ID A0A1I4JAL4_9ACTN Unreviewed; 472 AA.
AC A0A1I4JAL4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=SAMN04488085_114108 {ECO:0000313|EMBL:SFL63156.1};
OS Geodermatophilus ruber.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=504800 {ECO:0000313|EMBL:SFL63156.1, ECO:0000313|Proteomes:UP000199152};
RN [1] {ECO:0000313|EMBL:SFL63156.1, ECO:0000313|Proteomes:UP000199152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45317 {ECO:0000313|EMBL:SFL63156.1,
RC ECO:0000313|Proteomes:UP000199152};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FOSW01000014; SFL63156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4JAL4; -.
DR STRING; 504800.SAMN04488085_114108; -.
DR InParanoid; A0A1I4JAL4; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000199152; 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 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:UP000199152};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 300..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..235
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 241..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 49045 MW; 907AEB5F051F01F9 CRC64;
MSLSLRYAAR SDRGLVRGNN QDSVYAGPRL LAVADGMGGH AAGDVASKVV IAALEHLDDD
APSGDMLQAL RAAVFEGSEH LREVIRESPQ LEGMGTTLTA ILFAGGRLAL CHVGDSRAYL
LRDGALTQIT HDDTFVQTLI DDGRITPEEA NHHPQRSLLL RALNGQDVDP DLSMREARAG
DRYLLCSDGL SGVVSEETLA EALKDPDPQS TADRLIELAL RSGGPDNITV IVADVVEDSG
HTPPLDPVVD GAAGDNVGQR EVDPRSAAGR AALADPPPPP PSTAAPTAAA PPPSRSRRRL
LWALGGALLV AAAAVGAYLW VLSNWFVGVQ DTADGERVAV YRGIDASLLG MELNRVAAVT
DLDVADLTPA DTSKVRRGIE ATDGAHADRI VAMLEEQSLP VCADLEPPTE PAPTSEAAPT
TEAAPSPPPG PEPAPGANGA EPGISAAPTD TTPPVAPPTK TLEPGVDCRE VE
//
