GenomeNet

Database: UniProt
Entry: A0A0D2TKT3_GOSRA
LinkDB: A0A0D2TKT3_GOSRA
Original site: A0A0D2TKT3_GOSRA 
ID   A0A0D2TKT3_GOSRA        Unreviewed;       774 AA.
AC   A0A0D2TKT3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B456_009G068500 {ECO:0000313|EMBL:KJB55206.1};
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:KJB55206.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB55206.1, 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: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR   EMBL; CM001748; KJB55206.1; -; Genomic_DNA.
DR   EMBL; CM001748; KJB55209.1; -; Genomic_DNA.
DR   EMBL; CM001748; KJB55211.1; -; Genomic_DNA.
DR   RefSeq; XP_012443238.1; XM_012587784.1.
DR   RefSeq; XP_012443239.1; XM_012587785.1.
DR   RefSeq; XP_012443240.1; XM_012587786.1.
DR   RefSeq; XP_012443241.1; XM_012587787.1.
DR   RefSeq; XP_012443242.1; XM_012587788.1.
DR   RefSeq; XP_012443243.1; XM_012587789.1.
DR   RefSeq; XP_012443244.1; XM_012587790.1.
DR   AlphaFoldDB; A0A0D2TKT3; -.
DR   STRING; 29730.A0A0D2TKT3; -.
DR   EnsemblPlants; KJB55206; KJB55206; B456_009G068500.
DR   EnsemblPlants; KJB55209; KJB55209; B456_009G068500.
DR   EnsemblPlants; KJB55211; KJB55211; B456_009G068500.
DR   GeneID; 105768066; -.
DR   Gramene; KJB55206; KJB55206; B456_009G068500.
DR   Gramene; KJB55209; KJB55209; B456_009G068500.
DR   Gramene; KJB55211; KJB55211; B456_009G068500.
DR   KEGG; gra:105768066; -.
DR   eggNOG; KOG0458; Eukaryota.
DR   OrthoDB; 470716at2759; -.
DR   Proteomes; UP000032304; Chromosome 9.
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:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd16267; HBS1-like_II; 1.
DR   CDD; cd04093; HBS1_C_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   DOMAIN          42..71
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          345..569
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          192..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  84359 MW;  47F1C5DCD4A71DBE CRC64;
     MPRKVNCGID YDDGYDDDFD DYDYGYDVEE NVKEPSLQDT IKRGVWRCSV CTYDNDDTMS
     SCDICGILRS PSVSNGTYDE KRTVHGICKV SGVSIMAKSL FASRPHQMSK KEVDSQQQND
     DFVVKENNNF HMLGNNQGQF HEFHKAYSSP THSRINIAPF KFDVPSPDDL VSNGLHSSAQ
     HSKAKIFDFK SSRAPSRGVG KNEAVKVLSS AKSSDSSHDS TGKDKHDGII FSKNLEINTS
     SGFKASDKSS ASMAKGRVED SDGRSVSINL CSSGQSSSSL MPKERTDMVE DGSSLTHGGE
     GHLTSNLKNM TLGAKSGNSK DIKANSRAQY KPEKWMFPEK AEGSLTQLNL AIVGHVDSGK
     STLSGRLLHL LGRISRKEMH KYEKESKLQG KGSFAYAWAL DESAEERERG VTMTVAVTYL
     DSKRYHVVVL DSPGHKDFVP NMITGATQAD AAILVIDASI GSFEAGMDGT KGQTREHAQL
     IRSFGVDQII VAVNKMDAVE YSKDRFDLIK SQLGTFLRSC DFKDSSVTWI PLSAVENQNL
     VVAPSDLRLS WYHGPYLLDA IDSFQPSSRD FSKPLLMPIC DVIKSSQGQV SACGKLEAGA
     VRSGSKVLVM PSADIATVRS LERDSQTCSI ARAGDNVAIN LHGIDGNHVI AGGVLCHPDF
     PVAFAKHLEL KVLVVDGATP ILMGSQLEFY AHHAKEAARV ARISSLLDSK TGKVAKKAPR
     CIVAKQSAVI ELVLQESICI EMFSKCKALG RVFLRTLGRT VAVGVVTRIV EELV
//
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