Q6FM81 (PP4C_CANGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 4 catalytic subunit
Short name=PP4C
EC=3.1.3.16

Gene names

Name:	PPH3
Ordered Locus Names:	CAGL0K10208g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces › Candida glabrata

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Forms the histone H2A phosphatase complex in association with the regulatory subunits PSY2 and PSY4, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint By similarity.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subunit structure	Catalytic subunit of the histone H2A phosphatase complex (HTP-C) containing PPH3, PSY2 and PSY4 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Methylation
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 309	309	Serine/threonine-protein phosphatase 4 catalytic subunit		PRO_0000223650
Sites
	Active site	113	1	Proton donor By similarity
	Metal binding	52	1	Iron By similarity
	Metal binding	54	1	Iron By similarity
	Metal binding	80	1	Iron By similarity
	Metal binding	80	1	Manganese By similarity
	Metal binding	112	1	Manganese By similarity
	Metal binding	162	1	Manganese By similarity
	Metal binding	236	1	Manganese By similarity
Amino acid modifications
	Modified residue	309	1	Leucine methyl ester By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FM81 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 18E0E819D03D0EBD	FASTA	309	35,186
	10 20 30 40 50 60 MLVDLDEILV SLKEGRHIPE ETVYALCMDS QELLMNESNV ARVDTPVTIC GDIHGQLHDL 70 80 90 100 110 120 LTLFEKSGGV EKTRYVFLGD FVDRGFYSLE SFLLLLVYKL RYPDRITLIR GNHETRQITK 130 140 150 160 170 180 VYGFYDEVMR KYGNSNVWRY CCEVFDYLSL GAIINDSIFC VHGGLSPDIT TLNEIRAIDR 190 200 210 220 230 240 KQEVPHEGGM CDLLWSDPDE VDTWSMSPRG AGFLFGKGEV DEFLHVNNVD LIARAHQLVM 250 260 270 280 290 300 EGYKEMFDGG LVTVWSAPNY CYRCGNVAAV LKIEDNLERK YTIFEAVQAQ NGVGNTIIPT KKAQMDYFL

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380957 Genomic DNA. Translation: CAG61626.1.
RefSeq	XP_448663.1. XM_448663.1.
3D structure databases
ProteinModelPortal	Q6FM81.
SMR	Q6FM81. Positions 3-308.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2890113.
KEGG	cgr:CAGL0K10208g.
Phylogenomic databases
HOGENOM	HOG000172696.
KO	K01090.
OMA	NDISMIC.
OrthoDB	EOG4HX88W.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PP4C_CANGA

Accession

Primary (citable) accession number: Q6FM81

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program