IF2_DESDA
ID IF2_DESDA Reviewed; 997 AA.
AC B8J1Y4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ddes_0059;
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) 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; CP001358; ACL47979.1; -; Genomic_DNA.
DR RefSeq; WP_012623711.1; NC_011883.1.
DR AlphaFoldDB; B8J1Y4; -.
DR SMR; B8J1Y4; -.
DR STRING; 525146.Ddes_0059; -.
DR EnsemblBacteria; ACL47979; ACL47979; Ddes_0059.
DR KEGG; dds:Ddes_0059; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
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.
FT CHAIN 1..997
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118759"
FT DOMAIN 496..665
FT /note="tr-type G"
FT REGION 36..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..512
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 530..534
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 551..554
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 605..608
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 641..643
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 45..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 551..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 605..608
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 997 AA; 106103 MW; 71E729913500DC83 CRC64;
MSEEKIKVSE LAKEFPAVPN KDMLRALREL GASAKSMAGS LTTEEAARVR EHFAEQKQAD
AERSGSHPNV IVRRRRKDAD KADAPEVTEA APAAREEVAP PAEEKPAAVE APAQAEPVAE
APAASPHKVE EKAAPEAAKA EPAEKAKSSK ARVVSAARVI SRPGEEEEKK PEPVVESKPE
PVAEISPVAA ALAAREAAAR AEEKSSEKGE EKGAKAARLA RPDASAMPEG SSAPTLPQRA
PEARTEAWKD ADASAAADAA PRRAPRADGG QAPSAAPQVR IISRPAPGSQ PDRSTRPAGG
RPGAPGGPRG DSAGRPPRPG GPRPSGPGGP RPAGGPRPGG FGQQPAAPAS PTDTRDGQSK
KKRLKGRRTV DFQQGDFGGR RDDDDSQRLN RGKGRRKGGK PTSSQATQPL KAAKRKIRVT
EAIRVADMAH QMGLKANEII KVLFGLGVMA TINQALDFDT ATLVASEFGY EVEKAGFSED
DYLTPKEVDA PETLKPRPPV VTIMGHVDHG KTSLLDAIRK SNVTSGEAGG ITQHIGAYHV
KTKRGEIVFL DTPGHEAFTA MRARGAQVTD LVILVVAADD GVMEQTREAI NHARAAGVPI
MVAVNKMDKP SADPDRVLRE LAELGLQAEE WGGDTIVAKV AAKTRMGLDD LLEMVALQSE
IMELKANPDK AAKGHIVEAK LDKGRGPVAT VLIQEGTLRQ GDSFVCGPFS GRVRALMNDQ
GKKVKEAGPS LPVEVQGFEG VPEAGEEFFV VSDEKLARRI ADSRAIKQRE RELASESRVT
LETFLSQRKS DQETLTLNLV LKSDVQGSLE AITEALLKQS TDKVRINVVH GGTGAITESD
ILLASASQAI IIGFNVRPTA KIKDVAEHEN VDIRFYEIIY KLVDDIKSAM AGLLAPVQRE
VYLGQAEVRD TFSVPKIGLI AGSYVADGKI ARNAGVRLLR DGVVVYTGKI SSLKRFKDDA
REVVKGNECG VGLENFNDVK IGDIIEAFET VEEAATL
