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Database: UniProt
Entry: A0A0T1SLV0_9ACTN
LinkDB: A0A0T1SLV0_9ACTN
Original site: A0A0T1SLV0_9ACTN 
ID   A0A0T1SLV0_9ACTN        Unreviewed;       742 AA.
AC   A0A0T1SLV0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Kinase {ECO:0000313|EMBL:KQX56166.1};
GN   ORFNames=ASD33_29335 {ECO:0000313|EMBL:KQX56166.1};
OS   Streptomyces sp. Root1304.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX56166.1, ECO:0000313|Proteomes:UP000051136};
RN   [1] {ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX56166.1, ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|EMBL:KQX56166.1,
RC   ECO:0000313|Proteomes:UP000051136};
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   -!- 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:KQX56166.1}.
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DR   EMBL; LMEP01000005; KQX56166.1; -; Genomic_DNA.
DR   RefSeq; WP_056556404.1; NZ_LMEP01000005.1.
DR   AlphaFoldDB; A0A0T1SLV0; -.
DR   STRING; 1736450.ASD33_29335; -.
DR   Proteomes; UP000051136; 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; GTP PYROPHOSPHOKINASE; 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:KQX56166.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQX56166.1}.
FT   DOMAIN          97..194
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          465..529
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          659..733
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  78657 MW;  3CD943CE0D15C85E CRC64;
     MSAEATNPVS AAESADTDVT VRRRGRARID LRRLGRAALL GATAGPAPRD RLPDAISHVA
     EAHRAHHPEA DLTVLRRAYV LAESSHRGQF RKSGEAYITH PLAVTLILAE LGAETTTLTA
     SLLHDTVEDT EVTLDQVRQE FGDEVAYLVD GVTKVEKIDY GAAAEPETFR KMLVATGNDV
     RVMSIKLADR LHNMRTLGVM RPEKQARIAR VTRDVLIPLA ERLGVQALKT ELEDLVFAIL
     HPEEYETTRA LIAAEPGAGD ALDAVAEQVS AVLREAGIGA EVLVRPRHFV SVHRVRLKRG
     ELRGCDFGRL LVLVTEDADC YGVLGELHTC FTPVISEFKD FIAAPKFNLY QSLHTAVAAP
     DGAVAEVLIR THRMHKVAEA GVVALGNPHV GQEAAAPSGT EPASGAAPAS AAEDLQDTAA
     GPAEDGERVD PTRPGWLSRL LDWQQAAPDP DTFWTSLRAD LAEDDEITVF RADGSAPGTL
     SLPAGASCVD AAYAQHGEAA HGCLGARVNG RLAPLSTVLG DGDTVQLLLA HDAVSGPSPE
     WLDHARTPAA RIAISGWLAA HPESAAPAAA AGPRPAAGLV ADRRSGAELH ADLEGERPSA
     VRPAGCCTPV PPDKITGFKV RGGSVTVHRS GCAAVDTMRG LGRDPVTVRW GDTAHGRVTL
     VAESFGRPGL LADLTEAIAV AGAAVVSATV EPPSEQRVRH TYTLHLPDAA GLSALMRAMR
     DVPGVYDVSR ARHRPSQEPR RA
//
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