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Database: UniProt
Entry: A0LNV4_SYNFM
LinkDB: A0LNV4_SYNFM
Original site: A0LNV4_SYNFM 
ID   A0LNV4_SYNFM            Unreviewed;       281 AA.
AC   A0LNV4;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Sfum_3435 {ECO:0000313|EMBL:ABK19106.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK19106.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK19106.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) 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; CP000478; ABK19106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0LNV4; -.
DR   STRING; 335543.Sfum_3435; -.
DR   KEGG; sfu:Sfum_3435; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_0_3_7; -.
DR   InParanoid; A0LNV4; -.
DR   Proteomes; UP000001784; 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   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:UP000001784}.
FT   DOMAIN          6..253
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          63..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  30227 MW;  62B318D785303A0E CRC64;
     MMVVEASGLT DKGKERANNE DALLVDDQLQ LYVVADGMGG HRAGEVASEL VVRSMSGFFR
     NSGRVARSRE REEDGEEVPS DPTLSAEAGR LLAGIRRANR AVYVQALSND EWRGMGSTVA
     AVRFTDRGMI AANVGDSPIW LVHGDRIEML SVAHTVLSEG LVSEREEAGR RFGRILTRAI
     GVGETVRADI CEAQCFAGDV VVIGSDGLSN HVHPDEIMDV VRGDSPASAC RLLVDLANRR
     AGDDNITVIV IKVKNVGRRA GFVSRFATTI TAGLRRLVSK A
//
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