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
//