ID   C5LIJ3_PERM5            Unreviewed;      1231 AA.
AC   C5LIJ3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN   ORFNames=Pmar_PMAR014612 {ECO:0000313|EMBL:EER03396.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER03396.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001062};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076}.
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DR   EMBL; GG682243; EER03396.1; -; Genomic_DNA.
DR   RefSeq; XP_002771580.1; XM_002771534.1.
DR   AlphaFoldDB; C5LIJ3; -.
DR   EnsemblProtists; EER03396; EER03396; Pmar_PMAR014612.
DR   GeneID; 9047482; -.
DR   InParanoid; C5LIJ3; -.
DR   OrthoDB; 177173at2759; -.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR015868; Glutaminase.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF04960; Glutaminase; 2.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT   DOMAIN          58..93
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REPEAT          500..532
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1092..1124
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1231 AA;  136911 MW;  5B8152A5D7CAFD2B CRC64;
     MDVVVSPSAS SQASSRCRSD RGGRAHRHAS FSEDSSEQEN DHTNTPLARA RLVSNMGRGK
     IDSKEIFKAL EPDEDGKVDS VKLLEFLKKS GLATSDGRMR NTYKELKSQD FVDFERFQTL
     KTSNELVGKA FRGELAISDF EAFCDVINDA YKDLEDCTEG ENADYIPTLA TVNPDYWAIS
     VCSVHAQRYS IGDSKVPFCL QSTCKPLNYC MAVELHGKEK VHEHVGHEPS GRNFNERVLL
     QPKGIPHNPL INAGAIMVSS LLYMDKSEWE RYEAVTETWQ HLAGMSRRPH IQYDTFMGER
     ATANRNYCLA YMMAEENAFP PNTDIQKTLE SYFQWCSLEL DCEEMSVVAA TLANGGICPK
     TGERVFSQDT VSSCLSMMMS CGMYDYSGEF AFTCGFPAKS GVSGVLCIVI PGVCGIATFS
     PRLDALGNSV RGVKFCQMLS KRLPVHAFGG ILTISCSVDV LTNFTLTEYS SLWWSAAVGD
     AIRIRHLAAR GIDVRTADYD LRTALHLAVC NHHRETVKLL MFLGADPEFR DRYNNTSVMD
     AQRESEDRCV RELKRDIALR ASCPPMLPGE DGDIVLARYF ADMPWPLDSR RLIRALEWYG
     LPRDSPRVQA LLKVLNGLYL VQDLGWYGSV GVGGMPDSLS VPGCLSVPED MNLTGEAEAL
     YSADEFSRIA KKHDIAVKAL CGKLIVPNWP KFTQRLNECF SACCEDHPHQ EIITVGVCTT
     DSQQYARDES ALPGSPSAAS CVSEYSPVWT PEECLKCFPT GGLIRPILYC MAVEMLGLEE
     VHKWMGREPS GEKQTYLGLD HLNRPHNPFV MMGTINLCAL LSRGLDKEYS GTGMRPSLER
     VLENWRKLSG SDTVPPEAAE LGKKLDRRHS DLARSMAYRL RSIHRFPNGA DIDDAIQLMF
     ETHEREVNVA GVAAVAASFA NSGVCPKTNE RVFKDQTIRY ALSLMYSCGM DQRSGMWAYN
     LGIPGKNSNL GAGMAVVPGV LGICVHCPSA EFGEESAEKT IRNYGTSEES YSLSRKGLDF
     FYHMEETFNF HLFKRHDPVL RGSDRHVDPT LYYGSVKHEL TNQLIMACAN KDVYTVQYLL
     QLGVDPNVAD YDSRTAVHLA AASGCLSAMK LLMDAGARLN TYDRWGNTPY EEAKRHGRKN
     IVKFLEKLVM EGSPSMREER KTKSLDSDAA EDDFVNDAEA VMEYFGDVEV LGVEGEPLWY
     DDKDPKEWNT GMPAEVEVLG IDDAPGSGGH Q
//