ID A0A9W8E0B3_9FUNG Unreviewed; 413 AA.
AC A0A9W8E0B3;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 18-JUN-2025, entry version 8.
DE RecName: Full=asparaginase {ECO:0000256|ARBA:ARBA00012920};
DE EC=3.5.1.1 {ECO:0000256|ARBA:ARBA00012920};
DE Flags: Fragment;
GN ORFNames=IWQ62_006199 {ECO:0000313|EMBL:KAJ1952541.1};
OS Dispira parvispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Dimargaritomycetes; Dimargaritales; Dimargaritaceae; Dispira.
OX NCBI_TaxID=1520584 {ECO:0000313|EMBL:KAJ1952541.1, ECO:0000313|Proteomes:UP001150925};
RN [1] {ECO:0000313|EMBL:KAJ1952541.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RSA 1196 {ECO:0000313|EMBL:KAJ1952541.1};
RA Reynolds N.K., Stajich J.E., Barry K., Grigoriev I.V., Crous P.,
RA Smith M.E.;
RT "Phylogenomic reconstructions and comparative analyses of Kickxellomycotina
RT fungi.";
RL Submitted (JUL-2022) 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:KAJ1952541.1}.
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DR EMBL; JANBPY010003163; KAJ1952541.1; -; Genomic_DNA.
DR OrthoDB; 542841at2759; -.
DR Proteomes; UP001150925; 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:UniProtKB-ARBA.
DR CDD; cd08963; L-asparaginase_I; 1.
DR FunFam; 3.40.50.40:FF:000001; L-asparaginase 1; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 1.
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 PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1.
DR PANTHER; PTHR11707; L-ASPARAGINASE; 1.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR PIRSF; PIRSF500176; L_ASNase; 1.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP001150925}.
FT DOMAIN 96..245
FT /note="L-asparaginase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00710"
FT DOMAIN 265..380
FT /note="Asparaginase/glutaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17763"
FT REGION 53..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
FT NON_TER 413
FT /evidence="ECO:0000313|EMBL:KAJ1952541.1"
SQ SEQUENCE 413 AA; 45302 MW; 92FE2A3902BDE754 CRC64;
MKNTDQGYVP VPNFLSEQLS RIDRFHDPTG WSQGLNISRS SSTNSLADMA TMASNPHATG
TPVPPSSTFP STEHSEEQTA GAFTMSPWLI TPKSMYGKRI QYRILEYSPL LDSCNMTMAQ
WIQIATDIET YYAHVDAFII LHGTDTMAYT ASALSFLLED LGKPVILTGS QVPISEVRND
AVENLLGALT IAGHFVIPEV CLYFSNTLYR GNRTSKMDAM NFNAFDSPNF HPLVEVGVDI
KVNWSDIVRP TALSRFRAHK VMNPNVATLR LFPGITAAAI RAFLTPPIAG IVLETYGAGN
APNTRQDLIA ALKEASERGV VIVNCSQCRK GLVSDLYATS KPLREANVVS GRDMTAECAL
TKLSYLLGKN FTPEECRVLM SKSLRGELTT ADPVHGVGFH NRVHHFLQIL ATT
//
