ID F0Z6W7_DICPU Unreviewed; 1142 AA.
AC F0Z6W7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN ORFNames=DICPUDRAFT_74095 {ECO:0000313|EMBL:EGC40334.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC40334.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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DR EMBL; GL870943; EGC40334.1; -; Genomic_DNA.
DR RefSeq; XP_003283085.1; XM_003283037.1.
DR AlphaFoldDB; F0Z6W7; -.
DR STRING; 5786.F0Z6W7; -.
DR EnsemblProtists; EGC40334; EGC40334; DICPUDRAFT_74095.
DR GeneID; 10503518; -.
DR KEGG; dpp:DICPUDRAFT_74095; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG0698; Eukaryota.
DR InParanoid; F0Z6W7; -.
DR OMA; CHFARIL; -.
DR OrthoDB; 22474at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00364; LRR_BAC; 11.
DR SMART; SM00365; LRR_SD22; 7.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51450; LRR; 6.
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 Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000001064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 885..1140
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 128208 MW; 4388E1CEE4A18EA6 CRC64;
MVHFKRKSEP ILSNLTKNNK NSNSNSNNND NNNNLVTSTS ASSSTLTINN NNNTTMSTND
INNENNSMSR STGIEKPALP PQENKPKRPL SFSVFTLSPP PPTSTSSSNS LHSSTGSGIN
RSGSCTPQKN QSPSSSSLSL SPHPVNGSPK SLLGLSGSTG SPPPLSKSTS THTFKMPPKT
GSMIYSVVYD KTSSNLEVID EELYSKISIQ RLLLGRNKLT EIPERVGELG KLSTIDLSYN
RLSTLPVSLS GLSDLSTLIL TGNKFMIPAT KENLEIQSMK KQFNQHQQDL KPEQEQQPDS
QNCSGVDNEA NNNQEVEIYN SDGLTEEKDK LNSIKEENEI QEPEQPEQPE QSEQSEQPEQ
QEQQEQQEKQ EQQEQIKENK EISSSGIEQP PPISLNHEQL NQGGIPWELC YNSNLKKLEL
GSNQSNDDKW DGSNILPSNL FWFTQIEQLL VPFCQLHSIS SDIQHLESLT HLDISNNNLT
ELPVELGQLC YLSTLIANNN QIKELPQQLT SLSETLTQLD VSDNEIESIP EDFYYLMYLE
KFDVSNNKIK HLPVSLFQGV NENLGLFSLK SFKCRNNQIS ELPSKFFSTC SQLTHLDLSF
NQLTELPNEG LNYLENISTI LLFNNKLKSI PKELFEGSPD SEVHVSGDPN AMDEGNIKEN
LTTFNVSGNQ LTELPVNIWK CKSLSQLSIG YNNFKEIVFP SQLVSYSLEE FYLNGNSSIE
FKVNQPRVGA NNNTVYPDFP SLRELGLGSC NLSEIPEFCK DIKSIEKFDL SNNRIKSLPN
WIGEFEHLLV LYLSRNQLST LPYEEFQNFK NMIILDLAMN PSLVLDQSLY KQLKDTTIIT
SPSLNEQQIA SKLLSTTTTS SNESDTPPSP ILNKHHMIIT KSNRFEMVYS DMIGRRPTME
DSFSIFGKFN DQDDYDLVSL FDGHAGNRAA TYSSEWFPKI MKKLMDIYPS LPPLQWLKQA
YSEISLQFKM YINNERPDLK YCGATAASLL ITRDYYCVSN IGDTRIVLCQ SNGVAKRLSF
DHKPSLPMET KRINNLGGYV VSNAHTSRVN GTLAVSRSIG DIYMEPFVIP DPYLSQTVRD
FELDQYLIVA CDGIWDEISD QQACNIVLNS SSIEEACNKL KDFAYFSGSD DNISVVLIKL
KK
//