ID A0A0D6ARP2_9CHRO Unreviewed; 587 AA.
AC A0A0D6ARP2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=GM3709_1849 {ECO:0000313|EMBL:BAQ65084.1};
OS Geminocystis sp. NIES-3709.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Geminocystis.
OX NCBI_TaxID=1617448 {ECO:0000313|EMBL:BAQ65084.1, ECO:0000313|Proteomes:UP000064126};
RN [1] {ECO:0000313|EMBL:BAQ65084.1, ECO:0000313|Proteomes:UP000064126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3709 {ECO:0000313|EMBL:BAQ65084.1,
RC ECO:0000313|Proteomes:UP000064126};
RA Hirose Y.;
RT "Geminocystis sp. NIES-3709 complete genome sequence.";
RL Submitted (MAR-2015) 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; AP014821; BAQ65084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6ARP2; -.
DR STRING; 1617448.GM3709_1849; -.
DR KEGG; gen:GM3709_1849; -.
DR PATRIC; fig|1617448.3.peg.1877; -.
DR Proteomes; UP000064126; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 542..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 224..488
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 587 AA; 67256 MW; E74E9DB76CE3EA3F CRC64;
MRIEGNLEKE YPLGVLISDR FFVCSQNIVI DTKPDLSPIF PENVPEEVVP YLKLFSHRLH
VPQIYGFVDD NFDKWLLEYE SIPLNEKGYL IHPDLFPSIG LSLFKASSLR QVNWLWQLVL
LWTPLAKQNV LSSLLEPKNI RVSGGIIKLI ELIPDKDSTP TLKDLGDLWV NWITRLNPLI
QDVMGKIILS LQENLFDNPS SVLDILDQIL YILGNNYYQR KFKLITVTDP GKRRKNNEDS
CYPPTDHLKE INSGIDTLTM VCDGLGGQEK GEIASHLAIE IMQKELEQDY KKTLKETLNN
KHWTPLIDSK KILKAVSKAN DTIARINNKE KRKDRERMGT TVVTTMAIAH EVYFAYVGDS
RIYWITGDSC HQVTVDDDLA TREVRLGYGF YRQLISNPQT GALLQALGME SSRRLKVHIR
RFVLDEDSVF LLCSDGLSDF ERVEQYWKSE VLPIISEGVN VEEAAQQILK IGLQKNGHDN
ITIGLLQCQI EEKNPEDYEG KLTWAYLQEI IPELPQPQGN LKLDKISKKK TSNSINFPFS
KSTLIVIISL IVVIIGLIFW YHNKSSQNKS INRDMIYSNL EIKNQVV
//
