ID B0CF40_ACAM1 Unreviewed; 269 AA.
AC B0CF40;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN OrderedLocusNames=AM1_5605 {ECO:0000313|EMBL:ABW30556.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW30556.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW30556.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW30556.1; -; Genomic_DNA.
DR RefSeq; WP_012165776.1; NC_009925.1.
DR AlphaFoldDB; B0CF40; -.
DR STRING; 329726.AM1_5605; -.
DR KEGG; amr:AM1_5605; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_034545_3_2_3; -.
DR OrthoDB; 500607at2; -.
DR Proteomes; UP000000268; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000000268}.
FT DOMAIN 4..241
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 245..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 29636 MW; 207E368CE0BA655A CRC64;
MKRLFAGLSD QGLVRKANQD SYRIDEPEGR FFIVADGMGG HAGGEEASRI AAETIQKFLV
ENWQAQLNPP DLLKKALLKA NQDIIQNQKD FPERADMGTT VVVVLFPAEG QPWCAHIGDS
RLYRWRGSQL SQITEDHTWI SQAVKSGLLT KDQARSHPWR HVLAQCLGRE ELDEIGIQQL
DVKSGDQLLL CSDGLTEELA DEQIAPFFEA KHPCETVVDA LVEAAKDEGG QDNITVVLVA
LGDGEEEESS SWADTPAMDD DPTGDLNEA
//
