ID   C5L6X1_PERM5            Unreviewed;      1264 AA.
AC   C5L6X1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN   ORFNames=Pmar_PMAR020392 {ECO:0000313|EMBL:EER07233.1};
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:EER07233.1, 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; GG679899; EER07233.1; -; Genomic_DNA.
DR   RefSeq; XP_002775417.1; XM_002775371.1.
DR   AlphaFoldDB; C5L6X1; -.
DR   EnsemblProtists; EER07233; EER07233; Pmar_PMAR020392.
DR   GeneID; 9059926; -.
DR   InParanoid; C5L6X1; -.
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          82..117
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REPEAT          554..586
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1123..1155
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1264 AA;  141101 MW;  DD1FBBAFD4F66A8C CRC64;
     MTIELDNEKR YITSRPLEKP QRGEMDVVVS PSASSQASSR CRSDRGGRAH RHASFSEDSS
     EQENDHTNTP LARARLVSNM GRGKIDSKEI FKALEPDEDG KVDSVKLLEF LKKSGLATSD
     GRMRNTYKEL KSQDFVDFER FQTLKTSNEL VGKAFRGELA ISDFEAFCDV INDAYKDLED
     CTEGENADYI PTLATVNPDY WAISVCSVHA QRYSIGDSKV PFCLQSTCKP LNYCMAVELH
     GKEKVHEHVG HEPSGRNFNE RVLLQPKGIP HNPLINAGAI MVSSLLYMDK SEWERYEAVT
     ETWQHLAGMS RRPHIQYDTF MGERATANRN YCLAYMMAEE NAFPPNTDIQ KTLESYFQWC
     SLELDCEEMS VVAATLANGG ICPKTGERVF SQDTVSSCLS MMMSCGMYDY SGEFAFTCGF
     PAKSGVSGVL CIVIPGVCGI ATFSPRLDAL GNSVRGVKFC QMLSKRLPVH AFGGPQESVT
     DEAQTPPNHP LVEHRIRNCL GDTFRWRTSA QIDVLTNFTL TEYSSLWWSA AVGDAIRIRH
     LAARGIDVRT ADYDLRTALH LAVCNHHRET VKLLMFLGAD PEFRDRYNNT SIMDAQRESE
     DRCVRELKRD IALRASCPPM LPGEDGDIVL ARYFADMPWP LDSRRLIRAL EWYGLPRDSP
     RVQALLKDLG WYGSVRVGGM PDSLSVPGCL SVPEDMNLTG EAEALYSADE FSRIAKKHDI
     AVKALCGKLI VPNWPKFTQR LNECFSACCE DHPHQEIITV GVCTTDSQQY ARDESALPGS
     PSAASCASEY SPVWTPEECL KCFPTGGLIR PILYCMAVEM LGLEEVHKWM GREPSGEKQT
     YLGLDHLNRP HNPFVMMGTI NLCALLSRGL DKEYSGTGMR PSLERVLENW RKLSGSDTVP
     PEAAELGKKL DRRHSDLARS MAYRLRSIHR FPNGADIDDA IQLMFETHER EVNVAGVAAV
     AASFANSGVC PKTNERVFKD QTIRSGMWAY NLGIPGKNSN LGAGMAVVPG VLGICVHCPS
     SEFGEESAEK TIRNYGTSEE SYSLSRKGLD FFYHMEETFN FHLFKRHDPV LRASDRHVDP
     TLYYGSVKHE LTNQLIMACA NKDVYTVQYL LQLGVDPNVA DYDSRTAVHL AAASGCLSAM
     KLLMDAGARL NTYDRWGNTP YEEAKRHGRK NIVNFLEKLV MEGSPSMREE RNQTKSLDSD
     AAEDDFVNDA EAVMEYFGDV EVLGVEGEPL WYDDKEPKEW NTGMPAEVEV LGIDDAPGSG
     GHQE
//