RSH3L_ARATH
ID RSH3L_ARATH Reviewed; 712 AA.
AC Q9M5P5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 82.
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;
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 [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10725385; DOI=10.1073/pnas.97.7.3747;
RA van der Biezen E.A., Sun J., Coleman M.J., Bibb M.J., Jones J.D.;
RT "Arabidopsis RelA/SpoT homologs implicate (p)ppGpp in plant signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3747-3752(2000).
CC -!- FUNCTION: Probable ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC synthetase that may be involved in a rapid plant ppGpp-mediated
CC response to pathogens and other stresses. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; AF225704; AAF37283.1; -; mRNA.
DR AlphaFoldDB; Q9M5P5; -.
DR SMR; Q9M5P5; -.
DR ExpressionAtlas; Q9M5P5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Stress response; Transferase; Transit peptide.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..712
FT /note="Probable GTP diphosphokinase RSH3, chloroplastic"
FT /id="PRO_0000429851"
FT DOMAIN 237..338
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 712 AA; 79372 MW; A7CAD39800AFFC28 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 GVSQLSKLAR
ENNTACKTVE ADRLHTMFLA MADARAVLIK LADRLHNMMT LYALPPVKRQ RFAKETLEIF
APLANRLGIS SWKVKLENLC FKHLHPDQHH EMSDMLEDSF DEAMITSAIE KLEQALKKEG
ISYHVVSGRH KSLYSIYCKM LKKKLTMDEI HDIHGLRLIV DNEKDCYKAL GVVHKLWSEV
PGKLKDYISH PKFNGYQSLH TVVMGDGTIP LEVQIRTKEM HLQAEFGFAA HWRYKEGDCK
HSSFVLQMVE WARWVVTWHF ETMSKDGSSI CSSEPLCSFP SHAEDCPFSY KPSGNQEGPV
YVIVIENEKM SVQEFPENST VSDLLRRAGP GSSRWSMYSI PAKEELRPRL NQTPVSDLKC
KLKMGDVVEL TPAIPDKSLT EYREEIQRMY DRGLAFSRPH RAATGTMVGW GS