ID A0A1D2IAG4_9ACTN Unreviewed; 739 AA.
AC A0A1D2IAG4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Bifunctional (P)ppGpp synthase/hydrolase relA {ECO:0000313|EMBL:ODA71443.1};
GN Name=relA_2 {ECO:0000313|EMBL:ODA71443.1};
GN ORFNames=APS67_004410 {ECO:0000313|EMBL:ODA71443.1};
OS Streptomyces sp. AVP053U2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA71443.1, ECO:0000313|Proteomes:UP000054731};
RN [1] {ECO:0000313|EMBL:ODA71443.1, ECO:0000313|Proteomes:UP000054731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA71443.1,
RC ECO:0000313|Proteomes:UP000054731};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-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:ODA71443.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMTQ02000026; ODA71443.1; -; Genomic_DNA.
DR RefSeq; WP_062190559.1; NZ_LMTQ02000026.1.
DR AlphaFoldDB; A0A1D2IAG4; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000054731; 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:ODA71443.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000054731};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 106..203
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 450..511
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 660..734
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 79758 MW; F83184EA8AA34F6A CRC64;
MNAEAAKPAI PGPVPSGSVP SGSVPSGRAT PAGTRRKARS RLDLRRLGRA AFLGPASRGR
LPDAIGHVVD AHRAHHPDAD LDPLRRAYLL AESSHRGQMR KSGEPYITHP LAVTLILAEL
GAETTTLTAS LLHDTVEDTE VTLDQVREQF GEEVCYLVDG VTKLEKVDYG AAAEPETFRK
MLVATGNDVR VMSIKLADRL HNMRTLGVMR PEKQERIAKV TRDVLIPLAE RLGVQALKTE
LEDLVFAILR PEENKHTREL ILRNASRADD PLAEVADEVR KVLREADLAA EVLIRPRHFV
SVHRVSRKRG RLRGADFGRV LVLVNEDADC YGVLGELHTC MTPVVSEFKD FIAVPKFNLY
QSLHTAVARD DGQVVEVLIR THQMHKVAEA GVVALGNPYA APAEEQSTSD GERVDPTRPG
WLSRLLEWQR GAPDPDTFWS TLREDLAQDR EITVFRPDGG TIGLPEGATC VDAAYAQYGE
DAHACIGARV NGRLATLSTV LRDGDTVQLL MGQDPASEPS REWLEHAHTP AARIAIQRWL
TAHPADPVGQ VDPVGNDRAG SDAAQPAPRP ATGEPPAGHA PEAAPGSSGG AQILADRPGA
PVRLAGCCTP VPPDEVTGFL VRGGAVTVHR AECAAVARMK AAGRAEVGVR WGEGAECRVT
LVAESFVRPH LLADLTEAMA VEGAEIVSAT VEPPTHQQVR HTYTVQLPDA AHLPTLMRAM
RKVAGVYDVS RATPQTQGT
//
