IF2_JANSC
ID IF2_JANSC Reviewed; 824 AA.
AC Q28WF7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Jann_0038;
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX NCBI_TaxID=290400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) 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; CP000264; ABD52955.1; -; Genomic_DNA.
DR RefSeq; WP_011453164.1; NC_007802.1.
DR AlphaFoldDB; Q28WF7; -.
DR SMR; Q28WF7; -.
DR STRING; 290400.Jann_0038; -.
DR EnsemblBacteria; ABD52955; ABD52955; Jann_0038.
DR KEGG; jan:Jann_0038; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008326; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 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..824
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008256"
FT DOMAIN 321..491
FT /note="tr-type G"
FT REGION 1..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..337
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 355..359
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 377..380
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 431..434
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 467..469
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330..337
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 377..381
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 431..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 824 AA; 89054 MW; DF373452DF5CDA80 CRC64;
MSDQDGKKPL GLSGGARSGR VNQSFSRGRT KSVVVETKRK RVMVPKPGAP SAAAQNAEGG
KRDKSVPDAE MDRRLKALQA AKARESQEAE ERVKAERERE EERNRRRADA EAKEREERER
EEALKAKEEE DDRRKAEEEA RRNAPPEAAA PAVDPAAAAT PRGGGKAAPA RREPERDNKR
ENRSRGNDGG GRRAGKLTVN QAMSGGEGGR QRSMAAMKRK QERQRQKAMG GSVDREKVIR
DVKVPETIIV AELANRMSER VGDVVKALMN NGMMITQNQP IDADTAELII EEFGHRVQRV
SDADVEQVID TVEDDEGKLL PRPPVITIMG HVDHGKTSLL DRIRQANVVS GEAGGITQHI
GAYQVTTESG AVLSFLDTPG HAAFTSMRAR GAQVTDIVVL VVAADDAVMP QTIEAIAHAK
AAEVPMIVAI NKIDRPAADP QKVRTDLLQH EVIVEAMSGE VQDVEVSAMT GQGLPELLEA
IALQAELLEL KANPDRAAQG AVIEAQLDVG RGPVATVLVE KGTLRQGDIF VVGEQWGKVR
ALVNDQGDRV KDAGPSVPVE VLGLNGTPEA GDVLNVVETE AQAREIAEYR EQAAKDKRAA
AGAATTLDQL LANAKADENV RELQVVMKAD VQGSAEAIVQ ALEKIGNDEV RVRVLHYGVG
AITESDIGLA EASGTPVIGF NVRANAPARN AANQKGVEIR YYSVIYDLVD DVKAAASGLL
GAEIRENFIG YANIKEVFKV SGVGNVAGCL VTEGVARRSA GVRLLRDDVV IHEGTLKTLK
RFKDEVKEVQ SGQECGMAFE NYEDIRPDDV IEIFEREEVE RSLT
