ID A0A1M7TX03_9ACTN Unreviewed; 331 AA.
AC A0A1M7TX03;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05443668_107226 {ECO:0000313|EMBL:SHN75133.1};
OS Cryptosporangium aurantiacum.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=134849 {ECO:0000313|EMBL:SHN75133.1, ECO:0000313|Proteomes:UP000184440};
RN [1] {ECO:0000313|EMBL:SHN75133.1, ECO:0000313|Proteomes:UP000184440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46144 {ECO:0000313|EMBL:SHN75133.1,
RC ECO:0000313|Proteomes:UP000184440};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRCS01000007; SHN75133.1; -; Genomic_DNA.
DR RefSeq; WP_073260022.1; NZ_FRCS01000007.1.
DR AlphaFoldDB; A0A1M7TX03; -.
DR STRING; 134849.SAMN05443668_107226; -.
DR OrthoDB; 4088450at2; -.
DR Proteomes; UP000184440; 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 PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR PANTHER; PTHR35526:SF1; SERINE-PROTEIN KINASE RSBW; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF14417; MEDS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SHN75133.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184440};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:SHN75133.1}.
FT DOMAIN 12..159
FT /note="MEDS"
FT /evidence="ECO:0000259|Pfam:PF14417"
FT DOMAIN 204..316
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 331 AA; 36407 MW; 592EDA91394A1208 CRC64;
MTAAHSTGTG FDHAALIVDS DDTVQQLLVP VLRRHATDRT PVLLVVGPHT ERVLRAELGP
VAETLEWGTP DAFYQRLGFA FANFRQYLRE QHAQGRSVHV IAEPDVATDL EAPVDRVAAY
LSYESMCNDV YAAYGCPITC IWDSRRHPTL VIENVRSIHD HELTVDGRLE NDGFIPTDRY
LDGRADVTMP PAPEASDLDL VIDELDELTG CRAAISAWAT EHGFADLAAK QVSAAASEVL
TNGLRHGRPP VRVRTWHHDK TLVVHVEDRG GTPIPADAGY RPPLRPGDGM GLWVARQFAD
VLLTHTDVGC TAVRLYFPYG VTHRGLDVDE G
//
