IF2_SYNJA
ID IF2_SYNJA Reviewed; 1031 AA.
AC Q2JSB7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CYA_2338;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(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; CP000239; ABD00465.1; -; Genomic_DNA.
DR RefSeq; WP_011431138.1; NC_007775.1.
DR AlphaFoldDB; Q2JSB7; -.
DR SMR; Q2JSB7; -.
DR STRING; 321327.CYA_2338; -.
DR EnsemblBacteria; ABD00465; ABD00465; CYA_2338.
DR KEGG; cya:CYA_2338; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008818; 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 PRINTS; PR00315; ELONGATNFCT.
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..1031
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335515"
FT DOMAIN 522..695
FT /note="tr-type G"
FT REGION 33..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..436
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 103..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..349
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 1031 AA; 111749 MW; 10EFE49AD57CD452 CRC64;
MTDRVRLYEI AREMGCDNRE VLEVCEQLGI PFKSHSSTIS PEQAELVRSK LSEPRVVKPT
RPRLRPKLQP ESSQPQPPVE AKASERPQHI VGIRRPAPAQ QQAAAGEASS SKPSPQRPDQ
LSSEKGAAGG SLELIGPPRR QVDPPARPAA QEPQPAAAST RPEAAAKAGS PEPSPAPAAK
RPTVLPPPRR AASGPEPPQR APESRRPGLA EAPSPSGART SPPVEEKVSL PQAEQRPRPQ
LVGAPVRPGT RPEPRSPVAK KEESSDSGKA DEAPRPQRRL ELVGPPTRPV AKPLPPEPDA
SPRLPEGIPE ERPTPVLAEA PVRPAAPKLK RKTVEEEDEE LQALERRAGR TQAKRKRSRR
REEGDGDVLD LDPLTVLSSV KQAELNALKP LARPTAKPPS YRPPAAAARP RPAAERPQRP
SASAEATAPE AAAESLPEEK VLLLEGSLTV QELARRLRVA ETEIIKTLFF KGVRVTINQV
LDESLAESVA KELGYEVRRP EAEPKAKKTE ILDLEDIDHL VPRPPVVTIM GHVDHGKTTL
LDAIRHTNVA QREAGGITQR IGAYHVDVDF EGQKRRIVFL DTPGHQAFTA MRARGARVTD
IAVLVVAADD GVQPQTLEAL SHARAAQVPI IVAINKIDKP GSQPERVKQQ LAEHGLLPEE
WGGDTPMVEV SALTRRNLDA LLEMILLVAD VAELQANPNR PARGTVIEAH LDKARGPVAT
LLVQNGTLRV GDTLVAGAVL GRVKAMMDDR GQRLQEAGPS SAVQLLGLEE VPAAGDEFQV
YADEKEARRI AEERAEALRQ ARLQQALLSR RVSLGSISAK AQEGQLKELN LIIKTDVQGS
AEAIQTALQD LPQEEVRLRV LLAAPGEITE TDVDLAAASD AIILGFNTSF APGARQAADD
KGVDVREYDI IYNLLDDLRA AMEGLLEPEE VEEPLGQAEV RKVIPISRGA VAGSYVLSGK
VQRNALVRVR RKGEVVYQGR LDSLKRFKDD VREVAAGFEC GIGIEKFDAW QEGDLIEVYQ
MVTKRRTLAP A
