RSH3C_ARATH
ID RSH3C_ARATH Reviewed; 715 AA.
AC Q9SYH1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable GTP diphosphokinase RSH3, chloroplastic;
DE EC=2.7.6.5;
DE AltName: Full=RelA/SpoT homolog 3;
DE Short=AtRSH3;
DE AltName: Full=ppGpp synthetase RSH3;
DE Flags: Precursor;
GN Name=RSH3; OrderedLocusNames=At1g54130; ORFNames=F15I1.23;
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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18535838; DOI=10.1007/s00425-008-0758-5;
RA Mizusawa K., Masuda S., Ohta H.;
RT "Expression profiling of four RelA/SpoT-like proteins, homologues of
RT bacterial stringent factors, in Arabidopsis thaliana.";
RL Planta 228:553-562(2008).
CC -!- FUNCTION: Possesses ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC synthetase activity in vitro and is able to functionally complement
CC E.coli relA mutants. May be involved in a rapid plant ppGpp-mediated
CC response to pathogens and other stresses.
CC {ECO:0000269|PubMed:18535838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, shoots, cotyledons,
CC rosette and cauline leaves, stems, petals, sepals, stamens, pistils and
CC siliques. {ECO:0000269|PubMed:18535838}.
CC -!- INDUCTION: Circadian-regulation with a peak at dusk.
CC {ECO:0000269|PubMed:18535838}.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; AC006577; AAD25787.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33053.1; -; Genomic_DNA.
DR EMBL; AK227169; BAE99211.1; -; mRNA.
DR PIR; D96582; D96582.
DR RefSeq; NP_564652.2; NM_104291.8.
DR AlphaFoldDB; Q9SYH1; -.
DR SMR; Q9SYH1; -.
DR BioGRID; 27078; 3.
DR STRING; 3702.AT1G54130.1; -.
DR iPTMnet; Q9SYH1; -.
DR PaxDb; Q9SYH1; -.
DR PRIDE; Q9SYH1; -.
DR ProteomicsDB; 228065; -.
DR EnsemblPlants; AT1G54130.1; AT1G54130.1; AT1G54130.
DR GeneID; 841853; -.
DR Gramene; AT1G54130.1; AT1G54130.1; AT1G54130.
DR KEGG; ath:AT1G54130; -.
DR Araport; AT1G54130; -.
DR TAIR; locus:2014335; AT1G54130.
DR eggNOG; KOG1157; Eukaryota.
DR HOGENOM; CLU_012300_7_1_1; -.
DR InParanoid; Q9SYH1; -.
DR OMA; PNCKLRM; -.
DR OrthoDB; 505873at2759; -.
DR PhylomeDB; Q9SYH1; -.
DR BioCyc; ARA:AT1G54130-MON; -.
DR BRENDA; 2.7.6.5; 399.
DR PRO; PR:Q9SYH1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYH1; baseline and differential.
DR Genevisible; Q9SYH1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IMP:TAIR.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IDA:TAIR.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR007685; RelA_SpoT.
DR Pfam; PF04607; RelA_SpoT; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS51831; HD; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; GTP-binding; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Stress response; Transferase; Transit peptide.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..715
FT /note="Probable GTP diphosphokinase RSH3, chloroplastic"
FT /id="PRO_0000429850"
FT DOMAIN 237..341
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 65..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 79715 MW; 599E4941B05BFEB1 CRC64;
MVVATTIALY ASPASTVCST AHQINAHISC DLDLNSRSSS ASSSTSSPTI GGLSLLFSGA
SVKSSSSSSS SHPSVGEELA SIRHDRSEDR TLSGSFCYSP SKFIGSSYLK RDHQSPVSVL
HGPISSGNSP PMRISRDRNL DGGSALRVGS SRLFNGFVRK AIGSCVDYDT DSVLVDEQLP
FTMDDGFEGE RRQPYARDLL RRAQLKHKIF EDESVIKAFY EAEKAHRGQM RATGDPYLQH
CVETAMLLAD IGANSTVVVA GILHDTLDDS FMSYDYILRT FGSGVADLVE GVSKLSQLSK
LARENNTACK TVEADRLHTM FLAMADARAV LIKLADRLHN MMTLYALPPV KRQRFAKETL
EIFAPLANRL GISSWKVKLE NLCFKHLHPD QHHEMSDMLE DSFDEAMITS AIEKLEQALK
KEGISYHVVS GRHKSLYSIY CKMLKKKLTM DEIHDIHGLR LIVDNEKDCY KALGVVHKLW
SEVPGKLKDY ISHPKFNGYQ SLHTVVMGDG TIPLEVQIRT KEMHLQAEFG FAAHWRYKEG
DCKHSSFVLQ MVEWARWVVT WHFETMSKDG SSICSSEPLC SFPSHAEDCP FSYKPSGNQE
GPVYVIVIEN EKMTVQEFPE NSTVSDLLRR AGPGSSRWSM YSIPAKEELR PRLNQTPVSD
LKCKLKMGDV VELTPAIPDK SLTEYREEIQ RMYDRGLAFS RPHRAATGTM VGWGS
