IF2_SACD2
ID IF2_SACD2 Reviewed; 908 AA.
AC Q21H61;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sde_2708;
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD81968.1; -; Genomic_DNA.
DR RefSeq; WP_011469185.1; NC_007912.1.
DR AlphaFoldDB; Q21H61; -.
DR SMR; Q21H61; -.
DR STRING; 203122.Sde_2708; -.
DR PRIDE; Q21H61; -.
DR EnsemblBacteria; ABD81968; ABD81968; Sde_2708.
DR KEGG; sde:Sde_2708; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001947; 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; IPR009061; DNA-bd_dom_put_sf.
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; 2.
DR SUPFAM; SSF46955; SSF46955; 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..908
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008326"
FT DOMAIN 409..578
FT /note="tr-type G"
FT REGION 122..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..425
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 443..447
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 464..467
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 518..521
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 554..556
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 225..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 418..425
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 464..468
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 518..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 908 AA; 97952 MW; 9C4B5337860CD44B CRC64;
MAEVTVSELA KSVGAPVERI LSQMQQAGLT HQSPDDVVSD EEKQKLLTFL KSSHGETVAE
PKKITLKRKT TTTLKTGSGS GRKTVNVEVR KKRTYVKRDE VADEIEESAA VAEAEVAKVE
EPVVEPVQEP EVAAEPEVVE APEPEPVVEA IEEAPVEEPA APAAPVISQT TTASSLVDDA
EEMRIRAASA RIKAEEERLA AIEKARKEKA AKPAPAPGPA AAAKEDARPT KHVEDLAKLK
KPHDKKDEEF DEDGKKHNKK AGKAVKKVAG PKKVASALDY VEDKEEIEEV IHAPKPKRLS
ANRGPRPVIK VSNKHGFKKP TGKITYDVEI PETITVGELA QRMNVKAGEV VKCLMKMGTM
ATVNQPIDQE TAQLVVEELG HKAVLISADA IEIKLQEEVA ANVDGETIPR APIVTVMGHV
DHGKTSLLDY IRKAKVASGE AGGITQHIGA YRVQTSHGEL TFLDTPGHAA FTAMRARGAQ
CTDVVILVVA ADDGVMPQTE EAVQHARAAG VPLVVAINKM DKESADPDRV KNELSAKEVI
PEDWGGDTQF IEVSAHTGQG IEELLEAVAL QAELLELSAP KDVPARGVVV ESRMDKGRGV
VATVLVQGGD LKSGDILLAG QSFGRVRAMT NEFGEQVKTA GPSSPVEILG LDTPPQAGDE
FLVVPDERKA REVAEFRAER ERQEKLQRQQ AAKLENMFAG IGENETKVLS VVLKTDVRGS
LEAIQAALLD IGNDEVQVNI VGGGVGGITG NDVNLALTTG AIVLGFNVRA DASARKLAET
ESIEIRYYSI IYQLIDEVKS ALSGMLDPER VEEIVGIAEV RETFRSPKFG QVAGCMVVEG
SVHRNKPIRV LRENVVIFEG ELESLRRFKD DVSEVRNGTE CGIGVKNYDV KVGDQIEVFD
VKEVAREL
