ID A0A0D6KWZ1_9CYAN Unreviewed; 758 AA.
AC A0A0D6KWZ1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative GTP diphosphokinase {ECO:0000313|EMBL:EKF03994.1};
GN ORFNames=FDUTEX481_02997 {ECO:0000313|EMBL:EKF03994.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF03994.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKF03994.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF03994.1}.
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DR EMBL; AGCR01000013; EKF03994.1; -; Genomic_DNA.
DR RefSeq; WP_045869553.1; NZ_JH930358.1.
DR AlphaFoldDB; A0A0D6KWZ1; -.
DR STRING; 1188.FDUTEX481_02997; -.
DR PATRIC; fig|1188.3.peg.3018; -.
DR HOGENOM; CLU_012300_3_0_3; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
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; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR NCBIfam; TIGR00691; spoT_relA; 1.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF19296; RelA_AH_RIS; 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 Kinase {ECO:0000313|EMBL:EKF03994.1};
KW Transferase {ECO:0000313|EMBL:EKF03994.1}.
FT DOMAIN 66..165
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 411..472
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 680..754
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 581..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 86418 MW; 819AA38481767720 CRC64;
MSTIVLNSSI DVPLPEWLKK CLKESYRNGG VAEDDRRHND TVLIARAFQF AYQLHQGQYR
KSGEPYICHP VAVAGLLRDL GGSADMIAAG FLHDVVEDTD ITIEQIEELF SSDVRQLVEG
VTKLSKINFK SKTESQAENF RRMFLAMAQD IRVIVVKLAD RLHNMRTLQF MPEEKRRRIA
QETRDIFAPL ANRLGIWHFK WELEDLSFKY LEPEAFREIQ QHVSEKRTSR EEKLAKATAT
LRDRLQQTGI KCLDISGRPK HLYSIYQKMQ RQQKEFHEIY DLAALRIIVE TNEECYRALA
VVHDAFRPIP GRFKDYIGLP KPNRYQSLHT GVIGLTGRPL EVQIRTMEMH HIAEYGIAAH
WKYKETGNSN NSHLTATDEK FTWLRQLLEW QSDLKDAQEY LDSVKDNLFE DDVYVFTPKG
DVIPLSPGST SVDFAYRIHT EVGNHCAGAK VNGRMVPLST RLHNGDIVEV MTQKNSHPSL
DWLNFVRTSA AKYRIKQWYK RSRREENVAR GRELLEKELG KTGFESLLKS DAMHSVSEKC
NYHSVEDLLA GLGYGEITLN LVLNRWREVV KAQQPMVVAP PYLPKESPSN AKALRDAPAT
HSRASDSPIV GVEGLVYHLA GCCTPIPGEP IIGVVTRGRG ISIHRQGCNN LESVEYERLV
PVGWNNTPEH TARPHTYPVN VQIEALDRVG VLKDILSRLS DQGINVRHAQ VKTAIGQPAL
MDLGIEIRDR PQLEQVFTQI KKMSDILNIR RVGQLEDS
//
