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Database: UniProt
Entry: A0A0R3RYX8_9BILA
LinkDB: A0A0R3RYX8_9BILA
Original site: A0A0R3RYX8_9BILA 
ID   A0A0R3RYX8_9BILA        Unreviewed;       652 AA.
AC   A0A0R3RYX8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000750301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000750301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   AlphaFoldDB; A0A0R3RYX8; -.
DR   STRING; 1147741.A0A0R3RYX8; -.
DR   WBParaSite; EEL_0000750301-mRNA-1; EEL_0000750301-mRNA-1; EEL_0000750301.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.238.210; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   InterPro; IPR041541; Glutaminase_EF-hand.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF17959; EF-hand_14; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          78..167
FT                   /note="Glutaminase EF-hand"
FT                   /evidence="ECO:0000259|Pfam:PF17959"
FT   REPEAT          484..506
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          602..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  73113 MW;  A88182FABBDAE350 CRC64;
     MYSGTPINAQ RTKYRLAEHQ RRKNFKEMES DEYKCASAAV DNVSKILKNS RKSSVTRLLN
     DTAKGLKHVY QLSHPSQEDL TYDLFKCSKK PEEASLGKLL SVLRSFGIRE DDPRLKHTIE
     KMHEYELQIE DDCDTRHCLL TKEQFKECIR PSINLIAQTL RNDLIIPCWG EFTAKIKEIF
     DECASIHEGK VADYIPQLAR VDPKKWGLSI CTIDGQRVSY GDARVPFCFQ SISKAFNYAI
     VASDMGADFV HNYVGHEPSG RLFNEICLDC NGKPHNPLIN AGAIVVTSLL KMGHKMADRY
     DFVLTQYKKL AGGGYIGFNN ATFLSERDTA DRNYALSYYM KENNCFPGTV SLRDELDFYF
     QLCSLETTCE SAAVGLPAKS GVSGAMVVVV PNLMGICIWS PPLDKMSNSV RGVSFCKKMI
     DTFNFHNYDS LLHADTKKID PRKRGIPNES ELILEMMFAT KKGDIDDVRR MFLGGVDLNM
     SDYDGRTPLH LAASEGQTLM VDFFLDIAHV NPLVRDRWNR TAYDDALSFG FIKIAEKIKS
     AMDKISGGFV PITIPPDKAR QLLPENGDVL INLPEETNEW EKELRIVVDR LSYFDRSNSD
     CVTSPSSVEN GDGKTDFLEK SPDENGGSSA LDAESITDGS GGQIDLSIKF SS
//
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