Y9461_DICDI
ID Y9461_DICDI Reviewed; 1006 AA.
AC Q54WS9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Probable protein phosphatase DDB_G0279461;
DE EC=3.1.3.16;
GN ORFNames=DDB_G0279461;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: In the C-terminal section; belongs to the PP2C family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000031; EAL67669.2; -; Genomic_DNA.
DR RefSeq; XP_641638.2; XM_636546.2.
DR AlphaFoldDB; Q54WS9; -.
DR STRING; 44689.DDB0304651; -.
DR PaxDb; Q54WS9; -.
DR EnsemblProtists; EAL67669; EAL67669; DDB_G0279461.
DR GeneID; 8622044; -.
DR KEGG; ddi:DDB_G0279461; -.
DR dictyBase; DDB_G0279461; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_298681_0_0_1; -.
DR InParanoid; Q54WS9; -.
DR PRO; PR:Q54WS9; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..1006
FT /note="Probable protein phosphatase DDB_G0279461"
FT /id="PRO_0000369245"
FT DOMAIN 744..1005
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..122
FT /evidence="ECO:0000255"
FT COILED 450..516
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 784
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 784
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 785
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 956
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 996
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1006 AA; 111161 MW; 173B5733030E9B62 CRC64;
MMVPSLSTSI SSPALFKNRE GGEEGNDGGL EQLQNQVNDL GDLNFNEEGD YNNDQQPTNE
EEGTADNELE SLMSLVNDNN NNNNNTSGID DDNNNDIDDN NNNNNNNNNN NNNNNNNKEG
LNDLFISSIN VSTLLNDLDQ LSDTHSHASV SNQSSNGSVR RGYDIKTQRS VGTKGQGGSS
GSSPRSNSLR VYRTFPYRGD HHFSWLNNIR DVDSSEDPNS CHNSNNNNKN NKNNQPSSTH
DQTNINNNNN NNCNDNEKPI KPNSTNGIRH SRKYKGLQQL DFLGSNIILP QQQQPQPIED
NQQVVPQPFQ VDAESNYNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNDNE NNQHPINPVN
TQNTQQNVTH SNNNNNNNNN NTAPPNQWSE LIESLGYGSQ SDEQKTFGST LDDLNNANSC
SDLKDLIVDG ISINNETSPS QSQEITDFSK IDNLNKNINI NNNNNTDSQQ PLPSIDVNFS
HNNNNNNNDN DNNNNNNNNN NNNNNNNNNN NIQDIQIPYH QNDQDYNIQE GNDINNDNYE
IRVSNNDDDN DSSNNNNNNN SKFQENLNLL NTGMGGRICK TDQKKQLSRT ITFADPSSIL
SFFGSIPTDE DQNNNNNKNK NTTTTTTTTN TTTTTTTTTS ASAAAQNKLD LLSSLSAGQS
SGGVGGGNNV LNSSSTPAIK VNHQHKVTEQ NRTSSKISLS TIFPKLPPFT NQQSPPTLSP
SKYYYPLLQP EPTTLIRGFS SAADINKRGL KRAKKPMEME DVYLTQYPLG DDQDSQIALF
AIFDGHSGKG CAVAAKEIFP NILLKYIKST KNENGGKPIY DMRGVFLNAF KEVDAQLSKF
EYEGATATVC LVWRAGHQRF VQSANVGDST AFLSYGNETL FLSKDHRATD PEEIQRIKND
GITLTEGQTR INGLMVSRAL GDHFIKHLNC GLSGEPYVSP PISITPFHSH LIVASDGLWD
VISGNRAMEI VKVQQTEEKM SNSLLQCAIG SIKAKDNISI IVVTLQ
