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Database: UniProt
Entry: A0A1I0ZN08_9PSEU
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ID   A0A1I0ZN08_9PSEU        Unreviewed;       309 AA.
AC   A0A1I0ZN08;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=SAMN05216266_107118 {ECO:0000313|EMBL:SFB26742.1};
OS   Amycolatopsis marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=490629 {ECO:0000313|EMBL:SFB26742.1, ECO:0000313|Proteomes:UP000243799};
RN   [1] {ECO:0000313|Proteomes:UP000243799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3568 {ECO:0000313|Proteomes:UP000243799};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FOKG01000007; SFB26742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0ZN08; -.
DR   STRING; 490629.SAMN05216266_107118; -.
DR   OrthoDB; 4088450at2; -.
DR   Proteomes; UP000243799; Unassembled WGS sequence.
DR   GO; GO:0016301; F: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.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:SFB26742.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243799};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:SFB26742.1}.
FT   DOMAIN          13..155
FT                   /note="MEDS"
FT                   /evidence="ECO:0000259|Pfam:PF14417"
FT   DOMAIN          195..305
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
SQ   SEQUENCE   309 AA;  32883 MW;  0874BE5E248E610E CRC64;
     MTARNAETGT FSHPALFYRG RDEYLAGTVP FVLDGLAAGE PVAVAVPGGN LDLIKAELGT
     AAASVHLVNM EQAGLNPGRI IPGVLLAFAN QHEGAVRVIG EPIWPGRSEL EYPACAQHEA
     LINRAFAGRS ATVLCPYDTV GLAAEVVEDA EATHPELIRN DGSMTSASYD PDRIIKQYNF
     ALDRPADAPS SAFDLSGLRD VRSFAVARGT ELGVRDELLD DLALIVAELS ANSVVHGGGT
     GALWIWREDD HVVCEVNDNG HLADPLAGRV PARPDQLGGR GLLMVNQIAD LVRVYSEPGS
     TMVRAYLRV
//
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