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Database: UniProt
Entry: A0A3S8W8G3_9ACTN
LinkDB: A0A3S8W8G3_9ACTN
Original site: A0A3S8W8G3_9ACTN 
ID   A0A3S8W8G3_9ACTN        Unreviewed;       633 AA.
AC   A0A3S8W8G3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Protein phosphatase {ECO:0000313|EMBL:AZM53188.1};
GN   ORFNames=DMA15_11770 {ECO:0000313|EMBL:AZM53188.1};
OS   Streptomyces sp. WAC 01529.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2203205 {ECO:0000313|EMBL:AZM53188.1, ECO:0000313|Proteomes:UP000269043};
RN   [1] {ECO:0000313|EMBL:AZM53188.1, ECO:0000313|Proteomes:UP000269043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 01529 {ECO:0000313|EMBL:AZM53188.1,
RC   ECO:0000313|Proteomes:UP000269043};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP029617; AZM53188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S8W8G3; -.
DR   OrthoDB; 9807247at2; -.
DR   Proteomes; UP000269043; Chromosome.
DR   CDD; cd16936; HATPase_RsbW-like; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1.
DR   PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
PE   4: Predicted;
FT   DOMAIN          393..632
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|SMART:SM00331"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   633 AA;  67350 MW;  DB9FE3659493FE17 CRC64;
     MQRETEFRAC AKDPDRPRPP AVVRTSLPGT SLSPADARQF VRAALADWCE LDVPAAAGLT
     DRVADDAVLL VSELVTNAVV HAGTAVELLC RLDEAGPGEE TDTLVIEVSD HHPSRAVRGE
     QHPPPSGTPE YGRGLQLVAT LSESWGITYR TGTKTVWARL PVEGARSGHD SEPSVSEQAP
     QRGPRTADLL APLPKRVTHD TEWVNRGALS FLAEASDLLA GQFDEDLVAA LAGQLLVPRL
     ADWCAVWLDD ASEGQARAAP GAPGARLARV WHTCEHRVEE LRRVLEKDPP WLPEAAGSGA
     CPVPWPGEGP ASESSGTALA YRLTAGGRAL GTLVIGRTGL LRFPDEVTGL IEDFSRRVAL
     AVSTARRYQR QANISQVLQR GLLPSKVAQI PGVQSGLVYE PRDKGGPGGD FYDVFQAGAG
     RWCFALGDVQ GKGPEAAVVI GLARPWLRLL AREGYQVAEV LDRLNQLLLD DATEAADAAA
     AVVAVAGGQG VPTDGATARF LSLLYGELVP YEGGVRCTIA CAGHPLPLLL SPEGEVRAAA
     TPQMLLGVVD DETYTSESFD LRTGDTLLCV TDGVTERRSG RLQFDDGDGL ARALAECAGL
     GAGVVAERIR RLVHEFSERP PDDDMALLVL RAE
//
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