IF2_PARD8
ID IF2_PARD8 Reviewed; 973 AA.
AC A6LHS1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BDI_3534;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(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}.
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DR EMBL; CP000140; ABR45235.1; -; Genomic_DNA.
DR RefSeq; WP_005859394.1; NZ_LR215978.1.
DR AlphaFoldDB; A6LHS1; -.
DR SMR; A6LHS1; -.
DR STRING; 435591.BDI_3534; -.
DR EnsemblBacteria; ABR45235; ABR45235; BDI_3534.
DR KEGG; pdi:BDI_3534; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_0_10; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; PDIS435591:G1G5A-3626-MON; -.
DR Proteomes; UP000000566; 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..973
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008292"
FT DOMAIN 472..642
FT /note="tr-type G"
FT REGION 97..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..488
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 506..510
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 528..531
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 582..585
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 618..620
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 97..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 481..488
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 528..532
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 582..585
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 973 AA; 108318 MW; 92D0C0D9EF8ED7D5 CRC64;
MPIKLIQVQR KLNVGINTVV EFLHRNGFSV EDNPNTRISD EQYALLVKEF GKDLPEKDRN
FAADRMRKEV PSVKEEKTAE IKTVIPEEFR PKIVMKGHID LDGGQHKKQQ EEPKAKEEPK
VKEEPKVKEE PKVKEAPAAP AAQAPVKPAQ PAQAPTEKKE EKVIVVEVEK EKTVEKQPVV
AEPKVESVKP EQEVEKTEEK DDNLFRLNSV KLESKIKVTG KIDLDALNQS TRPKKKTKEE
KRKERDEKQK FNNNRPGNNS NGPGAPHKSP NSPTLIKPNA PAKPGEEGDA KKKRKRIKKD
RVDVNNTPGT NYPRPNRDDR PNNDRKPRLK KPVKAEVSEE DVQKQIKETL ARLTNKNNKN
NKGAKYRRDK RDAAVKREHE LMEQEELESK VLKLTEFVTA NDLANMMDVS VTEVIGTCMS
IGLMVSINQR LDAETINIVA EEFGYKTEYV SADVVEAINA DEEDDNEEDW VARPPIVTVM
GHVDHGKTSL LDNIRSANVI AGEAGGITQH IGAYNVKLQN GRRITFLDTP GHEAFTAMRA
RGAKVTDIAI IIVAADDNVM PQTIEAINHA SAAGVPIVFA INKIDKPHAN PEKIKEELAN
MNYLVEDWGG KYQSQEISAK KGIGVEELLE KVLLEADLLD LKANPKKRAV GSIIESSLDK
GRGYVSTILV ENGTLKMGDI VLAGTHQGRI KAMFNERNQR VEKAGPSEPV LILGLNGAPQ
AGDTFNVLET EQEAREIANR REQLQRELGL RTQKMLTLDD IGRRIAVGNF QELNVIVKGD
VDGSVEALSD SLIRLSTEEI QVNVIHKAVG QISESDVVLA AASNAIIIGF QVRPSLQARR
NAEKEGVEIR LYSIIYDAIE EVKSAMEGML SPEIKEEITA YVEVQQVFKI TKVGTVAGCM
VKEGKIKRTN KIRLIRDGIV IYAGELGSLK RFKDDAKEVV AGLDCGLNIT NFNDIQVGDM
IEAYEETEIK KTL
