IF2_CHLT3
ID IF2_CHLT3 Reviewed; 1097 AA.
AC B3QUN2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ctha_0467;
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chloroherpeton.
OX NCBI_TaxID=517418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL Submitted (JUN-2008) 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: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; CP001100; ACF12938.1; -; Genomic_DNA.
DR RefSeq; WP_012499022.1; NC_011026.1.
DR AlphaFoldDB; B3QUN2; -.
DR SMR; B3QUN2; -.
DR STRING; 517418.Ctha_0467; -.
DR EnsemblBacteria; ACF12938; ACF12938; Ctha_0467.
DR KEGG; cts:Ctha_0467; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; KPGANTE; -.
DR OrthoDB; 79988at2; -.
DR Proteomes; UP000001208; 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..1097
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093771"
FT DOMAIN 591..761
FT /note="tr-type G"
FT REGION 79..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..607
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 625..629
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 647..650
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 701..704
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 737..739
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 79..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 600..607
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 647..651
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 701..704
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1097 AA; 122673 MW; 2F036EDA56B6DE6A CRC64;
MPAEKEKKKH KLIDIAVELQ VSLDDIRSFV EELGYRTTNS TKVTDSVKEL ILDNYSDEKK
KSDLHKKLKA EKNRKIQLLE KRVSPQADKF SKKKTAAKKE ASQEKADAHA KLEPSIPEEA
PAAIDIDDTP EVAPEIEIPS QNTQEPEPVE MDEVASAATL AVEEAPIAAA PTEEPMHNSE
AELPESKIDS AEAVAEEAAP EVEVHLEPKE QEVQELNHAE EAETPTTEAS SEETSAVMTK
EGDSNDAQPF TQHEPVSRKT QNTTNVSEEN KQHEKQPETL KSDKAMDVVQ PVPIAEETAE
QQLTEASSYE KKETNLQGEN LETNEADAAQ TEAKDDDAQS DSLQAEISRQ QNEISNRFSQ
SENIAGLKVF GEIELHKKKR KRKKNFREQA KDLKQQMTPE QPKQEEKPVK KEKPKEREKP
AAGKKEQTPG KKPVREDQKE RVLQDGPARV IKKKPKKAVD EKVVDRNIRQ TMMTMDDTND
SSARQKFRKI RKRERLREQE IEAAAKEAES KVLKITEFAS THELADMLGV TPKEVIQKCF
KLGKFITINQ RLDKETIELL SLEFNYEVHF ISDVEATEID DDPDLPEDMK TRPPVVTIMG
HVDHGKTSLL DYIRNSNVVA GESGGITQHM GAYEVTLENK QRLTFLDTPG HEAFTAMRAR
GAQVTDVVIL VVAADDNVMP QTVEAINHAK AAEVPIIVAI NKIDKPDANP EKIRTQLADI
GVLVEDWGGS VQCQEISAKK GTGVRDLIDK VLVEAELLEL KANYSEDKLS RGVVIEAELD
KGKGVIATIL VQTGIINVGM PFVAGGSSGR IRAMLDERGN RLETVYPSQP VRILGFEELP
QAGDLFSIMP SDREAREIAQ RRQVIRREHE FRHSSRVKLN DIAKQVQEGQ VQELRVIIKA
DTDGSIQALA DGLMKVQTDE VKVEVIHRGV GQITETDVLL AAASDAIIIG FRVRPNVNAK
KLAEKEEIDI RFYSVIYHVL EDIHDALEGM LSPELQEKVT ATVEIRDIFR ISKIGNVAGC
HVLDGKINRD SRVRLLRDGI QIYEGVLDSL KRHKDDVKEV DSGYDCGLTL KNYDDIKVND
IVESFETVET KRKLVVS
