Q10066 (ARGI2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginase
EC=3.5.3.1

Gene names

Name:	aru1
ORF Names:	SPAC3H1.07

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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.
Subunit structure	Homotrimer By similarity.
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Biological process	Arginine metabolism Urea cycle
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine catabolic process to ornithine Inferred from mutant phenotype. Source: GeneDB_Spombe urea cycle Inferred by curator. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	arginase activity Inferred from mutant phenotype. Source: GeneDB_Spombe metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 323	323	Arginase		PRO_0000173710
Regions
	Region	144 – 148	5	Substrate binding By similarity
	Region	155 – 157	3	Substrate binding By similarity
Sites
	Metal binding	119	1	Manganese 1 By similarity
	Metal binding	142	1	Manganese 1 By similarity
	Metal binding	142	1	Manganese 2 By similarity
	Metal binding	144	1	Manganese 2 By similarity
	Metal binding	146	1	Manganese 1 By similarity
	Metal binding	247	1	Manganese 1 By similarity
	Metal binding	247	1	Manganese 2 By similarity
	Metal binding	249	1	Manganese 2 By similarity
	Binding site	198	1	Substrate By similarity
	Binding site	292	1	Substrate By similarity
Experimental info
	Sequence conflict	278	1	A → R in AAA65456. Ref.1
	Sequence conflict	293 – 294	2	Missing in AAA65456. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10066 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 1E10876E0E969D66	FASTA	323	35,704
	10 20 30 40 50 60 MSPHKISDNH RHLMLSRFMM GNGVSIINMP FSGGQPKDGA ELAPEMVEKA GLVDDLEHLG 70 80 90 100 110 120 YDVKLIQNPE FKSRPSKEGP NQALMKNPLY VSNVTRQVRD AVQRELEQQR VVVNIGGDHS 130 140 150 160 170 180 LAIGTVEGVQ AVYDDACVLW IDAHADINTP ESSPSKNLHG CPLSFSLGYA EPLPEEFAWT 190 200 210 220 230 240 KRVIEERRLA FIGLRDLDPM ERAFLRERNI AAYTMHHVDK YGIGRVVEMA MEHINPGKRR 250 260 270 280 290 300 PVHLSFDVDA CDPIVAPATG TRVPGGLTFR EAMYICEAVA ESGTLVAVDV MEVNPLLGNE 310 320 EEAKTTVDLA RSIVRTSLGQ TLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Ocampos M. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"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. , 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	U24279 Genomic DNA. Translation: AAA65456.1. CU329670 Genomic DNA. Translation: CAA92260.1.
PIR	T38739. T52537.
RefSeq	NP_593549.1. NM_001018982.1.
3D structure databases
ProteinModelPortal	Q10066.
ModBase	Search...
Protein-protein interaction databases
STRING	Q10066.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC3H1.07.1; SPAC3H1.07.1:pep; SPAC3H1.07.
GeneID	2543377.
GenomeReviews	Gene locus aru1 in contig CU329670_GR.
KEGG	spo:SPAC3H1.07.
NMPDR	fig|4896.1.peg.3519.
Organism-specific databases
GeneDB_Spombe	SPAC3H1.07.
Phylogenomic databases
eggNOG	fuNOG04820.
GeneTree	EFGT00050000003865.
HOGENOM	HBG391953.
OMA	KYGIGKV.
OrthoDB	EOG432471.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001226-MONOMER.
Gene expression databases
ArrayExpress	Q10066.
Family and domain databases
InterPro	IPR014033. Arginase_subgr. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. IPR020855. Ureohydrolase_Mn_BS. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KO	K01476.
PANTHER	PTHR11358:SF2. Arginase_sub. 1 hit. PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PIRSF	PIRSF036979. Arginase. 1 hit.
PRINTS	PR00116. ARGINASE.
TIGRFAMs	TIGR01229. RocF_arginase. 1 hit.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGI2_SCHPO

Accession

Primary (citable) accession number: Q10066

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	December 14, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program