ID   B0C337_ACAM1            Unreviewed;       842 AA.
AC   B0C337;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Protein phosphatase 2C domain protein {ECO:0000313|EMBL:ABW27384.1};
GN   OrderedLocusNames=AM1_2374 {ECO:0000313|EMBL:ABW27384.1};
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Acaryochloridaceae; Acaryochloris.
OX   NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW27384.1, ECO:0000313|Proteomes:UP000000268};
RN   [1] {ECO:0000313|EMBL:ABW27384.1, 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   -!- 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; CP000828; ABW27384.1; -; Genomic_DNA.
DR   RefSeq; WP_012162854.1; NC_009925.1.
DR   AlphaFoldDB; B0C337; -.
DR   STRING; 329726.AM1_2374; -.
DR   KEGG; amr:AM1_2374; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_017255_0_0_3; -.
DR   OrthoDB; 500607at2; -.
DR   Proteomes; UP000000268; Chromosome.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        575..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          267..521
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          529..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          814..842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..555
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..632
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..791
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   842 AA;  91035 MW;  667A3D75701BA803 CRC64;
     MPHSQPQLQC PNLRCRAVNS DRDQFCQKCG TYLPKRFLWV VGARVDNFQV GDLLEDRFLF
     QGPRVVFDTQ PGIPLKMSVE LPDTLVPYLK LFPYRLHLPQ VYTLLSLGDP EPSLILLLEQ
     APLGSADLDP SHQGGLALGA GMPLFDAWVN AQPLRQLHWL WQIAQLWQPL RIQGVASSLL
     QPDFMRVEGS LFRLLELEND FRLEPSLADL GLVWQQLIPK TSGKLADSLD GLCDQLASGE
     VESAEELLAQ LESWIENIHK AYRVKIDIAT RTDTGMVREH NEDACYPADG AVTQNSLERM
     AIVCDGVGGH AGGEVASGIA IEALRDHLTQ LPIDDLSPAD VITELENASF KANDLISQRN
     DQEQRQDRQR MGTTLVTALS QTHQIYVSHI GDSRAYLITT QGCYQIMVDD DIASREVRLG
     YVPYREALLQ PASGSLVQAL GMASSSVLRP TVQRFLLDED CLFLLCSDGL SDYDRIDMIW
     REELLPLLQG GTDLASTSKR LIELANQLNG HDNVTVGLVH CHVTRQRQST GATGLNSAPA
     ETSAPVDNTP PTVLPKTQAV APDAPLDPKR SGSGFGLWIL LGLILLGVGG AVAYQLGFLK
     LPFLNQPIAD SSASPSPEPS LPDTPPPPPD LAQANKLDVL RLVSANDQPI EISVVKDPKE
     LLQGIGGVDD ASVDNPPTET SDAKIALGST ISIPSDSLVV VDGIFPPPLA DASDKTAPGA
     PIQALRIRTC QPVEEVSEQE GTGILPPEKL DEKLEKEGAD PDADSVAQLI DEKLSDENPS
     GSVTTPSTPQ IGWVDRSKLA SLVTEIIPAA QLSPEQQKAC TPAPLEGKDI PAGAPIGSDP
     TP
//