IF2_AZOPC
ID IF2_AZOPC Reviewed; 912 AA.
AC B6YQ44;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CFPG_053;
OS Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC Candidatus Azobacteroides.
OX NCBI_TaxID=511995;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19008447; DOI=10.1126/science.1165578;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT protist cells in termite gut.";
RL Science 322:1108-1109(2008).
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; AP010656; BAG83316.1; -; Genomic_DNA.
DR RefSeq; WP_012573077.1; NC_011565.1.
DR AlphaFoldDB; B6YQ44; -.
DR SMR; B6YQ44; -.
DR STRING; 511995.CFPG_053; -.
DR PRIDE; B6YQ44; -.
DR EnsemblBacteria; BAG83316; BAG83316; CFPG_053.
DR KEGG; aps:CFPG_053; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_0_10; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000723; 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; 1.
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..912
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000117320"
FT DOMAIN 411..581
FT /note="tr-type G"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..427
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 445..449
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 467..470
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 521..524
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 557..559
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 188..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 420..427
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 467..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 521..524
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 912 AA; 103020 MW; A834CCAB81D8C9FF CRC64;
MAIRLNKVTK LLNVGLSTIV KFLQSRGYLR EENPNTKISP EEYEILNQEF HKDKHVKLDS
EKLSKERFQK ENYDKDKLKQ IEEIKMGIPR SNEFQLLLTS KLDLDTLPQD KSQTTIEIKK
TIKTSEIKEI KRENKTDILK ERKQIEEIKN SYLNKQQKKS NLLSSTDSTI NFTITGKIDL
TTINNATRPK RKTKEEKQKE REERNKKIVN IKTEKTTQVN AGKKSIASTQ TNIEILKRKK
RNRIKHEKVN IEQQNISTIP NPKNKHFKFH KPTYKNEVSE EDVQKQIKET LAKLTNSSLK
KGTKYRKEKR DTLLQLKNEQ YKIKTQENKT IKITEFVTAN DLSKMMNVPV VQVISTCMSI
GIMVSINQRL DSETIDIVAD EFGYKTEYVS AEAIETIIDD ENENQEKELV LRPPIVTIMG
HVDHGKTSLL DNIRNTNVIA GEAGGITQHI GAYNVKLDDG RKITFLDTPG HEAFTAMRAR
GAKITDIAII IIASDDNIMP QTIEAINHAV AAGVPIIFAI NKIDKHGANP EKIKETLASM
NYLVEDWGGK YQSQDISAKK GIGIQELLEK VLLEAELLDL KANPKRYAIG SIIESSLDKG
RGYIATMLIQ NGTLKLGDIV LAGIYFGRVK AMFNERNLKI KEAGPSQAVL VLGLNGAPQA
GDTIRVVKTE QEAREIAAKR EQLQREQSLR TQKLLTLDDI SRRIAVKNFH KLNIIVKGDV
DGSVEALSDS LIRLSTEQIQ INVIHKGVGQ ISESDVILAT ASNAFIIGFQ VRPSLLTRKL
AEKEGVEIRL YSIIYNAIEE VKSAMEGMLI PKTKEEITSN VEIREVYKIT KVGSVAGCIV
KEGKIKQGDK IRLIRNGVVI YTGELGSLKR YKDYAKEVTQ GCECGLNIHN FNDIKVGDII
ETFENIETKQ KL
