Acid phosphatase precursor - Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast)

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P30887 (PHO2_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acid phosphatase
EC=3.1.3.2

Gene names

Name:	PHO2
Ordered Locus Names:	YALI0D03465g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia ›

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Probably serves to scavenge phosphorus for growing cells.
Catalytic activity	A phosphate monoester + H₂O = an alcohol + phosphate.
Cofactor	Magnesium By similarity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the SurE nucleotidase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acid phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding 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

Signal peptide

17

Potential

Chain

341

Acid phosphatase

PRO_0000033476

Sites

Active site

1

Potential

Metal binding

1

Magnesium By similarity

Metal binding

1

Magnesium By similarity

Metal binding

1

Magnesium By similarity

Metal binding

1

Magnesium By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

1

G → V in CAA46331. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P30887 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 0362F01F892E693B
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358

38,003

        10         20         30         40         50         60 
MKFSTIALPL LASAALAQTN SSHSGTNATS HNSTVPNENS KTTIVVTNDD SWASANIRAF 

        70         80         90        100        110        120 
YDELKKEGYN VFMFAPALQQ SGTGGTFVLP KNTTLAKGAE WGSAPVGAPA WGQDEKDDHI 

       130        140        150        160        170        180 
WYFDGTPGAA VTFGFDYALP KFHNNITVDL VVSGPNEGWN LGPFVYTLSG TEGAMYTSVL 

       190        200        210        220        230        240 
RGVPAIAFSG ENKHTYYANA SNSETASHNI YAKASTAIVK NLLKNAKGRP SVLPYGVGLS 

       250        260        270        280        290        300 
VNLPLVGDID PTGKCTDPKP IFTRQTGRGA ITDKLVFNET TGLFKYGDIK SDATKACLNG 

       310        320        330        340        350 
DCFLPDETDV INNWGCYSSI SVVSTDYDAP GALAAEAQFL NRGLVEFAPT GYGSFPGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a genomic sequence from the yeast Yarrowia lipolytica identifies a new phosphatase." Treton B.Y., le Dall M.-T., Gaillardin C. Curr. Genet. 22:345-355(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 20460 / W29 / CBS 7504 / IFP29.
[2]	"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. Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X65225 Genomic DNA. Translation: CAA46331.1. CR382130 Genomic DNA. Translation: CAG80552.1.
PIR	S19993.
RefSeq	XP_502364.1. XM_502364.1.
3D structure databases
ProteinModelPortal	P30887.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2910307.
KEGG	yli:YALI0D03465g.
Phylogenomic databases
eggNOG	COG0496.
HOGENOM	HOG000248507.
OrthoDB	EOG4VDT7J.
Family and domain databases
Gene3D	3.40.1210.10. 1 hit.
InterPro	IPR002828. SurE-like_Pase/nucleotidase. [Graphical view]
Pfam	PF01975. SurE. 1 hit. [Graphical view]
SUPFAM	SSF64167. SurE-like_Pase/nucleotidase. 1 hit.
TIGRFAMs	TIGR00087. surE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PHO2_YARLI

Accession

Primary (citable) accession number: P30887
Secondary accession number(s): Q6CAE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents