ID   Q3M1S6_TRIV2            Unreviewed;       617 AA.
AC   Q3M1S6;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Ava_A0002 {ECO:0000313|EMBL:ABA25060.1};
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OG   Plasmid pAnaB {ECO:0000313|Proteomes:UP000002533}.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=240292 {ECO:0000313|EMBL:ABA25060.1, ECO:0000313|Proteomes:UP000002533};
RN   [1] {ECO:0000313|Proteomes:UP000002533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937 {ECO:0000313|Proteomes:UP000002533};
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000120; ABA25060.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M1S6; -.
DR   KEGG; ava:Ava_A0002; -.
DR   HOGENOM; CLU_463605_0_0_3; -.
DR   Proteomes; UP000002533; Plasmid pAnaB.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABA25060.1};
KW   Plasmid {ECO:0000313|EMBL:ABA25060.1}.
FT   DOMAIN          363..612
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   617 AA;  68956 MW;  3477A570B4BD3EB9 CRC64;
     MTSPSTDASS SLVIQENQSF QIDNFQVEVL SYLGQFTSDV YSFKVKICSI DSNSTQSKLG
     LLRVGSDRGG LHREIQLREA LADYKMIAEL ITHITAESVI INPLSPILDI ENQENKQDEI
     KNKTEDTENT TNSENLILHE NVTDGNETKS AIDEDASYLS SLLEVDSEYL EDEYYPQIEI
     CSADSGSKLI LLSDFPENTT TLDTWLKSEY SLEEYLYITS QICQFFRYVC ERNWCFISLE
     PRMIQTGTPS RFFDLTNAYP VGEILTSGLL GNYCASELAY NNNPIHESMS SYTVGALLYH
     SIHKQPLSPH QSIDLKISPI PRIYQILKIC LSSIPEERFP LSQLLTILVE TRQAIRAPKI
     KWNVASRSTV GLSTSRLQNE DNYGVRQQQL SDIETMILGV VADGMGGMSQ GEVASKLSVQ
     TVLDEPIPPE FKTVGQRNEW LMSLFQKAND VVSKNVKNGG TTLSVVLAIA QQLMVAHVGD
     SRIYLLRQGE IRQLSEDHSL VAMLVASGQI TEAESLQHPD RNVLTKSLGS KSKLSDGYVQ
     DLKRTTQELS MTLENADILL LCSDGVWDLV AKNEFVEIFN NNKDLQAAVD TTIEQVIERG
     ASDNATLLAM QYQMEKS
//