CRSH3_ORYSJ
ID CRSH3_ORYSJ Reviewed; 578 AA.
AC Q75IS2; A0A0N7KK72; A7VL54;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=GTP diphosphokinase CRSH3, chloroplastic {ECO:0000305};
DE EC=2.7.6.5 {ECO:0000269|PubMed:17938177};
DE AltName: Full=Calcium-activated RelA/Spot homolog 3 {ECO:0000303|PubMed:17938177};
DE Short=OsCRSH3 {ECO:0000303|PubMed:17938177};
DE AltName: Full=ppGpp synthetase CRSH3 {ECO:0000303|PubMed:17938177};
DE Flags: Precursor;
GN Name=CRSH3 {ECO:0000303|PubMed:17938177};
GN OrderedLocusNames=Os05g0161800 {ECO:0000312|EMBL:BAS92409.1},
GN LOC_Os05g06940 {ECO:0000305};
GN ORFNames=OSJNBb0099P06.1 {ECO:0000312|EMBL:AAT07650.1};
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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, DOMAIN, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
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).
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).
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 {ECO:0000255}.
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; AB298325; BAF76773.1; -; mRNA.
DR EMBL; AC124144; AAT07650.1; -; Genomic_DNA.
DR EMBL; AP008211; BAH92957.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92409.1; -; Genomic_DNA.
DR RefSeq; XP_015638151.1; XM_015782665.1.
DR AlphaFoldDB; Q75IS2; -.
DR SMR; Q75IS2; -.
DR STRING; 4530.OS05T0161800-01; -.
DR PaxDb; Q75IS2; -.
DR PRIDE; Q75IS2; -.
DR EnsemblPlants; Os05t0161800-01; Os05t0161800-01; Os05g0161800.
DR GeneID; 9270381; -.
DR Gramene; Os05t0161800-01; Os05t0161800-01; Os05g0161800.
DR KEGG; osa:9270381; -.
DR eggNOG; KOG1157; Eukaryota.
DR HOGENOM; CLU_022292_1_0_1; -.
DR InParanoid; Q75IS2; -.
DR OMA; DDELRCT; -.
DR OrthoDB; 505873at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..578
FT /note="GTP diphosphokinase CRSH3, chloroplastic"
FT /id="PRO_0000429856"
FT DOMAIN 99..199
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 468..503
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 506..537
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 481
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 487
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 515
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 521
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 CONFLICT 333
FT /note="Missing (in Ref. 1; BAF76773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 61843 MW; 893BDFA7695D2F17 CRC64;
MANAGVNETV AVAVAIDAPG VGHDHGAAGE VRRPSTRRLA PAGSGGRLMA ELLGVFNGLT
ERMGEDVATS SSSRLLFRAL KLALPALRDG GGDGGGGQSV SRALVVAASL ADLQMDAEVI
SAGMVRGALD TGALAMADVE AQLGASAAGL VEESLKVKRA PSEVDVADEE AASALRKRCL
SSYDIRAVIL ELAVKLDAMK HLDVLPKHQQ RTTSLEVLKV FALLAHAVGA GELSLELEDL
SFQRLYPQAY AHIDQWLSSQ EDDCKRVIAA SKEELLRALT ADDELRCTVT GVDVMGRYKS
RFSTMKKLVK DGRRPEDVND ILGMRVILDP RPGGGGGGDG DGGDRACLRT HEVIKAMWKD
VPARTKDYIT RPKGNGYRSL HVAVDMSEPG PEGKKRPLME IQVRTREMDM AAVGGQASHA
LYKGGLTDPE EAKRLKAIML AAAEVAAQHL RDEPAGDGGQ TTAAASAATA GNVERAFQLL
DKNGDGRISM EELTEIMEDL GAGGHDAEEL MRLLDANSDG SLSSDEFALF QKRVKLKTKL
ENKDDEYKEI LKQKLQKVDD TGLIHVYRKN LSDKLVLV
