ID A0A1T3NW11_9ACTN Unreviewed; 555 AA.
AC A0A1T3NW11;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=B4N89_08540 {ECO:0000313|EMBL:OPC80988.1};
OS Embleya scabrispora.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Embleya.
OX NCBI_TaxID=159449 {ECO:0000313|EMBL:OPC80988.1, ECO:0000313|Proteomes:UP000190037};
RN [1] {ECO:0000313|EMBL:OPC80988.1, ECO:0000313|Proteomes:UP000190037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF3 {ECO:0000313|EMBL:OPC80988.1,
RC ECO:0000313|Proteomes:UP000190037};
RA Vazquez M., Ceapa C.D., Rodriguez Luna D., Sanchez Esquivel S.;
RT "Draft genome sequence of Streptomyces scabrisporus NF3, endophyte isolated
RT from Amphipterygium adstringens.";
RL Submitted (MAR-2017) 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:OPC80988.1}.
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DR EMBL; MWQN01000001; OPC80988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T3NW11; -.
DR STRING; 159449.B4N89_08540; -.
DR Proteomes; UP000190037; Unassembled WGS sequence.
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:SF267; 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 Reference proteome {ECO:0000313|Proteomes:UP000190037}.
FT DOMAIN 302..518
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 58023 MW; FC54E2A1B81A5B06 CRC64;
MPARGGFPER TLRQDELRAE RPAAVDDDIF GDLYLDFEDA PTRTPVEPSA APEPVAEPAV
EARAPRGFDD TFAAEPADPA APADRPEFDH DAAPAERPDT DHAPTAVGEP DGARAASPRD
RAPRPAETFA AEAADAEPAP DPVPHTVTPP AVRSESRAEA VPPPPTIAAA GSTDTTLASA
PAVPPPPTVP PMPTEPPRVP EPPYTPEAAG VPQTPYTPDA ARAPETPHAP EAAPTPEART
ELLPVAADAV EEPDELDVPT TSRSDSLRRA EATEEEIRAR SGPPLGVQAS AWSTSSHPGR
RRAARRERRG LGPELTARDN DDRYAATGEV FIVADGLGGH PAGWYAADVA VRTLVSELAA
ADLSAGWSDR LGAAIAVADL AVRRHGVAQY EGMRTTVVAA VLQHGRLHLA GCGDSVCWLV
RGGRAFRLTE QGNAAEFGRP WLLTSTPLGG SQAPEPELQR IELHPGDRVV LATDGVGHLP
DETVADLVHG DPFHAATTLT RTAVESGDDD ATAVVVECDA LPVPEGHRSG ADPREQSEDA
SGTPGALRSD GGTAW
//
