IF2_RUMCH
ID IF2_RUMCH Reviewed; 1161 AA.
AC B8I6E7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ccel_0457;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
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; CP001348; ACL74839.1; -; Genomic_DNA.
DR AlphaFoldDB; B8I6E7; -.
DR SMR; B8I6E7; -.
DR STRING; 394503.Ccel_0457; -.
DR EnsemblBacteria; ACL74839; ACL74839; Ccel_0457.
DR KEGG; cce:Ccel_0457; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NNQRSDR; -.
DR Proteomes; UP000001349; 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; 2.
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..1161
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118756"
FT DOMAIN 663..832
FT /note="tr-type G"
FT REGION 63..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..679
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 697..701
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 718..721
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 772..775
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 808..810
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 168..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 672..679
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 718..722
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 772..775
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1161 AA; 130125 MW; 1BD127E30A5A5B7D CRC64;
MEKARIYELA KELNTTSKRL MEKLAEIDIS VKNHMSLLEP HELDALYKHI GVIRHDDKKN
EVEEKKTVAE STNTTEKKKE VKKEVKKENK NAPRIIRTTE IIIDSSTEDS SGANNFPKNE
TKNVQKKNYK NNFVKVESST SGLRPGFVRD VKPDLRNKQN AASSKNEVKK ALPKETSAPK
EEVLNSKIIN EDIHKEEKTV ADNKGNGSKV LKGSSNTESA QLNNKVAAVE KEEQKSINKP
ESAQISTQSE NKPQQSNGAK QPEEAVVSVN KDSIGKSEQV TAQNDVPSVN KVHPQEKPVH
RTDRPQGQYN NQRSDRPQGQ YNNQRSDRPQ GQYNNQRSDR PQGQYNNQRS DRPQGQYNNQ
RSDRPQGQYN NQRSDRPQGQ YNNQRSDRPQ GQYNNQRSDR PQGQYNNQRS DRPQGQYNNQ
RSDRPQGQYN NQRSDRPHGQ YNNQRSDRPQ GQYGNKRPDR PQGQHRQQNL DIPKPDASVA
QEAFDSQRNE ARREFQGRDF DKNVKREEKQ KKEAPKSNTA TKQRFRPQKI VIEKKGVSEI
LSEDYIFNEF YNDDGKKKKH RNKRNDKVQV KYIPPKAVLT SITIPESLTV KDLAESLKKT
STEIIKKLMA YGVMATLNNE VDFETATIIA EEYGVKTEKA IQVSEEDILF DDDEVQDESK
LQPRPPVVVV MGHVDHGKTS LLDAIRSEHV IDSEAGGITQ HIGAYTVKAN DRAITFLDTP
GHEAFTAMRA RGAQVTDIAI LVVAADDGVM PQTIEAINHA KAANVTIIVA INKIDKPSAN
PDKVKQELTE YGIVAEEWGG DAIMVPVSAK KRENIDQLLE MVLLAADMLE LKADPERQAK
GTVIEAKLDK ERGPVATVLV QRGTLKTGDS LIAGSTFGRI KAMTSDKGHA IKAAGPSIPV
EILGMDEVPE AGEVFYAVTE DKVAKHLVEK RKFKQKEQQF KATSKVTLED LFTQIKEGKV
KDLNIIIKAD VQGSVEAVKQ SLEKLSNDEV RVKTIHGAVG AITESDVTLA QVSNAIIIGF
NVRPGANVTE AAKNAEVDMR LYSVIYKAIE DVQAAMNGML EPTYKEVILG HIEIRQIFKV
SGVGTIGGAY VTDGKVQRNS EVRVVREGIV IHEGKLASLK RFKDDVKEVA QGFECGVSIE
RFNDIKEGDV IEAFVMEEVK R
