ID A0A075AVA0_ROZAC Unreviewed; 645 AA.
AC A0A075AVA0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=asparaginase {ECO:0000256|ARBA:ARBA00012920};
DE EC=3.5.1.1 {ECO:0000256|ARBA:ARBA00012920};
DE Flags: Fragment;
GN ORFNames=O9G_005260 {ECO:0000313|EMBL:EPZ34178.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ34178.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ34178.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ34178.1,
RC ECO:0000313|Proteomes:UP000030755};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(2013).
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DR EMBL; KE560978; EPZ34178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075AVA0; -.
DR STRING; 988480.A0A075AVA0; -.
DR EnsemblFungi; EPZ34178; EPZ34178; O9G_005260.
DR HOGENOM; CLU_019134_3_0_1; -.
DR OrthoDB; 1421816at2759; -.
DR Proteomes; UP000030755; Unassembled WGS sequence.
DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006528; P:asparagine 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; 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 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; PS00144; ASN_GLN_ASE_1; 1.
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 Ligase {ECO:0000313|EMBL:EPZ34178.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030755}.
FT DOMAIN 33..270
FT /note="L-asparaginase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00710"
FT DOMAIN 290..404
FT /note="Asparaginase/glutaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17763"
FT REPEAT 486..518
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 519..551
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 584..606
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10099"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
FT NON_TER 645
FT /evidence="ECO:0000313|EMBL:EPZ34178.1"
SQ SEQUENCE 645 AA; 71668 MW; A74E72D25F98C5A3 CRC64;
MEPLCEETHL NESVAFQQTD AGISKMIHNK MSKVLIIYTG GTIGMKYNEK RGYIPVPNYM
YDKLASMSQF HDVSFVPPMK ETQLSALSSP NPAKNKSVSF KLPNKPTVNK NKFLVTPPSI
HQKRVMYSIL EYSPLLDSCD MSMDEWIRIA TDIELNYHSY DAFIVLHGTD TMAYTASALS
FLLEDLGKTV IVTGAQVPIG EVRTDATNNI LGALMVAGHY QIPEVGLFFN NKLYRGNRSV
KANAMDFDAF ESPNQKPLVK MGININVNWG LVLRPDNISQ MRAQKTMNSN VGSLRIFPSI
SETTIRSFLA PPMQGVVLQT FGVGNAPTRP DLLSALKEAS DRGVVIVNVS QCRKGNVSDV
YATGRALTEV GVIPGSDMTL ECALTKLSYL LGKGYPPDEV RRLMKKSLRG EMTSSVDKNL
FSFSNSEFLK NIFSAVKAEN SQEKDFVQQS IFPVLHISAA SKGCKGILEK LLNETNCAYI
NCYDSNAKTM LHVASAKGHY ELVEYLIMAG ANVHLKDSGN KNSLITAIMN NQIEIATLLI
KAGARITVDD NSIQLFFRAI EAGNDRLIKV WLDSGIDINF QNIEGKTALH KAVFSGDIAI
VQLLLNECKD RIQKNLKDRW NRRPVDDAAF FGYFDIVNLL FEDQE
//
