ID   ASPG_DIRIM              Reviewed;         590 AA.
AC   Q9U518;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=L-asparaginase;
DE            EC=3.5.1.1;
DE   AltName: Full=DiAsp;
DE   AltName: Full=L-asparagine amidohydrolase;
OS   Dirofilaria immitis (Canine heartworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Dirofilaria.
OX   NCBI_TaxID=6287 {ECO:0000312|EMBL:AAF20016.1};
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAF20016.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Larva;
RX   PubMed=10579432; DOI=10.1016/s0020-7519(99)00087-9;
RA   Tsuji N., Morales T.H., Ozols V.V., Carmody A.B., Chandrashekar R.;
RT   "Identification of an asparagine amidohydrolase from the filarial parasite
RT   Dirofilaria immitis.";
RL   Int. J. Parasitol. 29:1451-1455(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC         Evidence={ECO:0000269|PubMed:10579432};
CC   -!- TISSUE SPECIFICITY: May be present in the larval cuticle.
CC       {ECO:0000269|PubMed:10579432}.
CC   -!- DEVELOPMENTAL STAGE: Adult and larval stages.
CC       {ECO:0000269|PubMed:10579432}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the asparaginase 1
CC       family. {ECO:0000305}.
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DR   EMBL; AF116552; AAF20016.1; -; mRNA.
DR   AlphaFoldDB; Q9U518; -.
DR   SMR; Q9U518; -.
DR   GO; GO:0004067; F:asparaginase activity; IDA:UniProtKB.
DR   GO; GO:0006528; P:asparagine metabolic process; IDA:UniProtKB.
DR   CDD; cd08963; L-asparaginase_I; 1.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 3.40.50.1170; -; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR006033; AsnA_fam.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR   InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR   InterPro; IPR040919; Asparaginase_C.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR041725; L-asparaginase_I.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   Pfam; PF13637; Ank_4; 2.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF53774; SSF53774; 1.
DR   TIGRFAMs; TIGR00519; asnASE_I; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Hydrolase; Repeat.
FT   CHAIN           1..590
FT                   /note="L-asparaginase"
FT                   /id="PRO_0000171090"
FT   DOMAIN          6..357
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   REPEAT          398..427
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          431..460
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          497..526
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000305"
FT   REPEAT          530..559
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000305"
FT   REGION          44..351
FT                   /note="Asparaginase"
FT   ACT_SITE        16
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT                   ECO:0000255|PROSITE-ProRule:PRU10100"
FT   BINDING         85..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   590 AA;  66253 MW;  655B2920D4B680BC CRC64;
     MQCEEAHVLV LYTGGTIGMK YIDGVYQPEA NYLLHAIRDL SLLNDDDYVS TYYSDAEIRP
     YCLPPLQHSK KRVVYWMIEY DPLLDSSDMT FDDWIHIGKD IQRAYDQYVG FVILHGTDTL
     AYTACALSFM LENVRKPIVI TGAQIPVCEV RSDGRENLIG ALIIAANYDI PEVTVYFNNK
     LFRGNRTVKI DNRSMDAFES PNMLPIAYMD VDIKVNYDSI FRSPSMAPFV VHDQLCRNVG
     LLRIFPSMSI ENVRASLQAP IEGVVLQTFG AGNMPSHRTD IIDELKKAVD RGCIIINCSQ
     CVRGQVDIHY LTGKVLYDMG IIPGSDMTAE AALTKLSYVL SKDCWELVEK KAMMVKNIRG
     ELTVAKAEPL KDLEIVSQMA RFLHLSSSHE MKLLCHAIFP QLLCYAASNG DIEMLKALHE
     NGVDLSVVDY NGRNALHVAA SAGHVGAVKY LLTQGVSFHL RDQWDENALV SAVKMKNKIL
     IETLRSAGAL LSINSRRLGV ELCLCASYGD TETLNSWLAA GADINQQDYN GETALHIAVK
     SRNKQLVHYL LDRDADPYKI DDFNLTPLRH AKKLNLQDLV IRMKKMKKVQ