ID A0A5D0NG91_9ACTN Unreviewed; 430 AA.
AC A0A5D0NG91;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-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=FXF69_26435 {ECO:0000313|EMBL:TYB43363.1};
OS Actinomadura chibensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=392828 {ECO:0000313|EMBL:TYB43363.1, ECO:0000313|Proteomes:UP000323380};
RN [1] {ECO:0000313|EMBL:TYB43363.1, ECO:0000313|Proteomes:UP000323380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14158 {ECO:0000313|EMBL:TYB43363.1,
RC ECO:0000313|Proteomes:UP000323380};
RA Songsumanus A., Kuncharoen N., Kudo T., Yuki M., Igarashi Y.,
RA Tanasupawat S.;
RT "Actinomadura sp. nov. CYP1-5 isolated from mountain soil.";
RL Submitted (AUG-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:TYB43363.1}.
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DR EMBL; VSFG01000006; TYB43363.1; -; Genomic_DNA.
DR RefSeq; WP_067884011.1; NZ_VSFG01000006.1.
DR AlphaFoldDB; A0A5D0NG91; -.
DR STRING; 1220554.GCA_001552135_00169; -.
DR Proteomes; UP000323380; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR025874; DZR.
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; PF12773; DZR; 1.
DR Pfam; PF13672; PP2C_2; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000323380};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 123..408
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 37..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 43083 MW; 4C44A69D8C528D13 CRC64;
MTGDPGGAKA AELTCPSCGE IVFADEIFCE ECGHRLAESP PAAPAAPAPG AEPPAPDRVD
ATVVQSTPSA RRRASGRPCA GCGAATIDAD GYCEACGLRQ PAERDHVEIE LPAPGGNGTR
PVVAAGASDR GRRYSRNEDA IAIAAHSAGI AAVVSDGVGS SQRPDDASRT AADTGAAELV
ARLDAGDDPE EATRAAALAA AAAVAALSTS PAEAPSCTYV SAVTRGPAVT VGWVGDSRAY
WLAADGSVDD PAAEGSALDA AEVSTGDMAE LGPSRRLTDD DSWAAFMVAQ GSLTEAEAEA
HPNAHVITAW MGADAGQVNP HVATFRPSRP GTLLVCSDGL WNYFPAAGDI AALLAAGPDG
PGGAEAAAGA PDPGHDPAAD PLAVARTLVR HALDAGGRDN ITVAVIPLPP PAVPQSRVHP
SIPQSTEQPR
//
