ID A0A3R9WEH0_9ACTN Unreviewed; 470 AA.
AC A0A3R9WEH0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=EF918_32790 {ECO:0000313|EMBL:RSS60577.1};
OS Streptomyces sp. WAC06614.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487416 {ECO:0000313|EMBL:RSS60577.1, ECO:0000313|Proteomes:UP000277644};
RN [1] {ECO:0000313|EMBL:RSS60577.1, ECO:0000313|Proteomes:UP000277644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC06614 {ECO:0000313|EMBL:RSS60577.1,
RC ECO:0000313|Proteomes:UP000277644};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivate of ubiquitous gene clusters.";
RL Submitted (NOV-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:RSS60577.1}.
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DR EMBL; RPRY01000444; RSS60577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9WEH0; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000277644; 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:UP000277644}.
FT DOMAIN 212..462
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 31..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 47186 MW; 13A19F11B654AD75 CRC64;
MSMHRPSGCP SCAEPLEEGD RFCGVCGYDV SVPPPSATAP TDTTAPTAPT APTAPAAGPD
RPTLPLHSPP DQARDTTFGF GFAAAPPATA GGATPTAPGT PAAPGAPGAP GAAGRPTRYD
TPAPAAAVAH DPEPDDPRSG PVPPAPEQPA ADAPGTGAPA GDGPAGDTAA PGGTGKVCVA
CRAGRVDTDG YCEHCGHAQP RERDHLEEEL GSVAAVSDRG LRHHRNEDSF AVAATALADG
STATVAIVCD GVSSASRPDD ASAAAAATAN EFLLDALPRG THPQEAMHEA ILAAAQAVNA
LAPEVPGAQN APACTLVGAV VSGGLLTIGW VGDSRAYWVP DDRAALPRRL TEDDSWAAQM
VAAGLMGEAE AYADVRAHAI TGWLGADAYE LEPHTRTFRP DHPGVVVVCT DGLWNYAESA
QEMAHVLPAD AAEHPLHSAQ VLVGHALDGG GHDNVTVAVV PFAVPPGPDA
//
