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UniProtKB/Swiss-Prot entry Q9P6I7


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

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Entry information
Entry name ADA_SCHPO
Primary accession number Q9P6I7
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 35)
Name and origin of the protein
Protein name Adenosine deaminase
Synonyms EC 3.5.4.4
Adenosine aminohydrolase
Gene name
Name: dea2
Synonyms: aah1
ORFNames: SPBC1198.02
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-150.
DOI=10.1016/j.jmb.2003.10.005; PubMed=14643670 [NCBI, ExPASy, EBI, Israel, Japan]
Ribard C., Rochet M., Labedan B., Daignan-Fornier B., Alzari P., Scazzocchio C., Oestreicher N.;
"Sub-families of alpha/beta barrel enzymes: a new adenine deaminase family.";
J. Mol. Biol. 334:1117-1131(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
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
CU329671; CAB91177.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_595071.1; -.
3D structure databases
ModBase Q9P6I7.
Organism-specific databases
GeneDB_Spombe SPBC1198.02; -.
Gene expression databases
ArrayExpress Q9P6I7; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0000034; Molecular function: adenine deaminase activity (traceable author statement from GeneDB_SPombe).
GO:0004000; Molecular function: adenosine deaminase activity (inferred from electronic annotation from InterPro).
GO:0009168; Biological process: purine ribonucleoside monophosphate biosynthetic process (inferred from electronic annotation from InterPro).
GO:0043101; Biological process: purine salvage (traceable author statement from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR006650; A/AMP_deam_AS.
IPR001365; A/AMP_deaminase.
IPR006330; A_deaminase.
Graphical view of domain structure.
PANTHER PTHR11409; A/AMP_deaminase; 1.
Pfam PF00962; A_deaminase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01430; aden_deam; 1.
PROSITE PS00485; A_DEAMINASE; FALSE_NEG.
ProtoNet Q9P6I7.
Genome annotation databases
GeneID 2540066; -.
KEGG spo:SPBC1198.02; -.
NMPDR fig|4896.1.peg.937; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Hydrolase; Nucleotide metabolism; Nucleus.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   367  367     Adenosine deaminase. PRO_0000256237
ACT_SITE   209   209        Potential. 
ACT_SITE   257   257        Potential. 
ACT_SITE   290   290        Potential. 
ACT_SITE   291   291        Potential. 
MUTAGEN   150   150        R->H: In allele dea2-1. 
Sequence information
Length: 367 AA [This is the length of the unprocessed precursor] Molecular weight: 41199 Da [This is the MW of the unprocessed precursor] CRC64: 4470A2EF23405B85 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSNLPIYNFI RKLPKCEHHV HLEGCLSPDL VFRLAKKNGI TLPSDDAAYT TPSTLLASYE 

        70         80         90        100        110        120 
HFGCLDDFLR YYYIAVSVLI EASDFEALAY EYFSIAHSQG VHHAEVFFDP QTHTSRGISY 

       130        140        150        160        170        180 
DVVVSGFSAA CERANRDFGM STNLIMCFLR HLPSEAAHET FAEALKRNDF ENGIVAGVGL 

       190        200        210        220        230        240 
DSSEVDFPPE LFQEVYKLAA EKGIRRTGHA GEEGDPSYIR SGLDNLSLQR IDHGIRLVED 

       250        260        270        280        290        300 
KELMKRVAEE NIMLTMCPLS NLKLRCVNSI AELPVREFLE AGVPFSINCD DPAYFGGYTL 

       310        320        330        340        350        360 
ENYFAIQKHF NLTVKEWVFI ANAAINGSWI SGKRKEELLS SVQKCVKEYT AEIQQPKTLE 


TAVEVQA 

Q9P6I7 in FASTA format

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