O14094 (PPX1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative exopolyphosphatase
Short name=ExopolyPase
EC=3.6.1.11

Alternative name(s):
Metaphosphatase

Gene names

ORF Names:

SPAC2F3.11

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Degradation of inorganic polyphosphates By similarity.
Catalytic activity	(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.
Cofactor	Binds 2 manganese ions per subunit Potential.
Sequence similarities	Belongs to the PPase class C family.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	polyphosphate catabolic process Inferred from sequence orthology. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase mitochondrial matrix Inferred from sequence orthology. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase plasma membrane Inferred from sequence orthology. Source: PomBase
Molecular_function	exopolyphosphatase activity Inferred from sequence orthology. Source: PomBase manganese ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 384	384	Putative exopolyphosphatase		PRO_0000158600
Sites
	Metal binding	40	1	Manganese 1 By similarity
	Metal binding	42	1	Manganese 2 By similarity
	Metal binding	116	1	Manganese 1 By similarity
	Metal binding	116	1	Manganese 2 By similarity
	Metal binding	138	1	Manganese 2 By similarity
	Metal binding	200	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	O14094 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 643CC43C7AF185EA	FASTA	384	43,297
	10 20 30 40 50 60 MKLGRFLENG REQIRNLLLN ASTVSSAPSF SFVSGNESAD LDSCASSIVY AYCLQRKQLG 70 80 90 100 110 120 RIVVPFFNIP RKELRLRPEL SYLLNLASIS SDDIVFLDDI VKLPKRIFSN PIYLVDHNSL 130 140 150 160 170 180 DRKDLENFNG SIAGIIDHHK DEGGSLHADP RIIEECGSCC TLVCRYFMPV IRSLYDSKVS 190 200 210 220 230 240 ELHQTATNLA VLALGPILID TGNLKNEKTT DTDVKIVNDL CSFVPKDWVR DEFFDTLKEK 250 260 270 280 290 300 KKSCKGFSFD DLLRRDLKQY FPDGIVVNYA SVGKGLDWIK KKRLGWEDEL KSFAEVQNSD 310 320 330 340 350 360 LVIVGLSLSK NDEFGRQLIL YKRTERGAGL ADSFLKLSKQ NLGLEIIEEK DNGDLSMWNQ 370 380 RNSAASRKKV VPLLMDSVKQ VASK

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB16267.1.
PIR	T38544.
RefSeq	NP_594390.1. NM_001019812.2.
3D structure databases
ProteinModelPortal	O14094.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC2F3.11-1.
Proteomic databases
PaxDb	O14094.
PRIDE	O14094.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC2F3.11.1; SPAC2F3.11.1:pep; SPAC2F3.11.
GeneID	2541853.
KEGG	spo:SPAC2F3.11.
Organism-specific databases
PomBase	SPAC2F3.11.
Phylogenomic databases
eggNOG	COG1227.
KO	K01514.
OMA	WIVRKAG.
OrthoDB	EOG4KSSV6.
Family and domain databases
InterPro	IPR004097. DHHA2. IPR001667. Pesterase_RecJ. [Graphical view]
Pfam	PF01368. DHH. 1 hit. PF02833. DHHA2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802941.

Entry information

Entry name

PPX1_SCHPO

Accession

Primary (citable) accession number: O14094

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program