ID A0A212ETD0_DANPL Unreviewed; 1045 AA.
AC A0A212ETD0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=asparaginase {ECO:0000256|ARBA:ARBA00012920};
DE EC=3.5.1.1 {ECO:0000256|ARBA:ARBA00012920};
GN ORFNames=KGM_202693 {ECO:0000313|EMBL:OWR44746.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR44746.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR44746.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR44746.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
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:OWR44746.1}.
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DR EMBL; AGBW02012595; OWR44746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212ETD0; -.
DR STRING; 278856.A0A212ETD0; -.
DR KEGG; dpl:KGM_202693; -.
DR InParanoid; A0A212ETD0; -.
DR Proteomes; UP000007151; 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; 2.
DR Gene3D; 3.40.50.40; -; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 2.
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; 2.
DR PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1.
DR PANTHER; PTHR11707; L-ASPARAGINASE; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00710; Asparaginase; 2.
DR Pfam; PF17763; Asparaginase_C; 2.
DR PRINTS; PR00139; ASNGLNASE.
DR SFLD; SFLDS00057; Glutaminase/Asparaginase; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00870; Asparaginase; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF53774; Glutaminase/Asparaginase; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 2.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT DOMAIN 4..143
FT /note="L-asparaginase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00710"
FT DOMAIN 162..269
FT /note="Asparaginase/glutaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17763"
FT REPEAT 337..369
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 477..692
FT /note="L-asparaginase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00710"
FT DOMAIN 711..818
FT /note="Asparaginase/glutaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17763"
FT REPEAT 991..1023
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
FT ACT_SITE 590
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
SQ SEQUENCE 1045 AA; 114865 MW; 1F4D53FA8098864D CRC64;
MIEYEILLDS SNMAFDDWIQ IAEDVMKYYD QYDGFVVLHG TDTLSYTASA LSFMFENIGK
SIVLTGSQIP IFEPRSDGSD NLVSSLLIAG GLNIPEVTVF FGNKLYRGNR TRKISANNLN
AFSSPNCVPL VEVGIDFEVN KKAIFKPTNK ERCHLHAKMS KNVGLLRIFP SISTSLIRAF
FQPPIEGVVL ESYGAGNIPS NREDLLTEIS AAVKRGMIVV NITQCLRGGV VAAMYETGKF
LSECGVVSGY DMTPEAALAK LSYVLSKTEL TYQQKVDDDT LLEALALTLN IESQNKLVEV
TGKVFNALLL YAIGKNDVGA VKMMLDMGAN INTKNSDGST VLHEAVLKGN MQMIEYLLKN
GAEVNIWTRC GESPLLAAIH KDNVAVICLL QKYGACLSSE DRKIVADMSS LAARCGDLKK
LKTLIAAGLD LSAPDEIGQN LLHKKIEAKV KKARSFVELS ILNTSNSVKS LGRNERRVLV
LYTGGTIGMV KNKDGVLVPQ KGAFENLIRG YPQLHDIMSW RQRLSEPNFD TSFLVLPEAK
ELDMRISYKI IEYENLLDSS NMTEQEWIRI AEDIMKHYEE YDGFVVLHGT DTLSYTASAL
SFMFENIGKG IVLTGSQIPI FEPRSDGSDN LVSSLLIAGG LNIPEVTVFF GNKLYRGNRT
RKISVNNLYA FNSPNCVPLV EVGIDFEVNK KAIFKPTVIE RCHLHAKMSK NVGLLRIFPS
ISASVVRTFF QPPIEGVVLE SYGAGNIPSN REDLFSEIAA AVKRGMIVVN ITQCTRGSVI
SPMYETGRLI SECGVVSGYD MTPEAALTKL SYVLSKTELT YQQKVDMMVT NIRGELTNTS
SIAIEDNTLI DALASSLNIQ SPKKLIEVTE KVFSALLLYA IEHDDLRAVK KMLDMGADVN
AQNSEGKTVL YEAILRGNMP IVECGETPLL TAIHKDDHTI ISLLRQCGAH LANVDTKPVA
EMLSLAARSG VVHKLESLRA AGSELNLPDE IGQTPLHKAV LCNNPAVVRY LLSQGVDKET
KDILGFTPMD CAIKLELTNI IDMLK
//
