ID   ASGL1_DROPS             Reviewed;         325 AA.
AC   Q29I93;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable isoaspartyl peptidase/L-asparaginase GA20639;
DE            EC=3.4.19.5;
DE            EC=3.5.1.1;
DE   AltName: Full=Beta-aspartyl-peptidase GA20639;
DE   AltName: Full=Isoaspartyl dipeptidase GA20639;
DE   AltName: Full=L-asparagine amidohydrolase GA20639;
DE   Contains:
DE     RecName: Full=Probable isoaspartyl peptidase/L-asparaginase GA20639 alpha chain;
DE   Contains:
DE     RecName: Full=Probable isoaspartyl peptidase/L-asparaginase GA20639 beta chain;
DE   Flags: Precursor;
GN   ORFNames=GA20639;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC       Does not have aspartylglucosaminidase activity and is inactive toward
CC       GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
CC       {ECO:0000250}.
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:0000250|UniProtKB:Q7L266};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC         polypeptide.; EC=3.4.19.5; Evidence={ECO:0000250|UniProtKB:Q7L266};
CC   -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC       autocleavage. {ECO:0000250}.
CC   -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC       activates the enzyme. The N-terminal residue of the beta subunit is
CC       responsible for the nucleophile hydrolase activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR   EMBL; CH379063; EAL32760.1; -; Genomic_DNA.
DR   RefSeq; XP_001355701.1; XM_001355665.3.
DR   AlphaFoldDB; Q29I93; -.
DR   SMR; Q29I93; -.
DR   STRING; 7237.FBpp0273649; -.
DR   EnsemblMetazoa; FBtr0275211; FBpp0273649; FBgn0080633.
DR   GeneID; 4815446; -.
DR   KEGG; dpo:Dpse_GA20639; -.
DR   eggNOG; KOG1592; Eukaryota.
DR   HOGENOM; CLU_021603_1_2_1; -.
DR   InParanoid; Q29I93; -.
DR   OMA; RRMAWGY; -.
DR   PhylomeDB; Q29I93; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0080633; Expressed in male reproductive system and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008798; F:beta-aspartyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033345; P:asparagine catabolic process via L-aspartate; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04702; ASRGL1_like; 1.
DR   InterPro; IPR033844; ASRGL1_meta.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000246; Peptidase_T2.
DR   PANTHER; PTHR10188; PTHR10188; 1.
DR   Pfam; PF01112; Asparaginase_2; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..183
FT                   /note="Probable isoaspartyl peptidase/L-asparaginase
FT                   GA20639 alpha chain"
FT                   /id="PRO_0000420569"
FT   CHAIN           184..325
FT                   /note="Probable isoaspartyl peptidase/L-asparaginase
FT                   GA20639 beta chain"
FT                   /id="PRO_0000420570"
FT   ACT_SITE        184
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         212..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         235..238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  34399 MW;  BA6B5E618AB35038 CRC64;
     MPRPVLLIHG GAGDIPDSRI AGKFKGIKEA LRCAWGSLVP ASGAKGGALD AVETAVRSME
     LDENFNAGYG SCLNTDGQVE MEASLMEGQD LRAGCVTLLR DVMHPITVAR RLMEKQRHTF
     IGGEAAQELA LSTGSERLPA NALVTEGARF TLQQFKEQLT QGKDPFFART ELAAEQKTDP
     SGETVGAVAM DHNGQIVVGT STGGITGKWP GRIGDTPILG SGTYADNARG GVSTTGHGET
     IMRYNLAQRI LAAIEHKGMS AQAAADQECR EMTRRIGGTG GAIVVGHAGD LGISFTSQRM
     AWGYIQDDTI FYGIEGQVVH QEPLS