOM; CLU_002656_3_3_2; -.
DR OMA; FRQSKPA; -.
DR OrthoDB; 17053at2157; -.
DR Proteomes; UP000002698; 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_0000228267"
FT DOMAIN 15..230
FT /note="tr-type G"
FT REGION 24..31
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 49..53
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 86..89
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 140..143
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 208..210
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 602 AA; 65542 MW; 1D2433DC192017EC CRC64;
MSESDTTDAG DGTALRTPIV AVLGHVDHGK TSLLDEVRGS AVTAGEAGAI TQHIGATAVP
LDTISELAGQ LVSPEDFDLP GLLFIDTPGH HSFSTLRSRG GALADIAILV VDVNDGFQPQ
SYEALDILKR TQTPFIVAAN KIDTVPGWNP NPDEPVQRTL EAQSDRAESR LNEQLYEIIG
ELSDEGFSAD MYWRVQNFRE NIGVVPVSAE TGEGVPDLLT VLMGLSQRYL KEEMSIDVGG
PGVGTVLEVK EERGFGTTLD IVLYDGTIRA DDTIVVGGKN ETIVTDVRAL LQPQPLAEIR
TEKQFEQVEA VGAAAGIKIA APDLDDAMAG APVRVVRDRP VEEVIAEVEA ELADIQVVTE
EEGIVVKADT LGSLEAIAAA LEEAEIPIVR AEVGDVAPRD IAVASTAEEP KHEAVLAFNV
DVLDDAEREA EEKDVKLFAD DVIYQLVEEY DDYVTEIEEA QQEQILDKIE RPCRFRVLKD
HVFRQSNPAV VGVEVLSGTL KRNSRVVKWD GNEPERVGEL KSLQDAGDDI DEARTGEQVA
ASIDGPTVGR QIEEGDELWA EVPEKHAKIL EQELADEIPT DELEALRMYL DKQRKRDPFW
GK