ID A0A429ATL9_9ACTN Unreviewed; 428 AA.
AC A0A429ATL9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=DMB42_33815 {ECO:0000313|EMBL:RSN03674.1};
OS Nonomuraea sp. WAC 01424.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2203200 {ECO:0000313|EMBL:RSN03674.1, ECO:0000313|Proteomes:UP000286861};
RN [1] {ECO:0000313|EMBL:RSN03674.1, ECO:0000313|Proteomes:UP000286861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01424 {ECO:0000313|EMBL:RSN03674.1,
RC ECO:0000313|Proteomes:UP000286861};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-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:RSN03674.1}.
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DR EMBL; QHHZ01000013; RSN03674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429ATL9; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000286861; 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 NCBIfam; NF033484; Stp1_PP2C_phos; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000286861};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 305..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..237
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 400..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 45259 MW; 6890430C09B1B030 CRC64;
MTIALRYAAR SDVGLLREGN EDSAYASGRL LAVADGMGGH AHGEVASSVA IAAMASLEEA
QQGGDLLNAI EAAVRDANRR LHEMVGRDPS LKGMGTTLTA MLWNGTQVAL VHVGDSRAYL
LRRGELYQIT HDHTLVQQLV DDGRITPEEA ATHPQRSILL RALDGSGEVD PDLTLREAQV
GDRYLLCSDG LSGVVSAETL HATLTNIDDP EEVVRQLIDL ANRGGGPDNI TCVLADVVEL
AEGQQVPVEA AVVGAAGMTR LRGGDQETSP GRVSAVTAPQ PAITGDDFDE PVAQAARRPG
KRRRVWPVLV TVLGIGAVAV GAGGYLGYQW TQDQFFVGAR GDEVVIFQGI KQEVGPFQFF
HVEKSTGRPL SKLSPADQAL IKSGIPVTDV DEGVTKINGL KFSQDDTGDA TSTSDTSPTP
TATKTKSR
//
