ID A0A366ZH08_9ACTN Unreviewed; 366 AA.
AC A0A366ZH08;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=DQ238_17215 {ECO:0000313|EMBL:RBY76430.1};
OS Geodermatophilus sp. TF02-6.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2250575 {ECO:0000313|EMBL:RBY76430.1, ECO:0000313|Proteomes:UP000253027};
RN [1] {ECO:0000313|EMBL:RBY76430.1, ECO:0000313|Proteomes:UP000253027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-6 {ECO:0000313|EMBL:RBY76430.1,
RC ECO:0000313|Proteomes:UP000253027};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Simposon S., Morris K.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Geodermatophilus sp. TF02-6.";
RL Submitted (JUL-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:RBY76430.1}.
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DR EMBL; QOHF01000020; RBY76430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366ZH08; -.
DR Proteomes; UP000253027; 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: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:RBY76430.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253027};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:RBY76430.1}.
FT DOMAIN 62..205
FT /note="MEDS"
FT /evidence="ECO:0000259|Pfam:PF14417"
FT DOMAIN 251..362
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 38730 MW; 73D2232343F68F04 CRC64;
MTTRTGHLGG AAGAGARGRR TVGRDDPVRE RSGAVDRAAG EHRTPTAVPH PGSGHPASPR
VRHGAAVVDG EAELLAAAVS FLEEGLRAGD LVALASPPET AELARAELGE RVPVDPALSL
LGARAPDVLA RVRRSAEEAA AGRGGRLRIL SQVDLGPYPA GWREGLRLES AANRFLGDAA
VDVLCVYDRQ RLPAEVVDHA ARTHPLLVRD GAWSVSPAFR DPAAYLRELP WPREPVEDTA
PVLAVDDAPG LAALRHALGA VLADRVPDRE QREDLLLAAA EVAANAFRHG ERPVSARIWT
DGRRVVCAIT DSGHTFADPL AGFQPAHGAD LSRGGMGLWL ARKLWDSVDL FPGPAGLTVR
LSSRLR
//