ID A0A505D2D5_9ACTN Unreviewed; 431 AA.
AC A0A505D2D5;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=FGD71_045015 {ECO:0000313|EMBL:TPQ15825.1};
OS Streptomyces sporangiiformans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2315329 {ECO:0000313|EMBL:TPQ15825.1, ECO:0000313|Proteomes:UP000317378};
RN [1] {ECO:0000313|EMBL:TPQ15825.1, ECO:0000313|Proteomes:UP000317378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-SSA 1 {ECO:0000313|EMBL:TPQ15825.1,
RC ECO:0000313|Proteomes:UP000317378};
RA Han L.;
RT "Streptomyces sporangiiformans sp. nov., a novel actinomycete isolated from
RT soil in Mount Song.";
RL Submitted (JUN-2019) 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:TPQ15825.1}.
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DR EMBL; VCHX02000347; TPQ15825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A505D2D5; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000317378; 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 InterPro; IPR026870; Zinc_ribbon_dom.
DR PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR Pfam; PF13672; PP2C_2; 1.
DR Pfam; PF13240; zinc_ribbon_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:UP000317378}.
FT DOMAIN 166..421
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 83..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 44640 MW; 8903A299E254FCCE CRC64;
MMSQMPPALS KCPSCEEPLE SGDRFCGACG YDLSAVPAPP HDSPTMTMNG AVPRPTSAGG
PVDWPVAPEV DSSDMPAPVH VPTDIQGTDS GGSELPAEVR FDGHPEPDEY ALQAPDPRTA
DFATPSAGTK LCVACRAGQV DRDGYCENCG HAQPRERDHM EQELGAVAAV SDRGLRHHRN
EDAFAVSSTA LPDGSPAVVA VVCDGVSSAT RPDEASLAAS RAANEALLDS LPRGAHPQQA
MHDAIIAASQ AVNSLAGTTP PDEHAPHQNA PACTLVGAVV TPSLLIVGWV GDSRAYWVPV
DRGSPAARLT EDDSWAAQMV AAGLMSEAEA YADERAHAIT GWLGADAYEL EPHTASFKPD
RPGVVVVCTD GLWNYAEAAE EMAEVIPPDA AVRPLHSAQV LVGHALDGGG HDNVTVAVLP
FPAPPQGAGS A
//
