ID F2UQB6_SALR5 Unreviewed; 1061 AA.
AC F2UQB6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=asparaginase {ECO:0000256|ARBA:ARBA00012920};
DE EC=3.5.1.1 {ECO:0000256|ARBA:ARBA00012920};
GN ORFNames=PTSG_10769 {ECO:0000313|EMBL:EGD79784.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL832988; EGD79784.1; -; Genomic_DNA.
DR RefSeq; XP_004988733.1; XM_004988676.1.
DR AlphaFoldDB; F2UQB6; -.
DR STRING; 946362.F2UQB6; -.
DR EnsemblProtists; EGD79784; EGD79784; PTSG_10769.
DR GeneID; 16069268; -.
DR KEGG; sre:PTSG_10769; -.
DR eggNOG; KOG0503; Eukaryota.
DR InParanoid; F2UQB6; -.
DR OrthoDB; 1421816at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
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; 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 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; 5.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000007799}.
FT DOMAIN 481..695
FT /note="L-asparaginase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00710"
FT DOMAIN 715..822
FT /note="Asparaginase/glutaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17763"
FT REPEAT 895..927
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 928..960
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 994..1018
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 38..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 490
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10099"
FT ACT_SITE 594
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
FT BINDING 576
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
FT BINDING 594..595
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
SQ SEQUENCE 1061 AA; 117357 MW; 855D5CCE54615931 CRC64;
MGNGGIRAEY VNGRRQALED DAKHQAVYES LAQPPRFVAP YQAGETRASS TSERFHGVGR
SASDLDAAGG RRIRTISGPA VPTLAEGASG PGTQQPSHAT SATSLTPTSL LFAEGVSTPG
SGKSSPIKQQ SDPGMMSDQS PGRPVKRERV RWRVRGHRPS RAKAEPRRRS QQGRSMFHQQ
QQQQQQQQQQ QQPQRKRQQQ QQQQQQQKKR WFFKRTRSMP QLRLRPPPMT AVLDSHASAA
EVHDAEEARK RALRELGQHQ RTRVHSHSTT RSGTPSTSAN LSSTSIKDAA TAAAVTSGGS
GSGGVGDDQG GTRPYASAHD QELAMLLGED LQIDWNYGDN QQQQQQQQQW QREETSPKKE
EEEEEEEEEE GTGEEAKESR ERIEQVEMQQ HEETVGGLEE EEEEEEEEQD EEDEGGELEW
GDAYEEERVS RLDEMDDDVT ASKRDRSGSA VRDPSVVVDP VNTALTAQER ELIDENCVIS
KVLVINTGGT IGMKRTPDGF APYPNFLEEY VRQTPLLNDV RYSRLFPEYA DGCVTPATSL
RANECFSRRV YYEVIECDPL LDSSNMDMTD WAQIASMIAD NYDAYQGFVI LHGTDTMSYT
ASALSFMLEN LGKSVVVTGA QRPMSENLSD GYSNFMGALT VAGYFNIPEV TILFSSKLYR
GNRTTKVTAF SLDAFDSPNY PPLMELGAGI SLRRDLVFPC KTLAKFQVHH NLIPNVSIMR
LFPGITVDTV ESFLKEPTQG VVIQSYGSGN GPDTRTDIWS AFKAAISRGV ILVNCTQCAH
GTVTDSYKAG RVLSAAGIIP GADMTPECAL TKLSYVLSMT DKTYAEKCAI MRQNLRGELT
TDPEEVEESK LDPMLAQLHP DIHPTLLCVA ASEGNIERLQ KLLDGGLSLL LYDYDMRTPL
HLACAEGHID TVRFLLRHGA SVHAVDRFGR TPLMDAILNT QLDVIELLVC TGATLQMSDV
EVGSVLCRLT SQEKFPEITA WIAARADCNC KDYNGQTALH VAAKLGFGRI AELLVTNGGA
DPNIPDEEGR TPLTLAIAYD RFDITEFLMR QEQLQDDIFV V
//
