ID A0A0Q9AUX2_9ACTN Unreviewed; 726 AA.
AC A0A0Q9AUX2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Kinase {ECO:0000313|EMBL:KRD22598.1};
GN ORFNames=ASE41_11710 {ECO:0000313|EMBL:KRD22598.1};
OS Streptomyces sp. Root264.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD22598.1, ECO:0000313|Proteomes:UP000051177};
RN [1] {ECO:0000313|EMBL:KRD22598.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD22598.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD22598.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD22598.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRD22598.1}.
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; LMIZ01000005; KRD22598.1; -; Genomic_DNA.
DR RefSeq; WP_057575360.1; NZ_LMIZ01000005.1.
DR AlphaFoldDB; A0A0Q9AUX2; -.
DR STRING; 1736503.ASE41_11710; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000051177; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRD22598.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000051177};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRD22598.1}.
FT DOMAIN 91..188
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 439..500
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 643..717
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 78480 MW; 9D9711B9D0335606 CRC64;
MSAEATNPAT PGPVTPATPR RRSLPRIDLR RLGRAALLGP ASRGRLPDAI SHVVEVHRAH
HPDADLEPLR RAYVLAESSH RGQMRKSGEP YITHPLAVTL ILAELGAETT ALTASLLHDT
VEDTDVTLDQ VGEEFGAEVR YLVDGVTKLE KVDYGAAAEP ETFRKMLVAT GNDVRVMSIK
LADRLHNMRT LGVMRPEKQA RIAKVTREVL IPLAERLGVQ ALKTELEDLV FAILHPEEYA
HTRELIAGNE AQETDPLAEF SDVMRAVLRE AGIQAEVLIR PRHFVSVHRV SRKRGRLRGC
DFGRLLVLVN EDADCYAVLG ELHTCMTPVV SEFKDFIAVP KFNLYQSLHT AVAREDGQVA
EVLIRTHQMH KVAEAGVIAL GNPYTASAEE HTGPGAPADE ERVDPTRPGW LSRLLDWQEA
APDPDTFWST LREDLAQDRE ITVYRPDGGA LGLPEGATCV DAAYAQYGED AHACIGARVN
GRLATLSTVL RDGDTVQLLM GQDPASEPSR EWLEHAHTPG ARIAIQRWLT THPAPAENAA
AEPAAGSVAE TAPSVRSAAD AAPADPSAPS PGAAITVVDR PDAHVRLAGC CTPVPLDEVT
GFAVRGGVVT VHRVECAAVA RMADAGREEV AVRWGDTTGC RVTLVAESFG RPHLLADLTE
AMALEGAEIV SATVEPPSQQ RVRHTYTVRL PDAAHLPDLL RAMRNVPGVY DVGRAQHHAA
APSGTR
//