ERG_ARATH
ID ERG_ARATH Reviewed; 437 AA.
AC O82653; Q6DBE6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=GTP-binding protein ERG;
GN Name=ERG; OrderedLocusNames=At1g30960; ORFNames=F17F8.15;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
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.-D., 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.-P., 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]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-410.
RX PubMed=9768362; DOI=10.1016/s0960-9822(98)70445-2;
RA Ingram G.C., Simon R., Carpenter R., Coen E.S.;
RT "The Antirrhinum ERG gene encodes a protein related to bacterial small
RT GTPases and is required for embryonic viability.";
RL Curr. Biol. 8:1079-1082(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND SER-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
CC -!- FUNCTION: Has a crucial role in plant growth and development, possibly
CC by influencing mitochondrial division.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01050, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC000107; AAF98187.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31297.1; -; Genomic_DNA.
DR EMBL; BT015076; AAT71948.1; -; mRNA.
DR EMBL; BT015910; AAU95446.1; -; mRNA.
DR EMBL; Y17969; CAA76979.1; -; Genomic_DNA.
DR PIR; C86435; C86435.
DR RefSeq; NP_174383.1; NM_102835.5.
DR AlphaFoldDB; O82653; -.
DR SMR; O82653; -.
DR BioGRID; 25218; 1.
DR STRING; 3702.AT1G30960.1; -.
DR iPTMnet; O82653; -.
DR PaxDb; O82653; -.
DR PRIDE; O82653; -.
DR ProteomicsDB; 220576; -.
DR EnsemblPlants; AT1G30960.1; AT1G30960.1; AT1G30960.
DR GeneID; 839983; -.
DR Gramene; AT1G30960.1; AT1G30960.1; AT1G30960.
DR KEGG; ath:AT1G30960; -.
DR Araport; AT1G30960; -.
DR TAIR; locus:2015771; AT1G30960.
DR eggNOG; KOG1423; Eukaryota.
DR HOGENOM; CLU_038009_2_0_1; -.
DR InParanoid; O82653; -.
DR OMA; YVIDHRL; -.
DR OrthoDB; 586738at2759; -.
DR PhylomeDB; O82653; -.
DR PRO; PR:O82653; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O82653; baseline and differential.
DR Genevisible; O82653; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IDA:TAIR.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR CDD; cd04163; Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTP-bd_Era.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR42698; PTHR42698; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR TIGRFAMs; TIGR00436; era; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51713; G_ERA; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..437
FT /note="GTP-binding protein ERG"
FT /id="PRO_0000180080"
FT DOMAIN 152..333
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 361..437
FT /note="KH type-2"
FT REGION 39..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..167
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 186..190
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 207..210
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 279..282
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 309..311
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 160..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 207..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 279..282
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 40
FT /note="P -> A (in Ref. 4; CAA76979)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..255
FT /note="Missing (in Ref. 4; CAA76979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49671 MW; 5F1AA1B32A50EE4D CRC64;
MKAFRSLRIL ISISRTTTKT TPRNPHQAQN FLRRFYSAQP NLDEPTSINE DGSSSDSVFD
SSQYPIDDSN VDSVKKPKEA TWDKGYRERV NKAFFGNLTE KGKVKVAEEE SSEDDEDSVD
RSRILAKALL EAALESPDEE LGEGEVREED QKSLNVGIIG PPNAGKSSLT NFMVGTKVAA
ASRKTNTTTH EVLGVLTKGD TQVCFFDTPG LMLKKSGYGY KDIKARVQNA WTSVDLFDVL
IVMFDVHRHL MSPDSRVVRL IKYMGEEENP KQKRVLCMNK VDLVEKKKDL LKVAEEFQDL
PAYERYFMIS GLKGSGVKDL SQYLMDQAVK KPWEEDAFTM SEEVLKNISL EVVRERLLDH
VHQEIPYGLE HRLVDWKELR DGSLRIEQHL ITPKLSQRKI LVGKGGCKIG RIGIEANEEL
RRIMNRKVHL ILQVKLK
