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Database: UniProt
Entry: A0A1V4D5E7_9ACTN
LinkDB: A0A1V4D5E7_9ACTN
Original site: A0A1V4D5E7_9ACTN 
ID   A0A1V4D5E7_9ACTN        Unreviewed;       745 AA.
AC   A0A1V4D5E7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:OPF79746.1};
GN   ORFNames=VT50_0215170 {ECO:0000313|EMBL:OPF79746.1};
OS   Streptomyces antioxidans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF79746.1, ECO:0000313|Proteomes:UP000033615};
RN   [1] {ECO:0000313|EMBL:OPF79746.1, ECO:0000313|Proteomes:UP000033615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC164 {ECO:0000313|Proteomes:UP000033615};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Streptomyces antioxidans MUSC 164.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family.
CC       {ECO:0000256|ARBA:ARBA00007476}.
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:OPF79746.1}.
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DR   EMBL; LAKD02000035; OPF79746.1; -; Genomic_DNA.
DR   RefSeq; WP_046087857.1; NZ_LAKD02000035.1.
DR   AlphaFoldDB; A0A1V4D5E7; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000033615; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 3.10.20.30; -; 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   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; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000313|EMBL:OPF79746.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          87..184
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          429..490
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          665..739
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          526..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   745 AA;  80352 MW;  96A930C3F315AFE2 CRC64;
     MSAEATDQAP FGRRRGLPRI DLRNLRRFSR AALLGSASRG RLPDAIEHVA KVHRAHHPGA
     DLDVLRNAYV LAESSHRGQM RKSGEPYITH PLAVTLILAE LGAETTTLTA SLLHDTVEDT
     DVTLDQVGEQ FGEEVRFLVD GVTKLEKVDY GAAAEPETFR KMLVATGNDV RVMSIKLADR
     LHNMRTLGVM RPEKQARIAR VTGDVLIPLA ERLGVQALKT ELEDLVFAIL HPAEYARTRE
     LLQAHADRPD PLAQAAEDVR GVLQEAGITA EVLVRPRHFV SVHRAGIKRG ELTGTDLGRL
     LVLVSDDADC YAVLGELHTC FTPVISEFKD FIAVPKFNLY QSLHTAVAGR DGEVTEVLIR
     THQMHRVAEA GVIALGNPYA PTEGADAPEG ERADPTRPGW LSRLLDWQSA TPDPDIFWTS
     LRDDLAQDRE ITVFRSDGGT LGLSAGASCV DAAYALYGDD AHSCIGARVN GRIATLSTVL
     RDGDTLQLLM ASDTRDTASH GPSPEWLDHA RTPAARIAIN RWLAAHPASQ HEPREAAEEP
     ESASELTVQD AHDTQDAQNA QDAQVTPGSE APQGGQTVAA ASPGAGRPEA GIVVDLPGAT
     VRLARCCTPV PPDAITGFAV RGGAVTVHRE RCAGAARMTS AGRTAVGVRW VDEDDGEGGG
     DYRVTLFAEA FSRPHLLADL TEAIAAEGAE VVAAAVEPPR EQRVRHTYTL QLPDAGRLPT
     LMRAMRNVPG VYDVTREGRR MAAAR
//
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