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O42887 (SPEB2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative agmatinase 2
EC=3.5.3.11
Alternative name(s):
Agmatine ureohydrolase 2
Short name=AUH 2
Gene names
ORF Names:SPBC8E4.03
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Agmatine + H2O = putrescine + urea.

Cofactor

Manganese Potential.

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: GeneDB_Spombe

   Cellular componentendoplasmic reticulum

Inferred from direct assay. Source: GeneDB_Spombe

fungal-type vacuole

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionagmatinase activity

Non-traceable author statement. Source: GeneDB_Spombe

manganese ion binding

Non-traceable author statement. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 413391Putative agmatinase 2
PRO_0000002092

Sites

Metal binding2061Manganese 1 By similarity
Metal binding2291Manganese 1 By similarity
Metal binding2291Manganese 2 By similarity
Metal binding2311Manganese 2 By similarity
Metal binding2331Manganese 1 By similarity
Metal binding3311Manganese 1 By similarity
Metal binding3311Manganese 2 By similarity
Metal binding3331Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O42887 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 577EF7AF936E1346

FASTA41345,902
        10         20         30         40         50         60 
MFTYQKIIQL ALLLSGVCGA LASIDTDSHL SPKVLEKLRP TENLAYEDDS LDDDTWRSKR 

        70         80         90        100        110        120 
WEFDYQYSGI STFAHLPHVR CLVEQSEDFD IAIIGVPFDT AVSHRPGARF GPKGIRSASS 

       130        140        150        160        170        180 
RQMAIRGFNP SLNVNPYESW AKILDCGDIP VSSYDNQLAV RQMTEGYIDL LSRKATASPA 

       190        200        210        220        230        240 
SNNLKTAGLA KDGIFHPRLI TLGGDHSIGL ASLRALGHFY GNVSVIHFDS HLDTWNPKRY 

       250        260        270        280        290        300 
YPSYWHSDRA DFTHGTMFWM ASKEGLINNG TSIHAGLRTR LSGTDYYDYE EDNRVGFTFI 

       310        320        330        340        350        360 
EAQEIDEIGV NGIVERIKQV VGDTLVYLSI DIDVVDPGLA PGTGTPETGG WTTREMKSIL 

       370        380        390        400        410 
RKLDGHLNLV GAEVVEVSPP YDDRAESTSL AASDFIFEIL SSMVKHPLYD VKK

« 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		CU329671 Genomic DNA. Translation: CAA16996.1.
PIRT39168. T50379.
RefSeqNP_596844.1. NM_001023866.1.

3D structure databases

ProteinModelPortalO42887.
ModBaseSearch...

Protein-protein interaction databases

STRINGO42887.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC8E4.03.1; SPBC8E4.03.1:pep; SPBC8E4.03.
GeneID2541279.
KEGGspo:SPBC8E4.03.
NMPDRfig|4896.1.peg.2710.

Organism-specific databases

GeneDB_SpombeSPBC8E4.03.

Phylogenomic databases

eggNOGfuNOG06303.
GeneTreeEFGT00050000003865.
HOGENOMHBG391953.
OMAIRTEYDH.
OrthoDBEOG4936SK.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-004817-MONOMER.

Gene expression databases

ArrayExpressO42887.

Family and domain databases

InterProIPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KOK01480.
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 nameSPEB2_SCHPO
AccessionPrimary (citable) accession number: O42887
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 1, 1998
Last modified: December 14, 2011
This is version 85 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents