ID IF2_MARMS Reviewed; 854 AA.
AC A6VU29;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mmwyl1_1027;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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; CP000749; ABR69958.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VU29; -.
DR SMR; A6VU29; -.
DR STRING; 400668.Mmwyl1_1027; -.
DR KEGG; mmw:Mmwyl1_1027; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_2_6; -.
DR OrthoDB; 9811804at2; -.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..854
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335490"
FT DOMAIN 354..523
FT /note="tr-type G"
FT REGION 52..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..370
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 388..392
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 409..412
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 463..466
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 499..501
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363..370
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 409..413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 854 AA; 93292 MW; F443290BFBBED005 CRC64;
MTVQTVKILS ELVSTPVDKL LAQMKDAGLP QTSASQEVSE VEKQVLLSYL KRQHGEEGDN
SQRITLQRKT TSTLSRDGGK AVNVAVKKKR TYVKRDDEEA QKQEELAKRL AEEQERLAQE
KARLELERKQ EEEKAAKAKA EAEEKARQEA AVKNVVADAG AVNETEQYVS DTGAAEPVES
PKQPKASKKV SQPAMDSKKS TVAPKGKKGP VRHDNDKDKD KPRGRVNPDN KRTSRVNVND
EDEFTRRGKL GRKNKKPSKQ EHGFQKPTAK MIHEVALPES ITVADLAEKM AVKGAEVIKI
MFKMGAMATI NQTIDRDTAT LVVEEMGHTV KFIDENAVEN DMIEAIDYQG EAIKRAPVVT
VMGHVDHGKT SLLDYIRTTR VAAGESGGIT QHIGAYHVET PHGMISFLDT PGHAAFTSMR
ARGAKATDIV ILVCAADDGV MPQTIEAIQH ARAAGVPMVV AMTKIDKEGA DIDRVKNELV
AQEVVPEEWG GDIQFVGVSA KSGEGIEALL EAVLLQAEVL ELTAVPSAPA KGVVVEARLD
RGRGSVATLL VQNGTLKKGD IVLAGLQMGR VRALLDETGK AIDSAGPSIP VEILGLDGTP
EAGEEFIVVA DERKAREVAN FRQGKYREVR FARQHSAKLE NLFSEMGKDE VRTLNVVLKA
DVRGSLEALI KSLTDMNTDE VKVNVVSSGV GGITETDATL ALASDAVIFG FNVRADNSAK
QFIERESIDL RYYSVIYNII DDVKSALSGM LSPDLREDIK GTAEVRDVFR SPKFGLIAGC
MVIEGTVYRN KQIRVLRDDV VIYEGELESL RRFKDAVNEV SRGMECGIGV KNYNDVKVGD
KIEVFETVEV ARTL
//
