ID A0A251WLN3_9CYAN Unreviewed; 1105 AA.
AC A0A251WLN3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN ORFNames=B0A82_00655 {ECO:0000313|EMBL:OUC16624.1};
OS Alkalinema sp. CACIAM 70d.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Alkalinema.
OX NCBI_TaxID=1934309 {ECO:0000313|EMBL:OUC16624.1, ECO:0000313|Proteomes:UP000194922};
RN [1] {ECO:0000313|EMBL:OUC16624.1, ECO:0000313|Proteomes:UP000194922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CACIAM 70d {ECO:0000313|EMBL:OUC16624.1};
RA Lima A.R., Siqueira A.S., Pereira J.S., Goncalves E.C.;
RT "Draft genome of Alkalinema sp. CACIAM 70d.";
RL Submitted (JAN-2017) 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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUC16624.1}.
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DR EMBL; MUGG01000005; OUC16624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251WLN3; -.
DR STRING; 1934309.B0A82_00655; -.
DR Proteomes; UP000194922; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000194922}.
FT DOMAIN 595..768
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 42..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 604..611
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 654..658
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 708..711
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1105 AA; 118269 MW; 616BE20CBE4026B1 CRC64;
MNNGKVRIYE LSKELNLENK DILAICDQLQ IAYKSHSSTI TEAEAEGIRS AAQQYSSTQV
NPSKPSPVRK SSAPTVKPRN NTPLNSQKKQ QILEIRRPVT RSDASGSEKP ELLGPPALQT
SRSSEGTVAV MPTEVEPSDR VAVTPSIEDA ALAASTVAPL EERAQSIAPE PIAPLSPVKP
DHASKAEDNQ SISHASEQAV TESAAKPTAT KPVAVKPGEG KPMEEKPAVA AKPPMPNREV
SNKETASNKE VSNKEVSNKE TATIPATNKA DGGNKPGGSP SGATKPEAPS RPSAPPAARP
VLNSKPILKA KTTTTGEKAA SSPGKSAGDA KKAGDRRPAA PGKAPISPAK PQIVELKRPK
PIASPDESGA EESTTREQPV LKGRPSRSGT PEKEAASPVE LLAKPTPPKA RRKVWEDEDE
ESAEKAKVGP KAKRRGPRIE EDDDEDFDLL DDDDSAVTPA QVSLSLARPP KPKSASAAKP
VATSTPTSQP KRRQFTRRDR RDQNSSKVEK PEIITLTGGV TVQELAQMMA VSDTEIIRNL
FMKGIAATVT QTLDVATATM VAEEMGVLVD QAEKESEAKK VIEMISEEDL ENLQRRPPVV
TIMGHVDHGK TTLLDSIRKT KVAAGEAGGI TQHIGAYHVD VEHNGEMQQV VFLDTPGHEA
FTAMRARGAR VTDVAILVVA ADDGVRPQTI EAISHAKAAG VPIIVAINKV DKEEAQPDRV
KQELTEFELV PEEWGGSTVM VPVSAMTGQN LDTLLEMILL VSEVEDLHAN PNRLAKGTVI
EANLDKAKGP VATLLVQNGT LHVGDIIVAG SALGKVRAMV DDRGRRVKEA SPSFAVEVLG
LGDVPAAGDE FEVYKDEKEA RAVADSRAEA KRQSRLMAAM SSRRVSLNTL SSKAQEGELK
ELNIVMKADV QGSVEAILGS LKQLPQNEVQ VRVLFAAPGE ISETDVDLAA ASEAVLIGFN
TTLATGARQA ADRAGVDVRE YNIIYNLLDD IQAAMEGLLE PELVEEPLGQ VEVRAVFPVG
KGAVAGCYIQ SGKAIRNCKI RVKRRGNLIF EGNLDSLKRM KEDTKEVNAG YECGIGIDNF
NAWEEGDIIE TFRMVTKRRT LTPSR
//
