ID A0A0D5A8E0_9NOCA Unreviewed; 967 AA.
AC A0A0D5A8E0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN ORFNames=NY08_1382 {ECO:0000313|EMBL:AJW39412.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW39412.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW39412.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW39412.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
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|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP010797; AJW39412.1; -; Genomic_DNA.
DR RefSeq; WP_045195525.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5A8E0; -.
DR STRING; 1564114.NY08_1382; -.
DR KEGG; rhb:NY08_1382; -.
DR PATRIC; fig|1564114.4.peg.1354; -.
DR HOGENOM; CLU_006301_9_4_11; -.
DR Proteomes; UP000032410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR01217; PRICHEXTENSN.
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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}.
FT DOMAIN 463..635
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 30..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 522..526
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 576..579
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 967 AA; 99320 MW; 6EE4079360B911EA CRC64;
MAGKARVHEL AKELGVTSKE LLARLKEQGE FVKSASSTVE APVARRLRES FPSDGADASA
PAAAAPNGRA AADRAAGSTA KPGAAKPGGP RPGPKPAPRP AEPEAPAAQA PAEAAPAAPA
TPAAAPAPAP AAPTPSPAAP AAPVEQAPAA SAATSDAAPA PAAPKPAGPG PKPGPKAPRV
GNNPYSSAPV ERPAPRPAPG APRPGGGRPA PGQGGPRPAT PSGGTRPAPG QGGPRPAPGQ
AGPRPSPGSM PPRPNPGAMP TRSARPGPAA GRPGRPGGAP GGRPGGGGGG GYRGGGAPGA
PGGAPAGGAP AGGFRGRPGG GGRPGQRGAA AGAFGRPGGA VRRGRKSKRA KRAEYESMQA
PAVGGVRLPR GNGETIRLAR GASLSDFADK IDANPAALVQ ALFNLGEMVT ATQSVNDETL
ELLGGEMNYV VQVVSPEDED RELLDSFDLT YGEDAGGEED LEQRPPVVTV MGHVDHGKTR
LLDSIRNTTV REGEAGGITQ HIGAYQVLTE LEGNERLVTF IDTPGHEAFT AMRARGAKAT
DLAILVVAAD DGVMPQTVEA INHAQAADVP IVVAVNKIDK EGANPDKIRQ QLTEYGLVAE
EYGGETMFVD ISAKQGTNID ALLEAVLLTA DASLDLRANP DMDAQGVAIE AHLDRGRGPV
ATVLIARGTL RVGDSIVAGD AYGRVRRMVD EHGEDVTEAM PSRPVQVIGF TSVPGAGDNL
LVVDEDRIAR QIADRRNARK RNALAAKSRK RISLDDLDAA LKETSQLNLI LKGDNSGTVE
ALEEALLGIE IDDEVELRVI DRGVGGVTET NVNLASASNA IIIGFNVRAE GKATELANRE
GVDIRYYSVI YQAIDEIEKA LKGMLKPVYE EVALGQAEIR ALFRSSKVGN IAGCLVTSGT
IRRNAKARLI RDSAVVAETV TISSLRREKD DATEVREGYE CGLTVTYSDI KVGDVIEAYE
LREKPRD
//
