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Database: UniProt
Entry: A0A1R2CFU2_9CILI
LinkDB: A0A1R2CFU2_9CILI
Original site: A0A1R2CFU2_9CILI 
ID   A0A1R2CFU2_9CILI        Unreviewed;       442 AA.
AC   A0A1R2CFU2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN   ORFNames=SteCoe_10367 {ECO:0000313|EMBL:OMJ87806.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ87806.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ87806.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ87806.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Enzyme with a broad specificity.
CC       {ECO:0000256|ARBA:ARBA00003302}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC       {ECO:0000256|RuleBase:RU003465}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMJ87806.1}.
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DR   EMBL; MPUH01000167; OMJ87806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2CFU2; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; 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; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR47992:SF119; PROTEIN PHOSPHATASE 2C 33-RELATED; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187209}.
FT   DOMAIN          149..440
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   442 AA;  50266 MW;  29AA43149E57C203 CRC64;
     MKRINLTQKF LAKDKSSKKL IVCKSISTET FPKSVKSPSI LRYPSLSPNP NLIKQSASPY
     LENSLRKNIS LMVFNKKIKK EIRVLPSIPK PHPIKKVKKM QRNKHRNSSL FSEKLNQTLM
     NPILNISQAS VELTAIKDSK KLSLSFDYRT QIGISQGKTK KENQDSVFYK ENFMQDNSHF
     FGVCDGHGVN GYEVVTLVRS SLIANIEKTY LEQSQSESQE TSIFTSFKTA FEMTEKLLFM
     SNIEVGFSGC TSVNTIIINN TIYCANLGDS RAIIGNYNGK KCVPVVLTKD HNPRNETESL
     RILQSGGIID NIRGKTYIDE EGNAYGPLRI WVKKNEYPGL AMTRCFGDSV SKIIGAISEP
     GSFYLEVTKY EMSINDRFMV IATDGIWEYL SNQKVVRVVN KEWEEGSVRT ACNKLMELAI
     QKWKKQGEYM DDISFFVIFF KD
//
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