ID A0A3A4ADN8_9ACTN Unreviewed; 323 AA.
AC A0A3A4ADN8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=D5H75_28800 {ECO:0000313|EMBL:RJL24784.1};
OS Bailinhaonella thermotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Bailinhaonella.
OX NCBI_TaxID=1070861 {ECO:0000313|EMBL:RJL24784.1, ECO:0000313|Proteomes:UP000265768};
RN [1] {ECO:0000313|EMBL:RJL24784.1, ECO:0000313|Proteomes:UP000265768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 75507 {ECO:0000313|EMBL:RJL24784.1,
RC ECO:0000313|Proteomes:UP000265768};
RA Tang S., Feng Y.;
RT "YIM 75507 draft genome.";
RL Submitted (SEP-2018) 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:RJL24784.1}.
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DR EMBL; QZEY01000014; RJL24784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A4ADN8; -.
DR OrthoDB; 3748385at2; -.
DR Proteomes; UP000265768; Unassembled WGS sequence.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; 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 InterPro; IPR025847; MEDS_domain.
DR InterPro; IPR047718; RsbA-like_anti_sig.
DR NCBIfam; NF041045; RsbA_anti_sig; 1.
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.
DR Pfam; PF14417; MEDS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:RJL24784.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265768};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:RJL24784.1}.
FT DOMAIN 17..162
FT /note="MEDS"
FT /evidence="ECO:0000259|Pfam:PF14417"
FT DOMAIN 204..317
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 323 AA; 34144 MW; 45E045D2AE89F3FF CRC64;
MADRNTARAT GLSPAHHQAQ FYSCREELVD AALPFLRDGV EERDLVFAVS GPGNVAAFRE
RLGPRASKVA FADAGRWFAQ PLRTLRAVHA LADTAESRGS GYLRLLGEQP WCGRTPAQVA
ASIRYEAVLD AVCADRGVRS LCPYDLSAAP AEAVNAARRA HPVLSGGSGP ARSPDYLGPH
GLLAVCDSRE LPEPPPEAVV HGFAHPRDLL ALRHRVREYG TAAGLAPSRV QEVVLAVHEL
AANILVHALS PGMIRMWAAP GDVVFDVVAP GPPPPPHPDG YLPPDLDGLG GRGLWLIQTL
SGDVESGTTA AGATTRIHAG PDR
//
