ID I1PQY1_ORYGL Unreviewed; 682 AA.
AC I1PQY1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA04G0260000.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA04G0260000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; I1PQY1; -.
DR STRING; 4538.I1PQY1; -.
DR EnsemblPlants; ORGLA04G0260000.1; ORGLA04G0260000.1; ORGLA04G0260000.
DR Gramene; ORGLA04G0260000.1; ORGLA04G0260000.1; ORGLA04G0260000.
DR eggNOG; KOG0458; Eukaryota.
DR HOGENOM; CLU_007265_3_3_1; -.
DR OMA; CGYKDSA; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
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; 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 PANTHER; PTHR23115:SF244; OS04G0677800 PROTEIN; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
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; 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 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 18..47
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 251..477
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 150..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 74833 MW; D0C843FAB0E4AFFF CRC64;
MFIPELDNRS DPQEPSRNPG IWQCTICEHG NDAKKISCEQ CGVLRYFSLY FNNALEVDGR
AKRRDKHYAV SVLARTLFSP SSAKSKDVVL SGGFKASRNA TGSTRATLDA LHKTYMTRKE
RHINIVPFKF DTPSPDDVVA TGLKSSRSFR KVDTDAPHVT EKRVMDNDSS TPEKDTTADS
NLPVKSNEFG ESSESVSVGS QNETLCLDHE LQHLSLERKS QKSKANIKKP VSSSLYKPEP
WMLQHEDEGI PRQLNLAIVG HVDSGKSTLC GRLLHALGRI SKKQMHKYEK EAKEKGKGSF
AYAWAMDESA DERERGITMT VGVAYFDTKN YHVVLLDSPG HKDFVPNMIS GATQSDAAIL
VIDASIGSFE AGMGINGIGQ TKEHSQLVRS FGVDNLIVVV NKMDSVEYSK ERFNFIKSQL
GAFLRSCGYK DSAVAWVPIS AMENENLMTT ASDTRLSSWY DGNCLLKAID TLPPPSRDVS
KPLRLPICDV FSSHKLGQVA IGGKVEVGAT RSGSKILVMP FGELAVVKTI ERNSSSCNLA
RAGDNVAIGL QGIDPSHVMP GGVICHPDYP VSVASCLELK ILVLDITVPI LVGLQFELHI
HHAKVSASMV KILSLLEQKT GKASKKIPRF LTSRQTAVIE VKLEKEVCVE EFSNLKALGR
VFLRSQGNTI AVGIVSRVRE QA
//
