IF2_XANOR
ID IF2_XANOR Reviewed; 906 AA.
AC Q5GXU9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=XOO3218;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW76472.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE013598; AAW76472.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5GXU9; -.
DR SMR; Q5GXU9; -.
DR STRING; 291331.XOO3218; -.
DR EnsemblBacteria; AAW76472; AAW76472; XOO3218.
DR KEGG; xoo:XOO3218; -.
DR PATRIC; fig|291331.8.peg.3566; -.
DR HOGENOM; CLU_006301_10_2_6; -.
DR Proteomes; UP000006735; 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; 1.
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..906
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228263"
FT DOMAIN 405..574
FT /note="tr-type G"
FT REGION 134..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..421
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 439..443
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 460..463
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 514..517
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 550..552
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 139..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 460..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 514..517
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 906 AA; 96366 MW; 7DC28409D3D5425A CRC64;
MSQQTTIRKL AELVNTPVDK LLVQLAEAGM KFSGPDQVVT STEKMKLLGF LRRTHGKAET
PAEAASEAAK KITLNRRKLQ EVTVSAGRTK TTVNVEVRQK RTYVKSENEG SGRATPMTPD
EERADILAKL AASRQRNLDE QQRLAESDRV RDEEIQRKRD EEQAAKDRAE AERKAAEEAA
AAASAPAPAP VAAAPTPSAA APAARAPSSP SSAPRPSRPG GASPASRPST PARPDDRNNA
AKHKTRGSHV MVAGVEDDDA TKRFAGQLHL SAADRARRSN VRGKPTGRPG SSSSRRGNDN
GRGSNQANSG PHGFERPTAP VVREVAIGET ITVADLAQKL ALKGGDVVKA LFKMGVMATI
TQSIDHDTAA LVTEELGHKA VRADNADFED ALLAHAEDAQ GDTTTRPPVV TIMGHVDHGK
TSLLDYIRRT KIASGEAGGI TQHIGAYHVE TDRGVISFLD TPGHAAFTSM RARGAKITDI
VVLVVAADDG VMPQTKEAVA HAKAAGVPLI VAVNKIDKAG ADPLRVKNEL LAENVVAEDF
GGDTQFIEVS AKVGTGVDTL LDAISLQAEV LELKAVAEGR ASGTVIESSL DKGRGPVATV
LVQQGALKRG DYLVCGIQYG RVRALFDETG HQPGSAGPSI PVQVLGLSGV PEAGDDFVVV
DDERLAKDVA QQRETKRRES RLVASATNRM EDILAQMGKG EGQQVLNLVI KADVQGSVEA
LKQSLVALSN EDIRINVIHS GVGGITESDA NSAAASKATI IGFNVRADAS ARKIVESNGV
DLRYFSIIYD VIDQVKQVAS GLLGVEIREE IMGIAQVRDV FRSSKFGAVA GCMIIEGVVK
RSKPIRVLRD SVVVFEGELE SLRRFKENVD EVRNGNECGI GVKAYNDVKA GDQIECFERI
EVARTL
