NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10547040 [NCBI, ExPASy, EBI, Israel, Japan]
Borsuk P., Dzikowska A., Empel J., Grzelak A., Grzeskowiak R., Weglenski P.;
"Structure of the arginase coding gene and its transcript in Aspergillus nidulans.";
Acta Biochim. Pol. 46:391-403(1999).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC 4;
DOI=10.1038/nature04341; PubMed=16372000 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).

Comments

CATALYTIC ACTIVITY: L-arginine + H₂O = L-ornithine + urea.
COFACTOR: Manganese (By similarity).
PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1 .
SUBUNIT: Homotrimer (By similarity).
SIMILARITY: Belongs to the arginase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U62482; AAB05775.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACD01000051; EAA63472.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_660505.1; -.

3D structure databases

HSSP

P07824; 1D3V. [HSSP ENTRY / PDB]

ModBase

Q12611.

Ontologies

GO:0004053;	Molecular function: arginase activity (inferred from electronic annotation from InterPro).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006525;	Biological process: arginine metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005924; Arginase.
IPR014033; Arginase_sub.
IPR006035; Ureohydrolase.
Graphical view of domain structure.

PANTHER

PTHR11358:SF2; Arginase_sub; 1.
PTHR11358; Ureohydrolase; 1.

PRINTS

PR00116; ARGINASE.

TIGRFAMs

TIGR01229; rocF_arginase; 1.

PROSITE

PS00147; ARGINASE_1; 1.
PS00148; ARGINASE_2; 1.
PS01053; ARGINASE_3; 1.

ProtoNet

Q12611.

Genome annotation databases

GeneID

2873985; -.

KEGG

ani:AN2901.2; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Arginine metabolism; Hydrolase; Manganese; Metal-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 324`	`324`	`Arginase.`	`PRO_0000173708`
`METAL`	`115 115`		`Manganese 1 (By similarity).`
`METAL`	`143 143`		`Manganese 1 (By similarity).`
`METAL`	`143 143`		`Manganese 2 (By similarity).`
`METAL`	`145 145`		`Manganese 2 (By similarity).`
`METAL`	`147 147`		`Manganese 1 (By similarity).`
`METAL`	`249 249`		`Manganese 1 (By similarity).`
`METAL`	`249 249`		`Manganese 2 (By similarity).`
`METAL`	`251 251`		`Manganese 2 (By similarity).`
`CONFLICT`	`35 35`		`E -> V (in Ref. 1; AAB05775).`
`CONFLICT`	`71 71`		`I -> V (in Ref. 1; AAB05775).`
`CONFLICT`	`86 86`		`A -> G (in Ref. 1; AAB05775).`
`CONFLICT`	`95 95`		`S -> R (in Ref. 1; AAB05775).`
`CONFLICT`	`132 132`		`Missing (in Ref. 1; AAB05775).`
`CONFLICT`	`258 258`		`A -> V (in Ref. 1; AAB05775).`
`CONFLICT`	`272 272`		`R -> C (in Ref. 1; AAB05775).`
`CONFLICT`	`300 300`		`E -> V (in Ref. 1; AAB05775).`

Sequence information

Length: 324 AA [This is the length of the unprocessed precursor]

Molecular weight: 35479 Da [This is the MW of the unprocessed precursor]

CRC64: 5767BEB9D7987A16 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSPSTIKQR FLSKPNQLGV VAVGFNGGQC KLGVEAAPMA LVEAGLLDQL RDDLDYEIHY 

        70         80         90        100        110        120 
DNTVHYYEKE IPAEDPDHRG MKKPRAVSAV TETLSSQVYE HSKEGKFTLT LGGDHSIAIG 

       130        140        150        160        170        180 
SISGIAKATR ERLGREIGVI WVDAHADINI PEMSPSGNIH GMPMAFLTRL ATEEKKDIFG 

       190        200        210        220        230        240 
WLQEEHKVNL RKLVYIGLRD VDRGEKKLLR EHGIKAFSMH DVDRHGIGRV VEMALAHIGN 

       250        260        270        280        290        300 
DTPIHLSFDV DALDPQWAPS TGTPVRGGLT LREGDFICEC VHETGNLISM DLVEVNPSLE 

       310        320 
AVGASDTIRT GCSLVRSALG DTLL

Q12611 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools