ID   Q113X1_TRIEI            Unreviewed;       645 AA.
AC   Q113X1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Protein serine/threonine phosphatase {ECO:0000313|EMBL:ABG51203.1};
GN   OrderedLocusNames=Tery_1950 {ECO:0000313|EMBL:ABG51203.1};
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG51203.1};
RN   [1] {ECO:0000313|EMBL:ABG51203.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101 {ECO:0000313|EMBL:ABG51203.1};
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., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; CP000393; ABG51203.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q113X1; -.
DR   STRING; 203124.Tery_1950; -.
DR   KEGG; ter:Tery_1950; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_017255_0_0_3; -.
DR   OrthoDB; 495860at2; -.
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; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 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   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        586..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          255..529
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          619..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          309..356
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   645 AA;  73442 MW;  2F32046B43D17179 CRC64;
     MINSAPIIHC PNINCSSVSH SWDQEECEAC QTKLIYRYLW AVAPKVEISV GELLGDRYYV
     VAPQVWLDTK PGEPPFMHEE FPDYIMPYLR LYPERLHTPD VYGFYQYGEE TYPTDILLLD
     NVPLDSKGNL LPSLVEAWPT ASPVRQVYWL WQMMQLWKPL SEERVAFSLL TNNLRVEDWR
     LRLLELNLET RKTKLRDFKI FWSNLLPTAH PNVQQPLTEI CHMISDIGES LEAIAPKLNQ
     LLLEQAAKLP LKSDIMGATD TGPVRMHNED CCYPTEEDLN SNQLVPNLAI ICDGVGGHDG
     GEVASQLAVQ SIKKLVQNLL IEVEQQEELT SPNLVNKQLE EIIRVVNNMI ATENDEQGRE
     SRQRMGTTLA MALQLPQQVK PSPESSPNNA HELYIVHVGD SRAYWLSRNT CQLLTVDDNV
     ASREVGLGHC LYWQGLKRRD GGALTQALGT RDGEFIYPTI QRFLIEQEGI LLLCSDGLSD
     NNWVENSWAE YASKVFQGEI SLKQGVESLI ELANHKNGHD NTSVVLVHYR LSPEKLILSN
     IPTVTTPEKE ILMTELSEAS KELLYNNDEE VSEAESEFQL EPVQNFFWLK PWMCMMGVLF
     ILLVGAIISV WRNWENFQST PRDSPAPWES PMRPEPSETR ISPSS
//