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Q9C0Y9 (SPEB3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. 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) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Agmatine + H2O = putrescine + urea.

Cofactor

Manganese By similarity.

Sequence similarities

Belongs to the arginase family.

Ontologies

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

Inferred by curator. Source: PomBase

   Molecular_functionagmatinase activity

Inferred from electronic annotation. Source: UniProtKB-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

Signal peptide1 – 2121 Potential
Chain22 – 408387Putative agmatinase 3
PRO_0000311760

Sites

Metal binding1981Manganese 1 By similarity
Metal binding2221Manganese 1 By similarity
Metal binding2221Manganese 2 By similarity
Metal binding2241Manganese 2 By similarity
Metal binding2261Manganese 1 By similarity
Metal binding3191Manganese 1 By similarity
Metal binding3191Manganese 2 By similarity
Metal binding3211Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9C0Y9 [UniParc].

Last modified June 13, 2012. Version 2.
Checksum: 3BB0F4614304C536

FASTA40845,085
        10         20         30         40         50         60 
MKSVEWFTWG VFLLLSGFGE AGRMGLGFQE KNPVFVKEKQ SPFYAVPSNY EEVEFSSIVE 

        70         80         90        100        110        120 
PMYSGIATFG RLENVECLSK RSEDFDIAFI GMPFDTGTSY RPGARFGPSS LREGSRRINT 

       130        140        150        160        170        180 
KYGAVNVPLE INPFKSWAKL VDCGDIPVTT YDILKAMDQL ESAYFQLIAR KPSSFTDHDG 

       190        200        210        220        230        240 
FAKNDTVLPR VLSLGGDHTI VLPILRALHR VYGQPISVIH FDSHLDTWAP GLIGDGDEAD 

       250        260        270        280        290        300 
GINHGSYFYF ASQEGIMSKD ANIHAGIRTP ISSFSDYDDD VDCGFKIIEA REIDDLGIDG 

       310        320        330        340        350        360 
IVKKIRDRVG DNLVYLSIDI DVLDPAFAPA TGTPETGGWS SREMRAILRG LQGLKFVGAD 

       370        380        390        400 
LVEVAPAYDV AEITSLAGAQ LLFDIVSMMV KYPLVKEADL SRYMPIHK 

« Hide

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Comparative functional genomics of the fission yeasts."
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. expand/collapse author list , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAC36899.2.
RefSeqNP_593990.2. NM_001019416.2.

3D structure databases

ProteinModelPortalQ9C0Y9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279984. 6 interactions.
STRING4896.SPAPB24D3.03-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAPB24D3.03.1; SPAPB24D3.03.1:pep; SPAPB24D3.03.
GeneID2543569.
KEGGspo:SPAPB24D3.03.

Organism-specific databases

PomBaseSPAPB24D3.03.

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204320.
OrthoDBEOG718KPD.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 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...

Other

NextBio20804576.

Entry information

Entry nameSPEB3_SCHPO
AccessionPrimary (citable) accession number: Q9C0Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 13, 2012
Last modified: February 19, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names