ID Q6CWA9_KLULA Unreviewed; 545 AA.
AC Q6CWA9;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=KLLA0_B05489g {ECO:0000313|EMBL:CAH02173.1};
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAH02173.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAH02173.1, ECO:0000313|Proteomes:UP000000598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC WM37 {ECO:0000313|Proteomes:UP000000598};
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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00001512};
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 Evidence={ECO:0000256|ARBA:ARBA00001482,
CC ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Composed of two components (A and B), the A component is the
CC catalytic subunit and the B component confers calcium sensitivity.
CC {ECO:0000256|ARBA:ARBA00011112}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000256|ARBA:ARBA00009905}.
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DR EMBL; CR382122; CAH02173.1; -; Genomic_DNA.
DR RefSeq; XP_451780.1; XM_451780.1.
DR AlphaFoldDB; Q6CWA9; -.
DR STRING; 284590.Q6CWA9; -.
DR PaxDb; 284590-Q6CWA9; -.
DR GeneID; 2897312; -.
DR KEGG; kla:KLLA0_B05489g; -.
DR eggNOG; KOG0375; Eukaryota.
DR HOGENOM; CLU_004962_6_2_1; -.
DR InParanoid; Q6CWA9; -.
DR OMA; YPAACNF; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:InterPro.
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:0097720; P:calcineurin-mediated signaling; IEA:InterPro.
DR CDD; cd07416; MPP_PP2B; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041751; MPP_PP2B.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000598}.
FT DOMAIN 180..185
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
SQ SEQUENCE 545 AA; 62681 MW; BA7DCEC99368AEC9 CRC64;
MSQEAIENTK KVNAALRVIE SKPSVRDDKD LDLTEYELED GVKRSTVERV VKSVPPVAAR
VPTDEELFKP DGLPNHEFLK KHFLKEGRLS RDQTKRILEM VIDVFAKEPN LLMLNSPLTI
CGDIHGQYYD LMKLFEVGGD PSETPYLFLG DYVDRGSFSF ECLIYLYALK INFPKTFWLL
RGNHECKHLT SYFTFKAECL HKYDLSIFDA CCKSFNYLPL AAVMNNQYFC THGGISPDLV
SVQDVNKINR FREIPSKGLM CDLMWADPIE NYDEDSNSEE RFVPNSLRGC SYAFTYKAVC
DFLKRNGLLS VIRAHEAQDQ GYRMYKNTKS MGFPSLMTLF SAPNYLDTYK NKAAILKYGD
NLMNIRQFNF SPHPYWLPNF MDVFSWSLPF VGEKVTEMLI AILNICAEEE LDEDVPIIDE
AVGKISEVDD GVNEKESPRS NILDEAKRRS LRNKIMAIAK VSRMYSVLRE ESEKVQYLKT
INSGTLPKGA LAHGAEGLTE TLSEFEKARK QDLINERVPP KMEEMESERE KYYRDMLQKI
KGDQI
//
