IF2_ANAPZ
ID IF2_ANAPZ Reviewed; 823 AA.
AC Q2GKQ2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=APH_0446;
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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; CP000235; ABD43852.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2GKQ2; -.
DR SMR; Q2GKQ2; -.
DR STRING; 212042.APH_0446; -.
DR PRIDE; Q2GKQ2; -.
DR EnsemblBacteria; ABD43852; ABD43852; APH_0446.
DR KEGG; aph:APH_0446; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001943; 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; 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..823
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057650"
FT DOMAIN 322..491
FT /note="tr-type G"
FT REGION 30..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..338
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 356..360
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 377..380
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 431..434
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 467..469
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 47..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331..338
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 377..381
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 431..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 823 AA; 88767 MW; A6C5FE76CBEE704D CRC64;
MSDVEKVDGE CSASGKRERL TLKLGDKLKV PPSLARGTST GKSFTTVEVR SKKRRPGEYI
SHDDKRRSGL NKAVSGLTAQ EQLFRINAIN MADSISAKEK ELAAARKAKE EEELAAAAAV
VEEAVEEVSV EGDVPPVEAV EAAVPDVEEV VAPVATPSHS NKSGHDDRGG KKYAHGATGR
HKEKEGVSIK KVASSRGASK HIKLDIENAL SGLEDKRVTR FSSSTHKRRS SNVKSGRRIS
REVVISDKMT VRDLALAMAE KAQDVLRMLS HVGVEARMDT GLDSEVACEI AVEFGHRPRV
VSIVKMEQEL SDVCGDDFVS EPRPPVVTVM GHVDHGKTSL LDVLRKSNVA EKEFRGITQH
IGAYQIDVDG KKITFLDTPG HEAFADMRAR GANVTDIVVL VVAADDGIMP QTVESINHVK
AAGVAMVVAV NKIDKSDADV GRITNELLQY GVIAEELGGD VMIVPVSAKT GENIDKLQSA
ILLLAEMLEL SAPRECRAQG VVIEAKIDRG CGVVATVIVQ KGTLKKGDII VAGDSSYGKV
RSMFDDADRV VTSALPAMPV RVLGLNAIPK AGDTLIVMPS EKQARDLLWH RSEINSAREE
NRAVPSFSGA IMASMDSKVE EINLILKADV AGSMEAVSCA VEQLVHEEVK FNVLHKEMGD
VTKSDVLLAE VSSAVILAFN VRVDAKARDL LRLKKVDVRH YQVIYDLVDD VRNMVSGKLK
PIVQEMQVGL LTVRQMFSSG KSGTVLGCYV TEGAVTRGAT VCVCRGETVI GEGTVKALRR
FKEDVKEVNR GLECGLLVDG VKGVLAGDVI KVLEIVERMR GVE
