Q6TUJ5 (Q6TUJ5_LEIME) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Arginase EMBL AAR06176.1

Gene names

Name:

ARG EMBL AAR06176.1

Organism

Leishmania mexicana EMBL AAR06176.1

Taxonomic identifier

5665 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania › Leishmania › Leishmania mexicana species complex

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Cofactor	Manganese By similarity. RuleBase RU003684
Sequence similarities	Belongs to the arginase family. RuleBase RU003684

Ontologies

Keywords
Ligand	Manganese RuleBase RU003684 Metal-binding RuleBase RU003684
Molecular function	Hydrolase RuleBase RU003684
Technical term	3D-structure PDB 4ITY PDB 4IU0 PDB 4IU1 PDB 4IU4 PDB 4IU5
Gene Ontology (GO)
Biological_process	arginine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	arginase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q6TUJ5 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 98A2BCA12455AF0B	FASTA	329	36,082
	10 20 30 40 50 60 MEHVQQYKFY KEKKMSIVLA PFSGGQPHSG VELGPDYLLK QGLQQDMEKL GWDTRLERVF 70 80 90 100 110 120 DGKVVEARKA SDNGDRIGRV KRPRLTAECT EKIYKCVRRV AEQGRFPLTI GGDHSIALGT 130 140 150 160 170 180 VAGVLSVHPD AGVIWVDAHA DINTMSGTVS GNLHGCPLSI LLGLDRENIP ECFSWVPQVL 190 200 210 220 230 240 KPNKIAYIGL RAVDDEEKKI LHDLNIAAFS MHHVDRYGID KVVSMAIEAV SPKGTEPVMV 250 260 270 280 290 300 SYDVDTIDPL YVPATGTPVR GGLSFREALF LCERIAECGR LVALDVVECN PLLAATESHV 310 320 NDTISVGCAI ARCMMGETLL YTPHTSSKL

References

[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., Gaur Dixit U., Wilson M.E., Hai Y., Christianson D.W. Submitted (JAN-2013) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 13-329.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY386701 Genomic DNA. Translation: AAR06176.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q6TUJ5.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.40.800.10. 1 hit.

InterPro

IPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]

PANTHER

PTHR11358. PTHR11358. 1 hit.
PTHR11358:SF2. PTHR11358:SF2. 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

Q6TUJ5_LEIME

Accession

Primary (citable) accession number: Q6TUJ5

Entry history

Integrated into UniProtKB/TrEMBL:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)