PP4C_KLULA
ID PP4C_KLULA Reviewed; 308 AA.
AC Q6CNT6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE Short=PP4C;
DE EC=3.1.3.16;
GN Name=PPH3; OrderedLocusNames=KLLA0E10032g;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
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.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Forms the histone H2A phosphatase complex in association with
CC the regulatory subunits PSY2 and PSY4, which dephosphorylates H2AS128ph
CC (gamma-H2A) that has been displaced from sites of DNA lesions in the
CC double-stranded DNA break repair process. Dephosphorylation is
CC necessary for efficient recovery from the DNA damage checkpoint (By
CC similarity). {ECO:0000250}.
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Catalytic subunit of the histone H2A phosphatase complex (HTP-
CC C) containing PPH3, PSY2 and PSY4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382125; CAG99490.1; -; Genomic_DNA.
DR RefSeq; XP_454403.1; XM_454403.1.
DR AlphaFoldDB; Q6CNT6; -.
DR SMR; Q6CNT6; -.
DR STRING; 28985.XP_454403.1; -.
DR EnsemblFungi; CAG99490; CAG99490; KLLA0_E10055g.
DR GeneID; 2893827; -.
DR KEGG; kla:KLLA0_E10055g; -.
DR eggNOG; KOG0372; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q6CNT6; -.
DR OMA; FKCFGPS; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IEA:EnsemblFungi.
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:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IEA:EnsemblFungi.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IEA:EnsemblFungi.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:EnsemblFungi.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Methylation; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..308
FT /note="Serine/threonine-protein phosphatase 4 catalytic
FT subunit"
FT /id="PRO_0000223651"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 308
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250"
SQ SEQUENCE 308 AA; 35167 MW; 5BF6D3BFDAB84CD8 CRC64;
MMKLDEIIET LRQGKHVDED SIYSLCVMAQ ELLMNESNVT HVDTPVTICG DIHGQLHDLL
TLFAKSGGIE KNRYIFLGDF VDRGFYSLES FLLLVCYKLR YPDRIVLIRG NHETRQITKV
YGFYDEVVRK YGNSNVWRYC CEVFDYLPLG AIVNNKVFCV HGGLSPDVLS INEIRTIDRK
KEVPHEGAMC DLLWSDPEDV DTWSLSPRGA GFLFGQNEVD KFLHTNSVEL IARAHQLVME
GYKEMFDGGL VTVWSAPNYC YRCGNVAAVL RIDDDMTKDY TIFEAVQARD SGGNVILPTK
KPQMDYFL
