ID A0A2M8MBN6_9ACTN Unreviewed; 569 AA.
AC A0A2M8MBN6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CUT44_02315 {ECO:0000313|EMBL:PJF01642.1};
OS Streptomyces carminius.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2665496 {ECO:0000313|EMBL:PJF01642.1, ECO:0000313|Proteomes:UP000230407};
RN [1] {ECO:0000313|EMBL:PJF01642.1, ECO:0000313|Proteomes:UP000230407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRM SA0054 {ECO:0000313|EMBL:PJF01642.1,
RC ECO:0000313|Proteomes:UP000230407};
RA Wang Y., Luo X., Wan C., Zhang L.;
RT "Streptomyces carmine sp. nov., a novel actinomycete isolated from Sophora
RT alopecuroides in Xinjiang, China.";
RL Submitted (NOV-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:PJF01642.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PGGW01000009; PJF01642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8MBN6; -.
DR Proteomes; UP000230407; 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 NCBIfam; NF033484; Stp1_PP2C_phos; 1.
DR PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00481; PP2C; 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:UP000230407}.
FT DOMAIN 21..252
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 298..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 60182 MW; 64A2362F510E1746 CRC64;
MGTVRMYPEP TGEVRMSLAL RFAAGSHKGM IREGNEDSGY AGPRLLAVAD GMGGQAAGEV
ASSEVISILV QLDDDVPGSD LLTSLGTAVQ RANEQLRVMV EEDSQLEGMG TTLTALLWTG
RRLGLVHVGD SRAYLLRDGR LSQITQDHTW VQRLVDEGRI TEEEATTHPQ RSLLMRALGS
GDRVEPDLSI REVRAGDRYL LCSDGLSGVV SHQTMEETLA GYQGPQETVQ ELIQLALRGG
GPDNITCIVA DVLDVEGGDT LAGQLNDTPV IVGAVAENQH QLGDPGTLQT PAARAAELGR
GGRGDHGQVP QQQSPEGSAG GFGPPGSGGH GNTPQEGSFD AYAGGDLSKP RGGWRWFRRS
LYLVLVLGLI GGGLYGGWRW VQTQYYVGAE GDRVAIYRGI SQKLGWIELS EVEERSPVEL
RYLPAYQRNE VRTGISMDSL EQAEARLARL AEQAEVCELV ARQRQERERA EESQDAAPGD
TGRDGSVREG GAGAGEEAGN SPSSAAVQPS AVESPAAGSP GTPAGGTART GRTGHVIHAS
DSTQSSTAPT PGPSLPEEQQ KLAKQCTTP
//
