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Q9C0Y9 (SPEB3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative agmatinase 3

EC=3.5.3.11
Alternative name(s):
Agmatine ureohydrolase 3
Short name=AUH 3
Gene names
ORF Names:SPAPB24D3.03
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Agmatine + H2O = putrescine + urea.

Cofactor

Manganese By similarity.

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processurea metabolic process

Inferred by curator. Source: GeneDB_Spombe

   Molecular functionagmatinase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 385385Putative agmatinase 3
PRO_0000311760

Sites

Metal binding1751Manganese 1 By similarity
Metal binding1991Manganese 1 By similarity
Metal binding1991Manganese 2 By similarity
Metal binding2011Manganese 2 By similarity
Metal binding2031Manganese 1 By similarity
Metal binding2961Manganese 1 By similarity
Metal binding2961Manganese 2 By similarity
Metal binding2981Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9C0Y9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0326AD45036B859E

FASTA38542,485
        10         20         30         40         50         60 
MGLGFQEKNP VFVKEKQSPF YAVPSNYEEV EFSSIVEPMY SGIATFGRLE NVECLSKRSE 

        70         80         90        100        110        120 
DFDIAFIGMP FDTGTSYRPG ARFGPSSLRE GSRRINTKYG AVNVPLEINP FKSWAKLVDC 

       130        140        150        160        170        180 
GDIPVTTYDI LKAMDQLESA YFQLIARKPS SFTDHDGFAK NDTVLPRVLS LGGDHTIVLP 

       190        200        210        220        230        240 
ILRALHRVYG QPISVIHFDS HLDTWAPGLI GDGDEADGIN HGSYFYFASQ EGIMSKDANI 

       250        260        270        280        290        300 
HAGIRTPISS FSDYDDDVDC GFKIIEAREI DDLGIDGIVK KIRDRVGDNL VYLSIDIDVL 

       310        320        330        340        350        360 
DPAFAPATGT PETGGWSSRE MRAILRGLQG LKFVGADLVE VAPAYDVAEI TSLAGAQLLF 

       370        380 
DIVSMMVKYP LVKEADLSRY MPIHK 

« Hide

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. expand/collapse author list , 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAC36899.1.
RefSeqNP_593990.1. NM_001019416.1.

3D structure databases

HSSPHSSP built from PDB template 1GQ6 based on UniProtKB P37819.
ProteinModelPortalQ9C0Y9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9C0Y9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2543569.
KEGGspo:SPAPB24D3.03.
NMPDRfig|4896.1.peg.3960.

Organism-specific databases

GeneDB_SpombeSPAPB24D3.03.

Phylogenomic databases

eggNOGfuNOG06303.
GeneTreeEFGT00050000003865.
HOGENOMHBG391953.
OMAMRRKYTK.
OrthoDBEOG4936SK.

Gene expression databases

ArrayExpressQ9C0Y9.

Family and domain databases

InterProIPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHERPTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEB3_SCHPO
AccessionPrimary (citable) accession number: Q9C0Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 2001
Last modified: December 14, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families