IF2_GLOVI
ID IF2_GLOVI Reviewed; 925 AA.
AC Q7NH85;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=glr2652;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC90593.1; -; Genomic_DNA.
DR RefSeq; NP_925598.1; NC_005125.1.
DR RefSeq; WP_011142646.1; NC_005125.1.
DR AlphaFoldDB; Q7NH85; -.
DR SMR; Q7NH85; -.
DR STRING; 251221.35213221; -.
DR EnsemblBacteria; BAC90593; BAC90593; BAC90593.
DR KEGG; gvi:glr2652; -.
DR PATRIC; fig|251221.4.peg.2689; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR InParanoid; Q7NH85; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR PhylomeDB; Q7NH85; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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 PRINTS; PR00315; ELONGATNFCT.
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..925
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137205"
FT DOMAIN 417..589
FT /note="tr-type G"
FT REGION 190..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..433
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 451..455
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 476..479
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 530..533
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 566..568
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 195..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426..433
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 476..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 530..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 925 AA; 98910 MW; A65A423276CF3B03 CRC64;
MTNANMQGKI RIYDLARDLG RDNRDVMAVC QRLGIAHKTH SSTISEQEAD SIREAFQRGL
PPGGRKKAKI QQQGAAAANK QQILEVRRPP VGYQPPVRTE VSQILVSTVT PAVPTEAQPL
PIPTLPELPV PEQVAEQAAA PSVQEAVEPI AVSPVTSPLP IDAADVEADN YTADEDSMPI
SIAQTVVEAP AAPTSEAAPP EPEPTPLPAP AAEAPQPVRP PAPPAPAKPT PAPAPAPRPT
AEQPSEPRRP QPPAQPPSRP EKRGGPLIAP NRGGLQPTRP VPAQPAPQTP TRSGSGIAKK
GAITKAGSGS GGGRPGGPMR RRDEREAAVV DEQPKILLLS GNISVQDLAQ RMHVPTTEII
KTLFMKSVMV NINQTLDQAT AELVARELGY EVQAETAVAQ ATKTEMLDVG DIESLEVRPP
VVTIMGHVDH GKTSLLDAIR SARVAEGEAG GITQHIGAYQ IEVPTEAGPR KLVFLDTPGH
EAFTAMRARG AKVTDITVLV VAADDGVKPQ TIEAISHAKA AGVPILVAIN KVDKPDANPE
RVKQELTEYD LVPEEWGGKT VMVPVSAKQK LNLDLLLENL LLVADYELEL MANPNRQAKG
TIIEANLDKA RGPVATALVQ NGTLHVGDII VVGSIFGKVR ALYDDRGNRV DAAPPSMPVE
VLGLTDVPQA GDEFEVYSDE REARRIADER TSKARENRLQ QQMASRRVSL GAFSAQAQEG
ELKELALIIR ADVQGSVEAI RASLEKLPQD KVQLRVLQAA AGEVSETDID LAAASNAVIL
SFSTTLASGA RQAAEQAGVD VREYDVIYKL LEDIQLAMEG LLDPELVEEA LGGAEVRQVF
PVGKGQVAGC YVKEGKLLRN AQMRVRRGKE VVFEGHVDSL KRFKEDAKEV ATGFECGVGS
DKFASWQPGD LIECFRMVTQ KRTLN
