ID K6X7H1_9ACTN Unreviewed; 659 AA.
AC K6X7H1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
DE Flags: Fragment;
GN Name=infB {ECO:0000313|EMBL:GAC00293.1};
GN ORFNames=GONAM_14_01520 {ECO:0000313|EMBL:GAC00293.1};
OS Gordonia namibiensis NBRC 108229.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1208314 {ECO:0000313|EMBL:GAC00293.1, ECO:0000313|Proteomes:UP000035058};
RN [1] {ECO:0000313|EMBL:GAC00293.1, ECO:0000313|Proteomes:UP000035058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108229 {ECO:0000313|EMBL:GAC00293.1,
RC ECO:0000313|Proteomes:UP000035058};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia namibiensis NBRC 108229.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000256|RuleBase:RU000644}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAC00293.1}.
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DR EMBL; BAHE01000014; GAC00293.1; -; Genomic_DNA.
DR RefSeq; WP_006866501.1; NZ_BAHE01000014.1.
DR AlphaFoldDB; K6X7H1; -.
DR Proteomes; UP000035058; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|RuleBase:RU000644};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU000644}.
FT DOMAIN 155..327
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GAC00293.1"
SQ SEQUENCE 659 AA; 70770 MW; 64420DA18B8B623D CRC64;
APAGGGFRGR PGGGGGRGRG GAAGAFGRPG GAPRKGRKSK RAKRAEYESM QAPSVGGVRL
PRGNGEIIRL ARGASLSDFA DKIDANPASL VQALFNLGEM VTATESVNDE TLELLGSEMN
YRVQVVSPED EDRELLDSFD LTYGEDEGGE EDLEQRPPVV TVMGHVDHGK TRLLDTIRKA
NVREGEAGGI TQHIGAYQVN THLNGEDRLI TFIDTPGHEA FTAMRARGAK ATDIAILVVA
ADDGVMPQTV EAVNHAQAAD VPIVVAVNKI DKEGADPQKI RGQLTEYGLV PEEYGGDAMF
VDISAKQGEN IDALLEAVLL TADASLDLRA NPDMDAQGVA IEAHLDRGRG PVATVLVQRG
TLRVGDSIVA GDAYGRVRRM VDEHGEDVPE ALPSRPVQVI GFTSVPGAGD NLLVVEEDRI
ARQIADRRNA RKRNALAARS RKRISLEDLD SALKETSQLN LILKGDNSGT VEALEEALLG
IEMGDEVSLR IIDRGVGGVT ETNVNLAAAS DAIIIGFNVR AEGKATELAN REGVDIRYYS
VIYQAIDEIE SALKGMLKPI YEEVELGRAE IRAIFKSSKV GNIAGCLVQS GIMRRNAKAR
LLRDNVVVAE NLTVSSLKRE KDDATEVREG YECGLTLTYS DIKVDDVIET YELQEKPRD
//