Q9U518 (ASPG_DIRIM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-asparaginase EC=3.5.1.1 Alternative name(s): DiAsp L-asparagine amidohydrolase
Organism	Dirofilaria immitis (Canine heartworm)
Taxonomic identifier	6287 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Nematoda › Chromadorea › Spirurida › Filarioidea › Onchocercidae › Dirofilaria

Protein attributes

Sequence length	590 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-asparagine + H2O = L-aspartate + NH3. Ref.1
Tissue specificity	May be present in the larval cuticle. Ref.1
Developmental stage	Adult and larval stages. Ref.1
Sequence similarities	In the N-terminal section; belongs to the asparaginase 1 family. Contains 4 ANK repeats.

Ontologies

Keywords
Domain	ANK repeat Repeat
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	asparagine metabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	asparaginase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 590	590	L-asparaginase		PRO_0000171090
Regions
	Repeat	398 – 427	30	ANK 1
	Repeat	431 – 460	30	ANK 2
	Repeat	497 – 526	30	ANK 3
	Repeat	530 – 559	30	ANK 4
	Region	44 – 351	308	Asparaginase
	Region	85 – 87	3	Substrate binding By similarity
	Region	117 – 118	2	Substrate binding By similarity
Sites
	Active site	16	1	O-isoaspartyl threonine intermediate By similarity UniProtKB P06608

Sequences

	Sequence		Length	Mass (Da)
	Q9U518 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 655B2920D4B680BC	FASTA	590	66,253
	10 20 30 40 50 60 MQCEEAHVLV LYTGGTIGMK YIDGVYQPEA NYLLHAIRDL SLLNDDDYVS TYYSDAEIRP 70 80 90 100 110 120 YCLPPLQHSK KRVVYWMIEY DPLLDSSDMT FDDWIHIGKD IQRAYDQYVG FVILHGTDTL 130 140 150 160 170 180 AYTACALSFM LENVRKPIVI TGAQIPVCEV RSDGRENLIG ALIIAANYDI PEVTVYFNNK 190 200 210 220 230 240 LFRGNRTVKI DNRSMDAFES PNMLPIAYMD VDIKVNYDSI FRSPSMAPFV VHDQLCRNVG 250 260 270 280 290 300 LLRIFPSMSI ENVRASLQAP IEGVVLQTFG AGNMPSHRTD IIDELKKAVD RGCIIINCSQ 310 320 330 340 350 360 CVRGQVDIHY LTGKVLYDMG IIPGSDMTAE AALTKLSYVL SKDCWELVEK KAMMVKNIRG 370 380 390 400 410 420 ELTVAKAEPL KDLEIVSQMA RFLHLSSSHE MKLLCHAIFP QLLCYAASNG DIEMLKALHE 430 440 450 460 470 480 NGVDLSVVDY NGRNALHVAA SAGHVGAVKY LLTQGVSFHL RDQWDENALV SAVKMKNKIL 490 500 510 520 530 540 IETLRSAGAL LSINSRRLGV ELCLCASYGD TETLNSWLAA GADINQQDYN GETALHIAVK 550 560 570 580 590 SRNKQLVHYL LDRDADPYKI DDFNLTPLRH AKKLNLQDLV IRMKKMKKVQ

References

[1]

"Identification of an asparagine amidohydrolase from the filarial parasite Dirofilaria immitis." Tsuji N., Morales T.H., Ozols V.V., Carmody A.B., Chandrashekar R. Int. J. Parasitol. 29:1451-1455(1999) [PubMed: 10579432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Larva.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF116552 mRNA. Translation: AAF20016.1.
3D structure databases
ProteinModelPortal	Q9U518.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR006033. AsnASEI. IPR006034. Asparaginase/glutaminase. IPR020827. Asparaginase/glutaminase_CS. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit.
PANTHER	PTHR11707. Asp/Glutamnse. 1 hit.
Pfam	PF00023. Ank. 1 hit. PF12796. Ank_2. 1 hit. PF00710. Asparaginase. 1 hit. [Graphical view]
PRINTS	PR00139. ASNGLNASE.
SMART	SM00248. ANK. 5 hits. SM00870. Asparaginase. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF53774. Asp/Glutamnse. 1 hit.
TIGRFAMs	TIGR00519. AsnASE_I. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 2 hits. PS00144. ASN_GLN_ASE_1. 1 hit. PS00917. ASN_GLN_ASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASPG_DIRIM

Accession

Primary (citable) accession number: Q9U518

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	May 1, 2000
Last modified:	October 19, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)