ID A0A164KJZ7_9CRUS Unreviewed; 742 AA.
AC A0A164KJZ7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=asparaginase {ECO:0000256|ARBA:ARBA00012920};
DE EC=3.5.1.1 {ECO:0000256|ARBA:ARBA00012920};
GN ORFNames=APZ42_033975 {ECO:0000313|EMBL:KZS03330.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS03330.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS03330.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS03330.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS03330.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS03330.1}.
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DR EMBL; LRGB01003310; KZS03330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164KJZ7; -.
DR STRING; 35525.A0A164KJZ7; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009066; P:aspartate family amino acid metabolic process; IEA:UniProt.
DR CDD; cd08963; L-asparaginase_I; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 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; 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 NCBIfam; TIGR00519; asnASE_I; 1.
DR PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1.
DR PANTHER; PTHR11707; L-ASPARAGINASE; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 2.
DR PIRSF; PIRSF500176; L_ASNase; 2.
DR PRINTS; PR00139; ASNGLNASE.
DR SFLD; SFLDS00057; Glutaminase/Asparaginase; 1.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT DOMAIN 155..369
FT /note="L-asparaginase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00710"
FT DOMAIN 389..505
FT /note="Asparaginase/glutaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17763"
FT REPEAT 582..614
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 615..647
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 681..713
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT ACT_SITE 164
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001220-1"
FT ACT_SITE 268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
FT BINDING 268..269
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
SQ SEQUENCE 742 AA; 81412 MW; 90D16CF778EC9E86 CRC64;
MNDVVTSQVM ETATEVAIGI GVRCLQWAVH LTIGAHHHQP ITHHLEPDLS TVEGPHLPAL
WATPMVDSIV TCTKRCHLIH TALDVEDMLS SSRKETEAVK IVASTLEADD DSEIVSTSPS
NGGRPPIDAA HVPKKLWRHS SMDVCANLET KNESKVLVLY TGGTIGMMRN ENGALVPMAN
ALERMIRKAI HLHDEKYATA RFGAGNTHKA PLALPSLGPD AKRILYTIYE YEPLLDSSNM
TMDDWINIAK DLRRSYELFD GFVILHGTDT LSYTASALSF MLENLGKTVI VTGSQIPIFE
IRSDGRDNFL GALIVAGTYC IPEVCVFFNH KLYRGNRTVK RSNGSLDAFD SPNLPSLAHF
GIDVHVEYRS VFRPVTIDRF RVHSILNRNV CLLRLFPSIT IQTVRALLHP PIEGIVMQTY
GSGNVPSNRL DLIDELRRAT KNGVLIINTT QCCHGAVQAI YETGAALLEA GVIPGADMTP
EAALTKLSYV LSKDEWDLET KRQMMMTNLR GELTLPHTKL DKEMELVEAL ARSLHLSSSE
EMEQLKDVLF PSLICSAVKT GDLYKLESLE RYGANLSAGD VDGRTPLHAA ASEGRLAVVE
FLLGRGASVH SRDRSGNTPL MSAVTGDHND VIAVLVQCGA HLTSGPHTIG EMLCSAAARG
NVKRLISLME AGADLNQPDV SNRTALHLAA HHNQESCVIF LLKNRALRDK KDDFGLTPAD
VARKFEHGNV LKMLSVSEEN YV
//
