ID IF2_SYNP6 Reviewed; 1030 AA.
AC Q5N0A5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=syc2075_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(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; AP008231; BAD80265.1; -; Genomic_DNA.
DR RefSeq; WP_011244385.1; NC_006576.1.
DR AlphaFoldDB; Q5N0A5; -.
DR SMR; Q5N0A5; -.
DR KEGG; syc:syc2075_d; -.
DR eggNOG; COG0532; Bacteria.
DR Proteomes; UP000001175; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..1030
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228253"
FT DOMAIN 522..695
FT /note="tr-type G"
FT REGION 56..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..538
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 556..560
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 581..584
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 635..638
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 671..673
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 183..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 531..538
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 581..585
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 635..638
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1030 AA; 110570 MW; 0AB450400867F9E5 CRC64;
MNNGKVRIYE LSKELNLDNK DVLAVCDRLE IPYKSYSSTL SEEQVVQVRQ VLAGAAPSEP
VAAASAADSP KAERKQEIVS VRRPTPQAAG GAKPEIVGRP TASEKPQAER PNIVAPPRRP
AAANEPAKAP IKPARPEKSA EKPEIVTPRP PAPAASAEPA KSPSRPAPAA TPRPVAETKK
PKPAAAELLR KPEIVRRSEA KPERTSEAPT PRPKIERRPE QTGPARPQLG QPVAGNGVSK
PAKPVKPIEL VAPPSRPKVA ASASGVPAAA SRVLPNKPQK PTAPGGPELK QRPKPAAPAS
GEDLAATVDV FQPVPPLELR RPTAPARPAR PRKGWEEEED ERAAANRKAG NKAAAKAKRR
QLIQDDDDDD LLTAEQELAA ADALNLAMSL ARPSKPKVPQ AKPAVAVMPT KGRKPRRESA
RERQHRRRME REQKPVRPEL ISLRSSMTVQ ELAQLMVVPE TDIIKSLFFK GIAATVTQSL
DVATIEQVAE EFGILVEQET EESGARKTTQ MVEDADAESL QTLPPVVTAM GHVDHGKTTL
LDAIRKTRVA AGEAGGITQH IGAYHVDVEH NGDQHQIVFL DTPGHEAFTA MRARGARVTD
IAILVVAADD GVRPQTLEAI SHAKAAEVPL IVAINKCDKE EAQPDRVKQE LTEYGLVPEE
WGGETVMVPV SAIKGENIDQ LLEMILLVTE VEELVANPDR AARGTVIEAH LDKARGPVAT
LLVQNGTLRV GDVLVAGSVL GKVRAMVDDR GDRVEAATPS FAVEVLGLGD VPAAGDEFEV
YSDEKSARAV ATSRADEQRQ SRLQQAMASR RVSLGTVSAQ AQEGELKELN LILKADVQGS
VEAILGSLEQ LPQKQVQVRV LLAAPGEITE TDVDLAAASG AVIVGFNTTL ASGAKRAADE
AGVDVRDYDI IYKLLEDIQA AMEGLLEPEL VEEPLGQVEV RAVFSIGRGA VAGCYVQSGK
AIRNCNIRVR RGSNLVYTGT LDSLKRMKED VKEVNSGYEC GIGLDSFSAW QEGDIIETYR
MVTKRRTLEV
//
