IF2_CYTH3
ID IF2_CYTH3 Reviewed; 1008 AA.
AC Q11PK5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
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=CHU_3422;
OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS 15051 / NCIMB 9469 / D465).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Cytophaga.
OX NCBI_TaxID=269798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX PubMed=17400776; DOI=10.1128/aem.00225-07;
RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA McBride M.J.;
RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT hutchinsonii.";
RL Appl. Environ. Microbiol. 73:3536-3546(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000383; ABG60658.1; -; Genomic_DNA.
DR RefSeq; WP_011586765.1; NZ_FPJX01000019.1.
DR AlphaFoldDB; Q11PK5; -.
DR SMR; Q11PK5; -.
DR STRING; 269798.CHU_3422; -.
DR EnsemblBacteria; ABG60658; ABG60658; CHU_3422.
DR KEGG; chu:CHU_3422; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG5180; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; PRPGYQG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001822; 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; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR028626; Ribosomal_S28e_CS.
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; 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..1008
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335464"
FT DOMAIN 507..677
FT /note="tr-type G"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..523
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 541..545
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 563..566
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 617..620
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 653..655
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 153..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 516..523
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 563..567
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 617..620
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1008 AA; 108860 MW; B1C8D1EB348466E3 CRC64;
MAEEKMMRLS QVAKKLNVGT STIIDHLSAK GYDIENNPNA KITVDMYAFL SKEYESSAQV
KKEAESLTIG KKHMGDVVID ADQVNVAPEH DEEDEVRIIN NSPAEAVVPE VPAVTAQEAP
KTAPTAESPE DVKGNVTLQG LKVLGKIDLG TADKDSKKSA KNTKPVEKVA AEKPIEKAKP
ETVAPPVEPK PEPKQETPKT EQPVKKETPK AETQKPPVAD KPAEKTPVVE EPAAPVADVP
VQVVQAHADK LQGLTVLGKI QLPDKKKEPT RVASSDEVVD KNKNKRKRKR LNDGPNKPAG
ANPNGPRPAG SNPNGPRPQG TNPNGPRPQG QGGNPNGPRP AGGPNRPGVP NRPNSNGPKP
TLTKASEKGE VTGKQIQDKI KATMAKLSGG GTKSGPVNRA KYRKDKRSAM ADAEEERLMA
EQEDAKSLKV AEFISASDLA SLMDVSINEV ISKCMAMGMF VSINQRLDAE AITIIADEFG
YDVNFQTTGE EDDVTDVDQD DPASLIDRAP IVTIMGHVDH GKTSLLDYIR KSKVVAGEAG
GITQHIGAYN VMTDSGKPIT FLDTPGHEAF TAMRARGAKI TDIVIIVVAA DDSVMPQTKE
AINHARVAGV PIIIAINKID KPAANPDKIK EELSKENILV EDWGGKYQCQ AISAKAGTGI
SELLDKVLLE AEMLELKANP DKRAIGAVIE ASLDKGRGYV TNVLVEAGTL RIGDIILAGA
HFGRVKAMVD HTGKKLKEAG PAMPLQVLGL NGAPQAGDKF QVMETEREAR EISSKREQLL
REQSIRTKKH ITLDEIGRRL AIGNFKELNI IVKADVDGSV EALSDSLLKL STEEIQIRIL
HKGVGQISES DILLASASDA IIVAFQVRPS TSARKLAEQE QIEIRMYSII YDAINEVKDA
MEGMLEPKME EVVLGTIDVR DVFKITKVGT VAGAYVSEGI VKRNNQVRLI RDGIVMFTGT
ISALKRFKDD VSEVKTSYEC GISLKGYNDI QIGDQIEAFE QKEVKRTL
