ID Q8L835_ARATH Unreviewed; 532 AA.
AC Q8L835;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit {ECO:0000256|ARBA:ARBA00015765};
DE AltName: Full=ERF-3 {ECO:0000256|ARBA:ARBA00031881};
DE AltName: Full=ERF2 {ECO:0000256|ARBA:ARBA00030845};
DE AltName: Full=Polypeptide release factor 3 {ECO:0000256|ARBA:ARBA00029585};
DE AltName: Full=Translation release factor 3 {ECO:0000256|ARBA:ARBA00030210};
GN OrderedLocusNames=At1g18070 {ECO:0000313|Araport:AT1G18070,
GN ECO:0000313|EMBL:AEE29670.1};
GN ORFNames=T10F20.8 {ECO:0000313|EMBL:AEE29670.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:AAM53327.1};
RN [1] {ECO:0000313|EMBL:AEE29670.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2] {ECO:0000313|EMBL:AAM53327.1}
RP NUCLEOTIDE SEQUENCE.
RA Southwick A., Karlin-Neumann G., Nguyen M., Tripp M., Miranda M.,
RA Palm C.J., Bowser L., Jones T., Banh J., Carninci P., Chen H., Cheuk R.,
RA Chung M.K., Hayashizaki Y., Ishida J., Kamiya A., Kawai J., Kim C., Lin J.,
RA Liu S.X., Narusaka M., Pham P.K., Sakano H., Sakurai T., Satou M., Seki M.,
RA Shinn P., Yamada K., Shinozaki K., Ecker J., Theologis A., Davis R.W.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAP68328.1}
RP NUCLEOTIDE SEQUENCE.
RA Kim C.J., Chen H., Cheuk R., Shinn P., Bowser L., Carninci P., Dale J.M.,
RA Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G.,
RA Kawai J., Lam B., Lin J., Miranda M., Narusaka M., Nguyen M., Onodera C.S.,
RA Palm C.J., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A.,
RA Toriumi M., Wong C., Wu H.C., Yamada K., Yu G., Shinozaki K., Davis R.W.,
RA Theologis A., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007829|PubMed:19376835}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5] {ECO:0000313|EMBL:AEE29670.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0007829|PubMed:22223895}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7] {ECO:0000313|EMBL:AEE29670.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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 -!- 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; AY120769; AAM53327.1; -; mRNA.
DR EMBL; BT008889; AAP68328.1; -; mRNA.
DR EMBL; CP002684; AEE29670.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29671.1; -; Genomic_DNA.
DR RefSeq; NP_001031063.1; NM_001035986.1.
DR RefSeq; NP_173247.1; NM_101669.3.
DR AlphaFoldDB; Q8L835; -.
DR SMR; Q8L835; -.
DR MetOSite; Q8L835; -.
DR ProteomicsDB; 187169; -.
DR EnsemblPlants; AT1G18070.1; AT1G18070.1; AT1G18070.
DR EnsemblPlants; AT1G18070.2; AT1G18070.2; AT1G18070.
DR GeneID; 838387; -.
DR Gramene; AT1G18070.1; AT1G18070.1; AT1G18070.
DR Gramene; AT1G18070.2; AT1G18070.2; AT1G18070.
DR Araport; AT1G18070; -.
DR TAIR; AT1G18070; -.
DR HOGENOM; CLU_007265_3_8_1; -.
DR OMA; GKMESGC; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L835; baseline and differential.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:InterPro.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03704; eRF3_C_III; 1.
DR CDD; cd04089; eRF3_II; 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; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003285; Sup35.
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 PANTHER; PTHR23115:SF36; TR-TYPE G DOMAIN-CONTAINING 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 PRINTS; PR01343; YEASTERF.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Elongation factor {ECO:0000313|EMBL:AEE29670.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:AEE29670.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q8L835,
KW ECO:0007829|ProteomicsDB:Q8L835};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 99..325
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 27..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 59243 MW; 53162B6392C97188 CRC64;
MDLEAEIRAL QLESADENNG VVIPEVHNSH EVENLDKAPE DLKDEVQESI PVPDEQEASE
DHDEVMLHPV HNPAKAKEKA AQEKAAKEEA EDVAEANKKR HLNVVFIGHV DAGKSTIGGQ
ILFLSGQVDD RQIQKYEKEA KDKSRESWYM AYIMDTNEEE RLKGKTVEVG RAHFETESTR
FTILDAPGHK SYVPNMISGA SQADIGVLVI SARKGEFETG YERGGQTREH VQLAKTLGVS
KLIVVVNKMD DPTVNWSKER YDEIEQKMVP FLKASGYNTK KDVVFLPISG LMGKNMDQRM
GQEICPWWSG PSFFEVLDSI EIPPRDPNGP FRMPIIDKFK DMGTVVMGKV ESGSIREGDS
LVVMPNKEQV KVVAIYCDED KVKRAGPGEN LRVRITGIED EDILSGFVLS SIVNPVPAVT
EFVAQLQILE LLDNAIFTAG YKAILHIHAV VEECEIIELK SQIDLKTRKP MKKKVLFVKN
GAAVVCRIQV TNSICIEKFS DFPQLGRFTL RTEGKTIAVG KVTELLSSVS SA
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