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Database: UniProt
Entry: A0A366ZH08_9ACTN
LinkDB: A0A366ZH08_9ACTN
Original site: A0A366ZH08_9ACTN 
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
//
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