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Q74ZW4 (ARGI_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 61. 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:
Arginase

EC=3.5.3.1
Gene names
Name:CAR1
Ordered Locus Names:AGR225C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-arginine + H2O = L-ornithine + urea.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Pathway

Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
Urea cycle
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

urea cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarginase 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 – 399399Arginase
PRO_0000173706

Regions

Region218 – 2225Substrate binding By similarity
Region229 – 2313Substrate binding By similarity

Sites

Metal binding1931Manganese 1 By similarity
Metal binding2161Manganese 1 By similarity
Metal binding2161Manganese 2 By similarity
Metal binding2181Manganese 2 By similarity
Metal binding2201Manganese 1 By similarity
Metal binding3221Manganese 1 By similarity
Metal binding3221Manganese 2 By similarity
Metal binding3241Manganese 2 By similarity
Binding site2731Substrate By similarity
Binding site3671Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q74ZW4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 8DDCF23F497F51EB

FASTA39942,555
        10         20         30         40         50         60 
MAQRNCWRRS WLGVGGGLCL GAHGAARGPR QLFHLTAKQS SAASDAKCRR WRAAGRGGGA 

        70         80         90        100        110        120 
GGVYNGRGAA AGSRQTSGMA HNEHPHYKFF ESKKASLVMA PFSGGQGKSG VEDGPKYLLK 

       130        140        150        160        170        180 
QGLREGVEGL GWEIEVQRPL DGHDFEERKQ RATEVVGRAK NPTLVGEATH LIHDAVRAAA 

       190        200        210        220        230        240 
HAGRLPVTLG GDHSIAIGTV SGVLDRYPDA GLLWVDAHAD INTLASTESG NLHGCPVSFL 

       250        260        270        280        290        300 
MGLERESWPA PLAWVPGTLR PSKIAYIGLR DVDPEEKEIL RRLGITAFSM YHVDRYGINK 

       310        320        330        340        350        360 
VVEMALAAIN PDGTGPVMVS YDVDAIDPMY VPATGTPVRG GLTLREGLFI VERVAETGNL 

       370        380        390 
VALDVVECNP ELAAHDLHVV DTVQTGCSIA RCALGETLL 

« Hide

References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016820 Genomic DNA. Translation: AAS54715.1.
RefSeqNP_986891.1. NM_211953.1.

3D structure databases

ProteinModelPortalQ74ZW4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ74ZW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4623193.
GenomeReviewsGene locus AGR225C in contig AE016820_GR.
KEGGago:AGOS_AGR225C.
NMPDRfig|33169.1.peg.4536.

Organism-specific databases

AGDAGR225C.

Phylogenomic databases

eggNOGfuNOG04820.
HOGENOMHBG391953.
OMADRHGIGK.
OrthoDBEOG432471.
PhylomeDBQ74ZW4.

Family and domain databases

InterProIPR014033. Arginase_subgr.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KOK01476.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. RocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGI_ASHGO
AccessionPrimary (citable) accession number: Q74ZW4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: December 14, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families