ID A0A1J1LQF6_9CYAN Unreviewed; 1041 AA.
AC A0A1J1LQF6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ECO:0000313|EMBL:CUR34816.1};
GN ORFNames=PL9214650255 {ECO:0000313|EMBL:CUR34816.1};
OS Planktothrix tepida PCC 9214.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=671072 {ECO:0000313|EMBL:CUR34816.1, ECO:0000313|Proteomes:UP000184315};
RN [1] {ECO:0000313|Proteomes:UP000184315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Regsiter A., william w.;
RL Submitted (OCT-2015) 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}.
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DR EMBL; CZDF01000172; CUR34816.1; -; Genomic_DNA.
DR RefSeq; WP_072721593.1; NZ_LN889813.1.
DR AlphaFoldDB; A0A1J1LQF6; -.
DR STRING; 671072.PL9214650255; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000184315; 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:UP000184315}.
FT DOMAIN 537..710
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 35..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 546..553
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 596..600
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 650..653
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1041 AA; 112287 MW; F088AEEA77CF5600 CRC64;
MNNAKVRIYE LSRELNLDNK DILAVCERLN ISVKSHSSTI SESDKERIEK YVATHPNPGQ
LDGKSERSHP NGKSSATAPG EKKKQEILEI QKPRIRPNSD VSAVYGSADS PASTSVATPP
KSLVSPKAPV KPTLNRPVLS KPNAPAQAGT ESSETTASEY SQAEQIGIPA PAEENTSFEE
VDLDLSEPPQ LSPPPVRPAS PVPVSSVPIS VVTTETAPIV KNKPVLKTNK PAPKSVEPKS
KTDGPERPTP KPQQAPSLAS AETKEKDSEA RKPPRKEIGT PRPSRSVPEL QPPPARKSAV
QAIDDDAEPS ESAEEEPLIA TDDLIKRPKR AAVTLTRPNP PRTGKRGPEW EEEEEEVVDT
GKAKSAKVKS KRRAKPSLDE DDDDELNALS LSNANNAMMS ISLARPPKPK AGPGQGNVAA
TTAKPKKQAP SRGGGSSAAN MRRTEAKPKA ERPEKVIVPG PMTVQELATA LALPETEIIK
RLFSQGIAVN ITETLDYNTI LVICQELNVQ VETEEQVSGA IKPDNIFNEE DLEHLQRRPP
VVTIMGHVDH GKTTLLDAIR ETKVAQGEAG GITQHIGAYH VDVEHEGKTQ QVVFLDTPGH
EAFTAMRARG ARVTDVAILV VAADDGVQPQ TIEAISHAKA AGVPMIIAIN KIDKEGAQPD
RVKQELTEFS LVPEEWGGDT IMVPVSAIKG ENLDTLLEMI LLVAEVEDLY ANPNRAAKGT
IIEAHLDKSR GPVATLLVQN GTLRVGDIVV AGSVLGKVRA MVDDRGDRVD EASPSFAVEV
LGLRDVPAAG DEFDVFENEK EASALATSRA ETKRQTRLTK GRISLSEFSA RAQEGELKEL
NLILKADVQG SVEAIVNALK KLPQKEVELQ LLLAAPGEIT ETDIDLAAAS DAVLLGFNTT
LAHGARQAAD RAGVDIRDYN IIYNLLDDVQ AAMEGLLEPE LVEEALGQVE VRAIFPVGRS
TVAGCYVLSG KVIRNCKVRV RRKGEIVHEG ALDSLKRMKE DAKEVNAGYE CGIALDNFND
WNMGDIIEAY RMTTKRRTLT L
//
