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
//