IF2_CARHZ
ID IF2_CARHZ Reviewed; 827 AA.
AC Q3AB98;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CHY_1766;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
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}.
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DR EMBL; CP000141; ABB14990.1; -; Genomic_DNA.
DR RefSeq; WP_011344660.1; NC_007503.1.
DR AlphaFoldDB; Q3AB98; -.
DR SMR; Q3AB98; -.
DR STRING; 246194.CHY_1766; -.
DR EnsemblBacteria; ABB14990; ABB14990; CHY_1766.
DR KEGG; chy:CHY_1766; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 99992at2; -.
DR Proteomes; UP000002706; 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 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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..827
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228181"
FT DOMAIN 326..495
FT /note="tr-type G"
FT REGION 49..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..342
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 360..364
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 381..384
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 435..438
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 471..473
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 49..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335..342
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 381..385
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 435..438
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 827 AA; 92574 MW; 59AED0DA3029768D CRC64;
MRKKRVFEIA KELNMESKEV INRLKAIGVE VKSHMSTVEN HHLNLLLKAL NREKEEKEKK
EQEKKQVEQK AEAQKLQSHP QRPKEQQQSK QGGQSRPREQ RSDRPQGQRY AGNQRPEPRD
KDKGRRPGEQ RSFNQNRPRD DRRRFDKERG VQGPKPFGEK KERPPFPREK KKGVLPAIPK
PEAPKGENKE PERRKGAPDK KREWEKALKK EEKVFALEEK KLNLKKEKKQ EKQEKQEPVA
AEPKAIVIPE RMTVQEFAKI MGKSAAEVIK KLMSYGILAT INQEIDADTA TIIATDFGYE
VTVEKEEKED IWLLEETPDD PESLEPRPPI VTVMGHVDHG KTSLLDAIRQ TNVTATEAGG
ITQHIGAYQV EHNGRKITFI DTPGHEAFTA MRARGAQVTD IAILVVAADD GVMPQTVEAI
NHAKAAGVPI IVAVNKIDKP NAQPDRVKQQ LTEYGLIPEA WGGDTVFVEV SALKKIGIEE
LLEMILLVAD LKELKANPNK PARGTVIEAK LDKGRGPVAT VLVQSGTLNV GDVVVVGLTY
GRVRALMDDK GRRVKKATPS MPVEVLGLND VPSAGDILVV VDDEKTARTL AEKRQEQKRE
EELRASSKVS LEDLFKHIQE GKIKELNIVL KADVHGSVEA IKQSLSRLST EEVKVNVIHS
GVGAITETDI MLASASNAIV IGFNVRPDSN ARKLAETEKI DVRVYRIIYE LLDDIKAAMA
GLLEPEQKEV VLGRAEVRKT FKASKVGTIA GLYVLEGKIT RSAKVRVIRD GIVIHEGNVE
SLKRFKDDVR EVAQGYECGL TIEKFNDIRE GDIIEAFTIE EVKRTLE
