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Q6TUJ5

- Q6TUJ5_LEIME

UniProt

Q6TUJ5 - Q6TUJ5_LEIME

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Protein
Submitted name: Arginase
Gene
ARG
Organism
Leishmania mexicana
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Cofactori

Manganese By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141Manganese 1; via pros nitrogenImported
Metal bindingi137 – 1371Manganese 1Imported
Metal bindingi137 – 1371Manganese 2Imported
Metal bindingi139 – 1391Manganese 2; via pros nitrogenImported
Metal bindingi141 – 1411Manganese 1Imported
Metal bindingi243 – 2431Manganese 1Imported
Metal bindingi243 – 2431Manganese 2Imported
Metal bindingi245 – 2451Manganese 2Imported

GO - Molecular functioni

  1. arginase activity Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Ligandi

ManganeseUniRule annotationImported, Metal-bindingUniRule annotationImported

Names & Taxonomyi

Protein namesi
Submitted name:
ArginaseImported
Gene namesi
Name:ARGImported
OrganismiLeishmania mexicanaImported
Taxonomic identifieri5665 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ITYX-ray1.80A13-329[»]
4IU0X-ray1.77A13-329[»]
4IU1X-ray1.95A13-329[»]
4IU4X-ray1.80A13-329[»]
4IU5X-ray1.95A13-329[»]
ProteinModelPortaliQ6TUJ5.

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family.UniRule annotation

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6TUJ5-1 [UniParc]FASTAAdd to Basket

« Hide

MEHVQQYKFY KEKKMSIVLA PFSGGQPHSG VELGPDYLLK QGLQQDMEKL    50
GWDTRLERVF DGKVVEARKA SDNGDRIGRV KRPRLTAECT EKIYKCVRRV 100
AEQGRFPLTI GGDHSIALGT VAGVLSVHPD AGVIWVDAHA DINTMSGTVS 150
GNLHGCPLSI LLGLDRENIP ECFSWVPQVL KPNKIAYIGL RAVDDEEKKI 200
LHDLNIAAFS MHHVDRYGID KVVSMAIEAV SPKGTEPVMV SYDVDTIDPL 250
YVPATGTPVR GGLSFREALF LCERIAECGR LVALDVVECN PLLAATESHV 300
NDTISVGCAI ARCMMGETLL YTPHTSSKL 329
Length:329
Mass (Da):36,082
Last modified:July 5, 2004 - v1
Checksum:i98A2BCA12455AF0B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY386701 Genomic DNA. Translation: AAR06176.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY386701 Genomic DNA. Translation: AAR06176.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4ITY X-ray 1.80 A 13-329 [» ]
4IU0 X-ray 1.77 A 13-329 [» ]
4IU1 X-ray 1.95 A 13-329 [» ]
4IU4 X-ray 1.80 A 13-329 [» ]
4IU5 X-ray 1.95 A 13-329 [» ]
ProteinModelPortali Q6TUJ5.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi IPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
PRINTSi PR00116. ARGINASE.
TIGRFAMsi TIGR01229. rocF_arginase. 1 hit.
PROSITEi PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Arginase plays a pivotal role in polyamine precursor metabolism in Leishmania. Characterization of gene deletion mutants."
    Roberts S.C., Tancer M.J., Polinsky M.R., Gibson K.M., Heby O., Ullman B.
    J. Biol. Chem. 279:23668-23678(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of arginase from Leishmania mexicana and implications for the inhibition of polyamine biosynthesis in parasitic infections."
    D'Antonio E.L., Ullman B., Roberts S.C., Dixit U.G., Wilson M.E., Hai Y., Christianson D.W.
    Arch. Biochem. Biophys. 535:163-176(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 13-329 IN COMPLEX WITH MANGANESE.

Entry informationi

Entry nameiQ6TUJ5_LEIME
AccessioniPrimary (citable) accession number: Q6TUJ5
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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