IF2_SYNC1
ID IF2_SYNC1 Reviewed; 947 AA.
AC Q3A4A7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pcar_1555;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) 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; CP000142; ABA88800.1; -; Genomic_DNA.
DR RefSeq; WP_011341283.1; NC_007498.2.
DR AlphaFoldDB; Q3A4A7; -.
DR SMR; Q3A4A7; -.
DR STRING; 338963.Pcar_1555; -.
DR PRIDE; Q3A4A7; -.
DR EnsemblBacteria; ABA88800; ABA88800; Pcar_1555.
DR KEGG; pca:Pcar_1555; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 132013at2; -.
DR Proteomes; UP000002534; 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..947
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228223"
FT DOMAIN 447..616
FT /note="tr-type G"
FT REGION 69..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..463
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 481..485
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 502..505
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 556..559
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 592..594
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 144..158
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 456..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 502..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 556..559
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 947 AA; 102913 MW; 07C30195B80B024C CRC64;
MGKKIRVYEL AQKMGVDNKV LLEKLHEAGI DAKSHMSVLS EEDVEKLDEA PAKVERVEER
RITAGVIRRR RKEVPQEEKA APPAAAEEPS SVDTAVAEEA PAEEVQPVSD QPEIAVEPPP
AGKQEEVAAP APEPKAEEPV VEEVIAEPAV EEVVEEPSAV EQEEHVETTP VAEEEPKVEE
QPSVEAESKA VSGELEESKT ADQSKGQSEA AEVSVTKEKP KVEKATANRA KILGRVELST
LTSPPKRQER AKNGKGRPER PKGAKPSGGP APRAKEAAPQ AAVPFDGGPA PDKEVRGGKK
GKKGKGNSYD KDKGFADGGK GRRARRQVYE PERDERRMRR GKKTPKPQKK TEVTVSKAIK
RIIRISDVIT VGELAKRMGV KSKDLITELM RQGQMVTINH PLDFETAAIL ASEFNYEVEN
VAFDEENLLA DTAAVTEEGD SEEGCVPRPP VVTIMGHVDH GKTSLLDAIR ATNVTGGEAG
GITQHIGAYD VSVDDKKITF LDTPGHEAFT SMRARGAKVT DIVILVVAAD DGVMPQTKEA
INHSKAAGVP IIVAVNKMDK PDANSDRVKQ ELTEFEMIPE EWGGDTIFVE VSAKNRTNLD
SLLEMVLLQA EVLELKANPN KRAKGAIVEA RLDRGRGPVA TVLVEEGTLR IGDPIVSGLH
YGKVRTMTND RGERLEEAGP ACPVEVTGLS GTPTAGDSFH AVESEKDAKE VATHRQRKVR
EQELASTSKI SLEQLYARMQ EGEVQELKVI IKADVQGSVE AVRDSLVKLS TDACRLVVIH
TAVGGINESD VSLASASDAI ILGFNVRAES KAAALAETEG VDIRFYNVIY DAVNDIRDAM
EGLLAPTLRE KHLGKVEVRE TFHVSKVGTI AGCYVTEGKV LRNAQVRLIR DHVVIWEGKL
ASLKRFKDDA REVQNGYECG LSLENYNDIK VGDIIEVFEM EEVKTSL
