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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
 
 
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