ID M7BIH3_CHEMY Unreviewed; 474 AA.
AC M7BIH3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=60 kDa lysophospholipase {ECO:0000313|EMBL:EMP28052.1};
DE Flags: Fragment;
GN ORFNames=UY3_14820 {ECO:0000313|EMBL:EMP28052.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28052.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB565341; EMP28052.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BIH3; -.
DR STRING; 8469.M7BIH3; -.
DR eggNOG; KOG0503; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
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; IPR027475; Asparaginase/glutaminase_AS2.
DR InterPro; IPR040919; Asparaginase_C.
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; 1.
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; PR01415; ANKYRIN.
DR PRINTS; PR00139; ASNGLNASE.
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; 2.
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:UP000031443}.
FT DOMAIN 49..156
FT /note="L-asparaginase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00710"
FT DOMAIN 151..251
FT /note="Asparaginase/glutaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17763"
FT REPEAT 332..364
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 365..397
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
FT BINDING 95..96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP28052.1"
SQ SEQUENCE 474 AA; 51975 MW; 05855CD1CFE87127 CRC64;
LAPEANKLVK ALKKMPMLHD EVYAKETKLY DFHRFPDNTL VLPLSEQNKR IVYTILELSP
LLDSSNMTTD DWAKIARNIE KYYEQYDGFV ILHGTDTMAY TASALSFMCE NLGKTIVLTG
SQVPIYELRN DGRANLLGAL LIAGQFVIPE VKAFLHAPME GIVLETYGTG NAPNNREDLL
EELRKATERK VVILNCTQCL RGSVAAVYAT GQTLTAVGVI PGGDMTPEAA LAKLSYTLSK
SHLSWEEKKE MLSENLRGEM TVVPTGAKIS LTDSKFIQVI AKSLSVSCKE ELEAIRDALI
PSLACAAAKT GDIDALKAIG EMGGNLSCED YDGRTPLHIA SSEGNLQLVE YLLKYGATVY
AKDMFGATPL KYAVKFRHVE VIQLLRETGA HLSSQELENI GTELCSLAAN GDVEGLYAWY
LAGANLEQAG YDGRTPLQIV CSKRYPVHIN MNSSKRHFDA LCNSNPHSLH CGTV
//
