ID A0A0D2NKW1_GOSRA Unreviewed; 990 AA.
AC A0A0D2NKW1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic {ECO:0000256|ARBA:ARBA00044105};
GN ORFNames=B456_002G104300 {ECO:0000313|EMBL:KJB13983.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB13983.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB13983.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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|ARBA:ARBA00025162}.
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}.
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DR EMBL; CM001741; KJB13983.1; -; Genomic_DNA.
DR RefSeq; XP_012462583.1; XM_012607129.1.
DR AlphaFoldDB; A0A0D2NKW1; -.
DR STRING; 29730.A0A0D2NKW1; -.
DR EnsemblPlants; KJB13983; KJB13983; B456_002G104300.
DR GeneID; 105782406; -.
DR Gramene; KJB13983; KJB13983; B456_002G104300.
DR KEGG; gra:105782406; -.
DR eggNOG; KOG1145; Eukaryota.
DR OMA; CGIGVED; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000032304; Chromosome 2.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 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; 1.
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT DOMAIN 461..634
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 104..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 105905 MW; A283645AD62B1F2B CRC64;
MVIVVGTMPS SSLASLVNLG TLNATFINYF SEPISSSYYS CVRRVSLSKR SFSRKCKCKY
SVAPTDFVAE ANNSSSYKDS DEIVLKPAPK PVLKSEGVKN DKGLSWNAEL SEGEDEDKEE
NERNKVIESL GEVLEKAEKL ETSNVNVNVN VNKPKASGDG SGSGGGKKAK TLKSVWRKGD
TVGIVQKVVK ESPKVNDKKG EGKVESQGES AAAPLRPPQP PVRPQPKLQA KPAVAPPPVV
KKPVILKDVG AGQKLESDTD GKSKERKPIL IDKFASKKSV VDPVIAQAVL APTKPGKGPA
PGKFKDDYRK KNVSAGGPRR RIISDDLEIP DEETSELNVS IPGAANSRKG RKWSKARRKA
ARIQAAKEAA PVKVEILEVG EKGMSVEELA YNLAIGEGEI LGYLYSKGIK PDGVQTLDKD
MVKMVCKEYE VEVIDADPVK VEQMAKKKEI FDEDDLDKLQ DRPPVLTIMG HVDHGKTTLL
DVIRKSKVAA SEAGGITQGI GAYKVLVPID GKPQPCVFLD TPGHEAFGAM RARGARVTDI
VIIVVAANDG IRPQTNEAIA HAKAAGVPIV IAINKIDKDG ANPERVMQEL SSVGLMPEVW
GGDIPVVQIS ALKGQNIDDL LETVMLVAEL QELKANPDRN AKGTIIEAGL HKSKGSVATF
IVQNGTLKRG DVVVCGEAFG KVRALFDDGG NRVDEAGPSI PVQVIGLNNV PLAGDEFEVV
DSLDVAREKA EACAELLRNE RMSAKAGDGK VTLSSLASAV SAGKLSGLDL HQLNIILKVD
LQGSIEAVRQ ALQVLPQDNV TLKFLLEATG DVSTSDVDLA VASKAIILGF NVKTPGPVKS
YAENKGVEIR LYRVIYELID DVRNAMEGLL EPVEEQVPIG SAEVRAVFSS GSGRVAGCMV
TEGKIVDGCG IRVIRNGRTV HVGVLDSLRR VKEIVKEVNA GLECGMGVED YDQWQEGDIL
EAFTTVQKKR TLEEASASMA AALEGVGVEL
//
