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Database: UniProt
Entry: A0A367ASU7_9ACTN
LinkDB: A0A367ASU7_9ACTN
Original site: A0A367ASU7_9ACTN 
ID   A0A367ASU7_9ACTN        Unreviewed;       472 AA.
AC   A0A367ASU7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=DQ244_08455 {ECO:0000313|EMBL:RBY92300.1};
OS   Blastococcus sp. TBT05-19.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=2250581 {ECO:0000313|EMBL:RBY92300.1, ECO:0000313|Proteomes:UP000253254};
RN   [1] {ECO:0000313|EMBL:RBY92300.1, ECO:0000313|Proteomes:UP000253254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBT05-19 {ECO:0000313|EMBL:RBY92300.1,
RC   ECO:0000313|Proteomes:UP000253254};
RA   Ennis N., Dharumadurai D., Sevigny J., Hall J., Simpson S., Morris K.,
RA   Thomas W.K., Tisa L.S.;
RT   "Genome Sequence of Blastococcus sp. TF05-19.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001482};
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:RBY92300.1}.
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DR   EMBL; QOHI01000002; RBY92300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367ASU7; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000253254; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992:SF233; ALPHABET, ISOFORM E; 1.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        303..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..235
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          267..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..445
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  49384 MW;  05A38870930A3D60 CRC64;
     MTLVLRYAAR SDRGLIRGNN QDSVYAGPRL LAVADGMGGH AAGDVASKVV IAALEHLDDD
     APSGDMLQAM RSAVFEGSEH LREVIRESPQ LEGMGTTLTA ILFAGGRLAL CHVGDSRAYL
     LRDGQFSQIT HDDTFVQTLI DDGRITVEEA NHHPQRSLLL RALNGQEVEP DLSMREARAG
     DRYLLCSDGL SGVVSEETLA EAMLDPDPQA TADRLIELAL RSGGPDNITV IVADVVEDTG
     GGGRLDPVVD GAAGDNVGQR QVDARSAAGR AALADAPPAS APPPTPTLPT GGGPSARRRP
     LRILLVAGAL LIVLVAGAIG TYVWALNHWF VGVDGTGEDS QVAVFRGLDV SVLGLDLYRL
     DRDTDLAVAD LTPAARTRVK GSITADDSGD VDRILEALRD QQLPLCRTLD AEATEPTPPP
     TPSPAVPTPP PPPVPGEPAL PEPPAPEEAT TTSSSARTTT SSEPGVNCRE AS
//
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