ID C1CW63_DEIDV Unreviewed; 760 AA.
AC C1CW63;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Putative GTP diphosphokinase (PpGpp synthetase I) (RelA/SpoT) (GTP pyrophosphokinase) {ECO:0000313|EMBL:ACO46430.1};
GN OrderedLocusNames=Deide_14760 {ECO:0000313|EMBL:ACO46430.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO46430.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO46430.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC -!- SIMILARITY: Belongs to the RelA/SpoT family.
CC {ECO:0000256|ARBA:ARBA00007476}.
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DR EMBL; CP001114; ACO46430.1; -; Genomic_DNA.
DR RefSeq; WP_012693553.1; NC_012526.1.
DR AlphaFoldDB; C1CW63; -.
DR STRING; 546414.Deide_14760; -.
DR PaxDb; 546414-Deide_14760; -.
DR KEGG; ddr:Deide_14760; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_0; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000002208; Chromosome.
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; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR PANTHER; PTHR43061; GTP DIPHOSPHOKINASE RSH1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR43061:SF1; GTP DIPHOSPHOKINASE RSH1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACO46430.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW Transferase {ECO:0000313|EMBL:ACO46430.1}.
FT DOMAIN 41..150
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 417..478
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 673..747
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 577..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..413
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 760 AA; 85193 MW; FD69ABDE075B62C5 CRC64;
MNELRALVGG RLQSDRDRIE LAYEFARDAH EGVNRKSGEP YITHPVAVAV ILARLGMDTE
SVMAGLLHDT VEDVEGVTFE SIEELFGPDV RRIVEGETKV SKLSKQGSQQ AEVAHTGRDM
QAENLRQMLI AMTADIRIIV VKLADRLHNM RTLGSMKPEK QQRIARETME IFAPLAHRLG
IGKIKWELED LSFQYLQPDD YAYLQSRLRT RQEERDALIQ GAVKQLREAL EDDLELPEWV
GEIDIAGRSK HLWSIHTKMK REGKALEQIF DLLAIRVILT PKDLIVPPGT DEKRRERAEE
TREKRICYHT VSIVHSMWTP LPGRFKDYIA VPKPNGYQSL HTTVISQSGQ PIEVQIRSRR
MHEVAEYGVA AHWMYKQGAQ LAARDRENWI SQLKELQNEI NDASDYMDAV KSDILSQRVR
VFTPKGLAIS LPAGSTSIDF AYHIHTRIGE TTVGSRVNGS IVPLSHHLKN GDMVEIVTSK
NGKPSKDWLN FAVTRSARAK IRHHFRTQER EDALKRGHDL LERYLRKRQL PVRQLMRTKL
LEDATHKLVG TRNPDDLYLA LHAAKTTPSA VARVLSPSLA QEQSSVPPGR RAPVPRPPEP
GGVYVEGFTT NTKLSQCCNP IRGDQIMGYL TRGRGVSVHR IDCPNMIRLL KDEPERCVAA
SWNSGTPGNI IMDLDVIAQD RSGLLADVLS VLAAEKRSPM KLEAGVSADN TATIHLRLAM
AGNSDLERLR AALLRVDGVT DLVRAGKSRN GGRARNGASA
//
