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Reviewed, UniProtKB/Swiss-Prot P33280 (ARGI_NEUCR)

Last modified September 1, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginase
    EC=3.5.3.1
Gene names
Name: car-1
Synonyms: aga
ORF Names: NCU02333
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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

Homohexamer.

Subcellular location

Cytoplasm. Ref.1

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative initiation
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

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

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 41 kDa (identifier: P33280-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 36 kDa (identifier: P33280-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Arginase
PRO_0000002087

Regions

Region176 – 1805Substrate binding By similarity
Region187 – 1893Substrate binding By similarity

Sites

Metal binding1461Manganese 1 By similarity
Metal binding1741Manganese 1 By similarity
Metal binding1741Manganese 2 By similarity
Metal binding1761Manganese 2 By similarity
Metal binding1781Manganese 1 By similarity
Metal binding2801Manganese 1 By similarity
Metal binding2801Manganese 2 By similarity
Metal binding2821Manganese 2 By similarity
Binding site2331Substrate By similarity
Binding site3251Substrate By similarity

Natural variations

Alternative sequence1 – 3333Missing in isoform 36 kDa.
VSP_018650

Experimental info

Sequence conflict351 – 3588CALGESLL → SRSRRNVL in AAC82503. Ref.1
Sequence conflict351 – 3588CALGESLL → SRSRRNVL in AAC82504. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 41 kDa [UniParc].

Last modified August 31, 2004. Version 3.
Checksum: 259CF279863D6977

FASTA35838,265
        10         20         30         40         50         60 
MSPSLVDNHA AAYIAAPSSA KAPMIQKPGN TFGMSSPIES KFLSQPRDLG IVAVGFSGGQ 

        70         80         90        100        110        120 
CKPGVDAAPS ALIESGLLTQ LREELGYRLH GDDEVHLYTD LVPKEDPPHR NMKNPRAVSN 

       130        140        150        160        170        180 
VTKRIAEQVH SHAKEGRLVL TLGGDHSIAI GTIAGSAKAI KERLGREIAV IWVDAHADIN 

       190        200        210        220        230        240 
TPETSGSGNI HGMPVSFLTG LASEDKEEFF GWLKPDHLLS VKKLVYIGLR DVDPGEKRIL 

       250        260        270        280        290        300 
RENGIKAFSM HDIDKHGIGR VMEMALGHIG NDTPIHLSFD VDALDPMWAP STGTPVRGGL 

       310        320        330        340        350 
TLREGDFICE CVHETGSLVA VDLVEVNPTL AAPNDVGAHE TVRAGCSLVR CALGESLL 

« Hide

Isoform 36 kDa.

Checksum: E6FFB8F34AAEDC8C
Show »

FASTA32534,939

References

« Hide 'large scale' references
[1]"Multiple forms of arginase are differentially expressed from a single locus in Neurospora crassa."
Marathe S.V., Yu Y.G., Turner G.E., Palmier C., Weiss R.L.
J. Biol. Chem. 273:29776-29785(1998) [PubMed: 9792692] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE INITIATION, SUBCELLULAR LOCATION.
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"Purification and characterization of arginase from Neurospora crassa."
Borkovich K.A., Weiss R.L.
J. Biol. Chem. 262:7081-7086(1987) [PubMed: 2953715] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

L20687 Genomic DNA. Translation: AAC82503.1.
L20687 Genomic DNA. Translation: AAC82504.1.
AABX02000010 Genomic DNA. Translation: EAA30523.2. Different initiation.
PIRT47228.
T47229.

3D structure databases

HSSPHSSP built from PDB template 1D3V based on UniProtKB P07824.
ModBaseSearch...

Protein-protein interaction databases

STRINGP33280.

Genome annotation databases

NMPDRfig|5141.1.peg.9042.
UCSCY18D10A.17. c. elegans.

Enzyme and pathway databases

BRENDA3.5.3.1. 266.

Family and domain databases

InterProIPR005924. Arginase.
IPR014033. Arginase_sub.
IPR006035. Ureohydrolase.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. rocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGI_NEUCR
AccessionPrimary (citable) accession number: P33280
Secondary accession number(s): Q7RV08, Q9URL4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 31, 2004
Last modified: September 1, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents