ID A0A263DY36_9PSEU Unreviewed; 447 AA.
AC A0A263DY36;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CFP66_11585 {ECO:0000313|EMBL:OZM82386.1};
OS Pseudonocardia sp. MH-G8.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1854588 {ECO:0000313|EMBL:OZM82386.1, ECO:0000313|Proteomes:UP000216936};
RN [1] {ECO:0000313|EMBL:OZM82386.1, ECO:0000313|Proteomes:UP000216936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH-G8 {ECO:0000313|EMBL:OZM82386.1,
RC ECO:0000313|Proteomes:UP000216936};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Non-contiguous finished genome sequence and description of Pseudonocardia
RT marinum sp. nov., an obligate marine actinomycete from a macroalgal
RT phycosphere.";
RL Submitted (JUL-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:OZM82386.1}.
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DR EMBL; NKYF01000003; OZM82386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263DY36; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000216936; 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:UP000216936};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 299..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..236
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 248..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 46881 MW; 07572B6E36FB0E4D CRC64;
MTLVLRYSAR SDRGLVRQNN QDAVYAGPRL LALADGMGGH AAGEVASSLV ISALASLDED
DPGDDLLAEL RDAAVDGNAA ITRHVADAPD LEGMGTTLTA ILFAGSRLGL VHIGDSRAYQ
LRDGYLTQIT KDDTFVQSLI DEGRITEEEA HTHPQRSLLL RAITGQDIDP SLTIREARPG
DRFLLCSDGL SGVVSDETLA ETLQAYRDPR ECADRMIELA LRGGGPDNIT CIVADVVDID
FGEDAPIVGG SVGDGSEDGP PPDSAAARAS ATTLTRTAPQ QVVSTPEVRP SRRRGRLRVV
LAVVAVLAVL AGGGLLARMW VMAQYYVSAD GEQVAIFQGV GGEVLGVALQ SVAERTDVAL
TDLPETERSQ VRDGITTDNG LAGARGVVDR LRARMLEPCP PPQPPQPPPP PPPVVDPGVP
VPGIPPVDTT PLPIPAPEPG TTCRSVG
//
