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Database: UniProt
Entry: I7MJV7_TETTS
LinkDB: I7MJV7_TETTS
Original site: I7MJV7_TETTS 
ID   I7MJV7_TETTS            Unreviewed;       636 AA.
AC   I7MJV7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=asparaginase {ECO:0000256|ARBA:ARBA00012920};
DE            EC=3.5.1.1 {ECO:0000256|ARBA:ARBA00012920};
GN   ORFNames=TTHERM_00483700 {ECO:0000313|EMBL:EAR97237.1};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR97237.1, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
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DR   EMBL; GG662667; EAR97237.1; -; Genomic_DNA.
DR   RefSeq; XP_001017482.1; XM_001017482.1.
DR   AlphaFoldDB; I7MJV7; -.
DR   SMR; I7MJV7; -.
DR   STRING; 312017.I7MJV7; -.
DR   EnsemblProtists; EAR97237; EAR97237; TTHERM_00483700.
DR   GeneID; 7840821; -.
DR   KEGG; tet:TTHERM_00483700; -.
DR   eggNOG; KOG0503; Eukaryota.
DR   HOGENOM; CLU_019134_3_0_1; -.
DR   InParanoid; I7MJV7; -.
DR   OMA; NCVCYLI; -.
DR   OrthoDB; 1421816at2759; -.
DR   Proteomes; UP000009168; 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; 1.
DR   Gene3D; 3.40.50.40; -; 1.
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; IPR006033; AsnA_fam.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
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; 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   SFLD; SFLDS00057; Glutaminase/Asparaginase; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 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:UP000009168}.
FT   DOMAIN          57..265
FT                   /note="L-asparaginase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00710"
FT   DOMAIN          284..398
FT                   /note="Asparaginase/glutaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17763"
FT   REPEAT          480..512
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  73183 MW;  B70673B4607AFE06 CRC64;
     MNQKLELEQQ NSIHLHSQNS QSQERKKEFD KHQAVVFREK HNLECSQGLR IANQSRKVLI
     ICTGGTISMF PTENGLAVKK GFFEKFLRED SYFCDSDYTY FHSSDGFLIT PLTIYQQRIW
     YKIYELENPI DSTNMNVIYY DQIASIIETN YTLYDSFIIL HGTDTMAYTA SALSFMLENL
     SKTVILTGSQ IPCSMMRNDG FNNLLCSLTI AGHYTIPEVL VCFNDKLFRG NRCTKMDSSA
     MDSFDSPNFE PLATFKITIK IKWDKVLKRD PEKKFHVQKN LCDKIAIVKM HPFISSDTLK
     AILTNKDTKA IIIETYGAGN IPINRPELMQ MLQEAYDQGK VIVNLSQCYK SKVESIYETG
     RALLKVGVLC GWDCTTEAMA SKLAYLFSKN DSIENIRKNV QKNLRGELSP PIENDMFEFQ
     QENFIQALND ALQYRTNEKI DILKNLILPN IVCYMSKGGF HQSMQQLKVY GIDFDKGDYD
     NRTGLHLSAR EGQLETVKFL IKECKNINTV DKFGRTALFE AVINRHHDVI VELQRAGGII
     QAPKQEITSI LMEAIRTGDQ ELFDLFHLGG LQDWNTFQTV DGRNLGHVAA TFRQIEIIRF
     LKYQCKFRFT DKDRWGKTAL DEAKKRDFKE ICKLLS
//
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