IF2_NOCFA
ID IF2_NOCFA Reviewed; 969 AA.
AC Q5YSC6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NFA_40670;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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 -!- SEQUENCE CAUTION:
CC Sequence=BAD58915.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP006618; BAD58915.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041560304.1; NC_006361.1.
DR AlphaFoldDB; Q5YSC6; -.
DR SMR; Q5YSC6; -.
DR STRING; 247156.NFA_40670; -.
DR EnsemblBacteria; BAD58915; BAD58915; NFA_40670.
DR GeneID; 61134710; -.
DR KEGG; nfa:NFA_40670; -.
DR eggNOG; COG0481; Bacteria.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_2_11; -.
DR OMA; QVRPEMI; -.
DR BioCyc; NFAR247156:NFA_RS20215-MON; -.
DR Proteomes; UP000006820; 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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..969
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228219"
FT DOMAIN 465..636
FT /note="tr-type G"
FT REGION 50..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..481
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 499..503
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 524..527
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 578..581
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 614..616
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 75..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 524..528
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 578..581
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 969 AA; 100739 MW; E9A0974F2358481B CRC64;
MAGKARVHEL AKELGVTSKE LLATLKEQGE FVKSASSTVE APVARRLRES FASKSAPANG
AKPGPAASAR PGAKPTPGGP RPGPRTPAPA ASAPQAPAEQ TARPTDARPG PAVKPGPAPT
PARPAAPEAP AAKAAPEAPA QRPTPGGPRP GQQQQRPGAP AQGGPRPGPK PGPKTPRVGN
NPYSSQPAPE RERPAARPGP GGPRPGPAQG GPRPGPGQGA PRPGATPGPR PAAAQGGPRP
GGPRPSPGSM PPRPNPGAMP QRTPRPGPSA GGRPGRPGGA PGAGRPGGGG GGYRGGGGAP
GAGAGAPAGG GFRGRPGGGG GRPGGPGGRG GAAGAFGRPG GAPRRGRKSK RQKRQEYDSM
QAPSVGGVRL PRGNGEIIRL ARGASLSDFA EKIDANPAAL VQALFNLGEM VTATQSVNDE
TLELLGSEMN YVVQVVSPED EDRELLESFD LTYGEDEGDE DDLQVRPPVV TVMGHVDHGK
TRLLDTIRKA NVREGEAGGI TQHIGAYQVM THLGDEDRLI TFIDTPGHEA FTAMRARGAK
ATDIAILVVA ADDGVMPQTV EAINHAQAAD VPIVVAVNKI DKEGANPEKI RQQLTEYGLV
AEEYGGDTMF VDISAKQGTN IDALLEAVLL TADAALDLRA NPNMDAQGVA IEAHLDRGRG
PVATVLIQRG TLRVGDSIVA GDAYGRVRRM VDEHGEDVEA ALPSRPVQVV GFTSVPGAGD
NLLVVDEDRI ARQIADRRNA RKRNALAARS RKRISLEDLD AALKETSELN LILKGDNAGT
VEALEEALMG IEVGDEVRLR VIDRGVGGVT ETNVNLASAS NAIIIGFNVR AEGKATELAN
REGVDIRYYS VIYQAIDEIE KALKGMLKPI YEEVELGRAE IRAIFRSSKV GNIAGCMVLS
GSVKRNAKAR LLRDNVVVAE TTTISSLRRE KDDVTEVREG FECGMTLTYN DIKEGDIIEA
YELREKPRD
