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CRSH1_ORYSJ
ID   CRSH1_ORYSJ             Reviewed;         583 AA.
AC   Q6ATB4; A0A0P0WIB5; Q9AYT4;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=GTP diphosphokinase CRSH1, chloroplastic {ECO:0000305};
DE            EC=2.7.6.5 {ECO:0000269|PubMed:17938177};
DE   AltName: Full=Calcium-activated RelA/Spot homolog 1 {ECO:0000303|PubMed:17938177};
DE            Short=OsCRSH1 {ECO:0000303|PubMed:17938177};
DE   AltName: Full=ppGpp synthetase CRSH1 {ECO:0000303|PubMed:17938177};
DE   Flags: Precursor;
GN   Name=CRSH1 {ECO:0000303|PubMed:17938177};
GN   Synonyms=RELA2 {ECO:0000303|Ref.1};
GN   OrderedLocusNames=Os05g0161200 {ECO:0000312|EMBL:BAS92404.1},
GN   LOC_Os05g06890 {ECO:0000305};
GN   ORFNames=OsJ_17215 {ECO:0000312|EMBL:EEE62424.1},
GN   OSJNBa0034O12.15 {ECO:0000312|EMBL:AAT93920.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare;
RA   Tozawa Y., Satsu H., Ito Y., Ochi K.;
RT   "Rice cDNA encoding plastid ribosomal protein L11.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP   DOMAIN, AND TISSUE SPECIFICITY.
RX   PubMed=17938177; DOI=10.1074/jbc.m703820200;
RA   Tozawa Y., Nozawa A., Kanno T., Narisawa T., Masuda S., Kasai K.,
RA   Nanamiya H.;
RT   "Calcium-activated (p)ppGpp synthetase in chloroplasts of land plants.";
RL   J. Biol. Chem. 282:35536-35545(2007).
CC   -!- FUNCTION: Possesses calcium-dependent ppGpp (guanosine 3'-diphosphate
CC       5'-diphosphate) synthetase activity in vitro and is able to
CC       functionally complement E.coli relA mutants. May be involved in a rapid
CC       plant ppGpp-mediated response to pathogens and other stresses.
CC       {ECO:0000269|PubMed:17938177}.
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         Evidence={ECO:0000269|PubMed:17938177};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22090;
CC         Evidence={ECO:0000269|PubMed:17938177};
CC   -!- ACTIVITY REGULATION: Activated by calcium.
CC       {ECO:0000269|PubMed:17938177}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:17938177}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC       {ECO:0000269|PubMed:17938177}.
CC   -!- DOMAIN: The calcium-binding sites of the 2 EF-hand domains are required
CC       for enzyme activity. {ECO:0000305|PubMed:17938177}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR   EMBL; AB042936; BAB21485.1; -; mRNA.
DR   EMBL; AC137614; AAT93920.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF16638.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS92404.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE62424.1; -; Genomic_DNA.
DR   EMBL; AK121808; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015637549.1; XM_015782063.1.
DR   AlphaFoldDB; Q6ATB4; -.
DR   SMR; Q6ATB4; -.
DR   STRING; 4530.OS05T0161200-01; -.
DR   PaxDb; Q6ATB4; -.
DR   PRIDE; Q6ATB4; -.
DR   EnsemblPlants; Os05t0161200-01; Os05t0161200-01; Os05g0161200.
DR   GeneID; 4337888; -.
DR   Gramene; Os05t0161200-01; Os05t0161200-01; Os05g0161200.
DR   KEGG; osa:4337888; -.
DR   eggNOG; KOG1157; Eukaryota.
DR   HOGENOM; CLU_022292_1_0_1; -.
DR   InParanoid; Q6ATB4; -.
DR   OMA; ACYRTHE; -.
DR   OrthoDB; 505873at2759; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   Genevisible; Q6ATB4; OS.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IDA:UniProtKB.
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; cd00051; EFh; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR007685; RelA_SpoT.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51831; HD; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Chloroplast; GTP-binding; Kinase; Metal-binding;
KW   Nucleotide-binding; Plastid; Reference proteome; Repeat; Stress response;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..69
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           70..583
FT                   /note="GTP diphosphokinase CRSH1, chloroplastic"
FT                   /id="PRO_0000429854"
FT   DOMAIN          119..219
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          473..508
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          510..542
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..38
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         486
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         488
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         490
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         492
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         497
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         520
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         522
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         524
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         526
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         531
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CONFLICT        223
FT                   /note="D -> N (in Ref. 1; BAB21485)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525
FT                   /note="G -> S (in Ref. 7; AK121808)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   583 AA;  64143 MW;  31C6AC538513C54E CRC64;
     MATAATTSAA AIPTGGGGRR QHPHPRRPGL RPRRLHRLRL PAQAAAAAAA SSPSTSSSSS
     SSSTPAEGGG RLVAELVGAF NELTGRMGEG LATSSSSRLL FRALKLALPA LRDGDGGRAL
     ARALAIAASL ADLQMDAEVI SAGILREALD AGAISMRDVK SEIGISTAHL LHESLRLKHA
     PSKLDVLDDE SASALRKFCL SYYDIRAVIL ELALKLDMMR HLDCLPRYLQ RIKSLEVLKI
     YAPLAHAVGA GNLSLELEDL SFRYLFPHSY DHIDQWLRSQ ETENKLLIDS YKEQLLQALK
     DDDELSQIVQ DISIQGRYKS RFSTMKKLVK DGRKPEEVND ILALRVILEP RCDGSSLDWG
     PRACHRTHEI IQAMWKEVPG RTKNYVTRPK ENGYQSLHVA IDVSEPGKMR PLMEIQIRTK
     EMHKFAVGGE ASHSLYKGGL TDPGEAKRLK AIMLAAAELA AMRLRDLPAS DQGDSNCTNR
     AFCQLDKNGD GRISIEELTE VMEDLGAGGK DAKELMHLLD ANSDGSLSSD EFEAFQRQIE
     LMRSLDDKDD RYRKILKEKL QTIDSAGLIQ VYRKQLGDKL LVS
 
 
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