ID A0A0Q6FC62_9ACTN Unreviewed; 317 AA.
AC A0A0Q6FC62;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=ASG49_09755 {ECO:0000313|EMBL:KQT92217.1};
OS Marmoricola sp. Leaf446.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Marmoricola.
OX NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT92217.1, ECO:0000313|Proteomes:UP000051542};
RN [1] {ECO:0000313|EMBL:KQT92217.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT92217.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT92217.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT92217.1,
RC ECO:0000313|Proteomes:UP000051542};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC {ECO:0000256|ARBA:ARBA00037972}.
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:KQT92217.1}.
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DR EMBL; LMRF01000002; KQT92217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q6FC62; -.
DR STRING; 1736379.ASG49_09755; -.
DR OrthoDB; 5244329at2; -.
DR Proteomes; UP000051542; Unassembled WGS sequence.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR PANTHER; PTHR35526:SF3; STAS DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Reference proteome {ECO:0000313|Proteomes:UP000051542};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 11..115
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
FT REGION 74..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 35344 MW; 0E83049F46616859 CRC64;
MVPLTKRSLV LPASPPSVKL ARSWVTRVLA EIGRDDLVES AALGVSELVT NALIHSQPPL
SVRIRGTVDH PRIEVVDSSP VPPQRSEMSP EPEDVDDLNV TTFGRGLDLV AMMSARWGSD
LAHDGSSKSV WFEPQGDGDH GGRTGEIFDF DPDFGLEDST EAGDEPQLNI RLLRLPPRLF
SLLRTFYYET RRELRLLSLT SPENYPLAHE MTAAYVQADR ERRVAVGVST LDQAIADNLE
TVDLDYLVPA TAPVTMARLR DLYVEIYREF ADEHLLALRP PEVIVELQNW YFTEFERQGR
GDAPLPWDGP TSVVTTA
//
