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Database: UniProt
Entry: A0A1V0A1R1_9ACTN
LinkDB: A0A1V0A1R1_9ACTN
Original site: A0A1V0A1R1_9ACTN 
ID   A0A1V0A1R1_9ACTN        Unreviewed;       164 AA.
AC   A0A1V0A1R1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-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=BKM31_24105 {ECO:0000313|EMBL:AQZ64134.1};
OS   Nonomuraea sp. ATCC 55076.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ64134.1, ECO:0000313|Proteomes:UP000190797};
RN   [1] {ECO:0000313|Proteomes:UP000190797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX   PubMed=28626548; DOI=10.1039/c6md00637j;
RA   Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA   Seyedsayamdost M.R.;
RT   "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT   date and the kistamicin biosynthetic gene cluster.";
RL   Med. Chem. Commun. 8:780-788(2017).
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; CP017717; AQZ64134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V0A1R1; -.
DR   STRING; 1909395.BKM31_24105; -.
DR   KEGG; noa:BKM31_24105; -.
DR   Proteomes; UP000190797; Chromosome.
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:SF1; SERINE-PROTEIN KINASE RSBW; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190797};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          14..124
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
FT   REGION          130..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   164 AA;  18161 MW;  4B54FFED225CFB63 CRC64;
     MVFEFELRCP ITADLGLIRD LVRLHGRHSG LSERRLEDLV LAVNEAVTNV LDHGGKAGVV
     TARAERGQVV VDILDFAGLL THDHLASAGL DHTASHGYGL WVIQNLCDEV VLERTEHGSL
     LSLRVRERHP AGSGDRHSAG NHDQLDGWHD DDWHDDDQRQ PASH
//
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