ID Q6CCU4_YARLI Unreviewed; 543 AA.
AC Q6CCU4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 24-JAN-2024, entry version 93.
DE RecName: Full=M-phase inducer phosphatase {ECO:0000256|RuleBase:RU368028};
DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU368028};
GN ORFNames=YALI0_C06460g {ECO:0000313|EMBL:CAG81821.2};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG81821.2, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG81821.2, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Functions as a dosage-dependent inducer in mitotic control.
CC Tyrosine protein phosphatase required for progression of the cell
CC cycle. {ECO:0000256|RuleBase:RU368028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001490,
CC ECO:0000256|RuleBase:RU368028};
CC -!- SIMILARITY: Belongs to the MPI phosphatase family.
CC {ECO:0000256|ARBA:ARBA00011065, ECO:0000256|RuleBase:RU368028}.
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DR EMBL; CR382129; CAG81821.2; -; Genomic_DNA.
DR RefSeq; XP_501518.2; XM_501518.2.
DR AlphaFoldDB; Q6CCU4; -.
DR STRING; 284591.Q6CCU4; -.
DR EnsemblFungi; CAG81821; CAG81821; YALI0_C06460g.
DR GeneID; 2909314; -.
DR KEGG; yli:YALI0C06460g; -.
DR VEuPathDB; FungiDB:YALI0_C06460g; -.
DR HOGENOM; CLU_017900_0_0_1; -.
DR InParanoid; Q6CCU4; -.
DR OrthoDB; 12481at2759; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central.
DR CDD; cd01530; Cdc25; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR000751; MPI_Phosphatase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR10828:SF17; CDC25-LIKE PROTEIN PHOSPHATASE TWINE-RELATED; 1.
DR PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU368028};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|RuleBase:RU368028};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368028};
KW Mitosis {ECO:0000256|RuleBase:RU368028};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU368028};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300}.
FT DOMAIN 349..472
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 79..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 60938 MW; FA6BE77876BC45C3 CRC64;
MQSVTSPLSR RHMFDDSPSY KRKLVSPACM AGDLTAAAVH IETPTLPTPR RSLFTAKTPA
FLNLPPPNDS STPCGVPMKK SMSMMEPMSP LSAGSDGSTT FGSSTSSNTS SNTSTSSIQM
HRLRKNNRST SSLRLTSAGV SFDPIDEEGS LRKPFRFSLE LDSPANTRFT HSMNEADSSM
DTDEDGLGSL SQNFRLGGST SHSNTHSLNF NGFTLGGAAD ESAGAVAAAD VTADDINDTP
SARPVRPSLN PLCKRSYNSS STPFAAKFKR PRRTHSMFQD PKELMQEELD EEKEMVRRLS
LSPDVNNNVD SFLVSADCTL ESFSVEGDPF RRIKRETLVQ ILDGHYSHYY DRHVVIDCRF
EYEYDGGHID GAININSKDR LEELLSNEEG ILGNNCNNMM RPGKRGGDSR KRTLLIFHCE
YSAHRGPRMA MHLRNRDRRL NMTNYPHLNF PDVVILQGGY NHFFEQFHTR CYPPQYVEMN
DSMHKSTCER EMGRFRRHMK LRSESSINKQ QGVICSPVGL SRSLSENVDY HRPKRVVSCQ
LWR
//
