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UniProtKB/Swiss-Prot entry P30887


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PHO2_YARLI
Primary accession number P30887
Secondary accession number Q6CAE8
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on October 11, 2004 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 51)
Name and origin of the protein
Protein name Acid phosphatase [Precursor]
Synonym EC 3.1.3.2
Gene name
Name: PHO2
OrderedLocusNames: YALI0D03465g
From
Yarrowia lipolytica (Candida lipolytica) [TaxID: 4952] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
DOI=10.1007/BF00352435; PubMed=1423722 [NCBI, ExPASy, EBI, Israel, Japan]
Treton B.Y., le Dall M.-T., Gaillardin C.;
"Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a genomic sequence from the yeast Yarrowia lipolytica identifies a new phosphatase.";
Curr. Genet. 22:345-355(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CLIB 122 / E 150;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X65225; CAA46331.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382130; CAG80552.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S19993; S19993.
RefSeq XP_502364.1; -.
3D structure databases
ModBase P30887.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0003993; Molecular function: acid phosphatase activity (inferred from electronic annotation from EC).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002828; SurE-like_Pase/nucleotidase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.1210.10; SurE-like_Pase/nucleotidase; 1.
Pfam PF01975; SurE; 1.
Pfam graphical view of domain structure.
ProDom PD005378; SurE; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00087; surE; 1.
BLOCKS P30887.
ProtoNet P30887.
Genome annotation databases
GeneID 2910307; -.
KEGG yli:YALI0D03465g; -.
Phylogenomic databases
HOGENOM P30887; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycoprotein; Hydrolase; Magnesium; Metal-binding; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    17  17     Potential. 
CHAIN   18   358  341     Acid phosphatase. PRO_0000033476
ACT_SITE   189   189        Potential. 
METAL   49    49        Magnesium (By similarity). 
METAL   50    50        Magnesium (By similarity). 
METAL   81    81        Magnesium (By similarity). 
METAL   156   156        Magnesium (By similarity). 
CARBOHYD   20    20        N-linked (GlcNAc...) (Potential). 
CARBOHYD   27    27        N-linked (GlcNAc...) (Potential). 
CARBOHYD   32    32        N-linked (GlcNAc...) (Potential). 
CARBOHYD   92    92        N-linked (GlcNAc...) (Potential). 
CARBOHYD   145   145        N-linked (GlcNAc...) (Potential). 
CARBOHYD   199   199        N-linked (GlcNAc...) (Potential). 
CARBOHYD   278   278        N-linked (GlcNAc...) (Potential). 
CONFLICT   228   228        G -> V (in Ref. 1; CAA46331). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 38003 Da [This is the MW of the unprocessed precursor] CRC64: 0362F01F892E693B [This is a checksum on the sequence]
        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 

P30887 in FASTA format

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View entry in raw text format (no links)
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