IF2_ANAD2
ID IF2_ANAD2 Reviewed; 951 AA.
AC B8JFY6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=A2cp1_1230;
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
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; CP001359; ACL64574.1; -; Genomic_DNA.
DR RefSeq; WP_012632556.1; NC_011891.1.
DR AlphaFoldDB; B8JFY6; -.
DR SMR; B8JFY6; -.
DR EnsemblBacteria; ACL64574; ACL64574; A2cp1_1230.
DR KEGG; acp:A2cp1_1230; -.
DR HOGENOM; CLU_006301_9_3_7; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000007089; 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.
FT CHAIN 1..951
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118744"
FT DOMAIN 450..619
FT /note="tr-type G"
FT REGION 58..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..466
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 484..488
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 505..508
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 559..562
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 595..597
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 87..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 459..466
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 505..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 559..562
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 951 AA; 101330 MW; FF9BE93416FAB91A CRC64;
MSKKRVHELG KQLKEQGIEL SNQELVEKLH ALGYLEVKSH SSSLEDDQAH AAYEKILAER
KPKPAPVRPS GPGFVVRKRA HVEPPTVTAP AAPPPAEPEY AEPQYAEPQQ AEQAYEPEPQ
EAQPEAAPEP VAAPEQPAEA APLAAQAAPS PGAEAAAPAA PQAQPAQPAA PVAPPAPSAQ
PSAPQPPAAQ PRPPQPPMPS RPPPAGYRPA PPPGARPPMS AAPGAPAQPG AAGQPPRPPV
DPRTLRPTST QAVVISRPLV PVRRVTPPTS ARQQFPVAPG PRALGEVREL KVVPGSLGRE
REFIDVSRDK RRGRQPGRPI SEEQAKSLSG KELLQAAISD RAYIPIRGKK KKPTKKGAKT
QITEKAEHKK VIRIEESISV SELSQVMGVK ASDLIRKLMQ MGKMVTINAQ IDADTAAILA
LEHGYTVEKK GFEVEEFIPE VEVDESKLVI RPPVVTVMGH VDHGKTSLLD AIRQADVAAG
EAGGITQHIG AYSVNTPQGP ITFLDTPGHE AFTAMRQRGA QVTDLVVLVV AADDGVMPQT
VESIKAAKAA GVTILVAINK VDKPQAAPER VMQQLTEYEL VAEQWGGTTI MLPVSARTKQ
GIPELLEYIA LQSEVLELKA NPDKLAAGRV IEAKLEKGRG PVATVLVEEG TLRVGDALVT
GVHFGRVRAM MNERGEQVDN VGPGYPVEVL GLSGVPVAGD EFDVVEDEKA AKEVAQHRAT
KQRQKELGGV KKATLEDLFA KAKTSGQKVL NLVVKADVQG SSEAVSQALE KAATKKVGVK
ILESAVGAIT KSDVLTAAAG NAVIVGFNTK PESEIENIAS QQGVKILMFG IIYEAVDRIR
EEMAGLLEPI IKEKPLGKAE VRQVFNIPRV GQIAGSAVTE GVVKRAGHVR VVRDRKVIFT
GKIGSLKRVK DDVREVAQGF ECGIGVDGFS DVKQGDILEV YELEEIRPSL D
