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Database: UniProt
Entry: C4XWF9_CLAL4
LinkDB: C4XWF9_CLAL4
Original site: C4XWF9_CLAL4 
ID   C4XWF9_CLAL4            Unreviewed;       469 AA.
AC   C4XWF9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN   ORFNames=CLUG_00282 {ECO:0000313|EMBL:EEQ36159.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ36159.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ36159.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ36159.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC       {ECO:0000256|RuleBase:RU003465}.
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DR   EMBL; CH408076; EEQ36159.1; -; Genomic_DNA.
DR   RefSeq; XP_002619123.1; XM_002619077.1.
DR   AlphaFoldDB; C4XWF9; -.
DR   STRING; 306902.C4XWF9; -.
DR   GeneID; 8499804; -.
DR   KEGG; clu:CLUG_00282; -.
DR   VEuPathDB; FungiDB:CLUG_00282; -.
DR   HOGENOM; CLU_013173_4_2_1; -.
DR   InParanoid; C4XWF9; -.
DR   OMA; CLLHDRP; -.
DR   OrthoDB; 11028at2759; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
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; PTHR13832:SF565; AT28366P-RELATED; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 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   Manganese {ECO:0000256|ARBA:ARBA00023211};
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:UP000007703}.
FT   DOMAIN          23..289
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          359..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..456
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  51559 MW;  4C0FFC631CB0D77F CRC64;
     MGQILSQPET EKHSEKDANK YLAYGLSCMQ GWRINMEDAH ATILSMNEDG DDQVAFFGVY
     DGHGGEKAAI FTGLHLHELI QQTEAFGRKD YSTALKDGFL SCDQAILQNQ ETRNDESGCA
     ATSAIITPKQ VICANAGDSR TVLSTNGFAK ALSFDHKPYN EGEKARICAA GGYVEMGRVN
     GNLALSRGIG DFVFKKNSDL PAEEQIVTCY PEVISHDLDY EKDEFVILAC DGIWDCLSSQ
     SCVECVRRGI YERKPFTQIC EEIMELCCAP NADGPGIGCD NMSILIVALL DQSKNETLDQ
     WYDRVISKIE LNKKQMEEHK TDDDEEEAPV AVEYGPISPP YNDLYKELFG DFAEIGQHSN
     TDARSSGSNG YSMFGNMGMR STSREDDNEE EASNGEDDSL RNGAISLQKL LSSNVITNEN
     GVIYLDTSSA QSLLASFGMP TESAEEDEEG EDVHESHIEE VEDGPSESS
//
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