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Database: UniProt
Entry: T1HK74_RHOPR
LinkDB: T1HK74_RHOPR
Original site: T1HK74_RHOPR 
ID   T1HK74_RHOPR            Unreviewed;       551 AA.
AC   T1HK74;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
DE   Flags: Fragment;
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC004447-PA, ECO:0000313|Proteomes:UP000015103};
RN   [1] {ECO:0000313|Proteomes:UP000015103}
RP   NUCLEOTIDE SEQUENCE.
RA   Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:RPRC004447-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2015) 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   EMBL; ACPB03011909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1HK74; -.
DR   STRING; 13249.T1HK74; -.
DR   EnsemblMetazoa; RPRC004447-RA; RPRC004447-PA; RPRC004447.
DR   VEuPathDB; VectorBase:RPRC004447; -.
DR   eggNOG; KOG0506; Eukaryota.
DR   HOGENOM; CLU_016439_1_0_1; -.
DR   InParanoid; T1HK74; -.
DR   OMA; RWGNRPI; -.
DR   OrthoDB; 537490at2759; -.
DR   Proteomes; UP000015103; Unassembled WGS sequence.
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; 1.
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; IPR015868; Glutaminase.
DR   InterPro; IPR041541; Glutaminase_EF-hand.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
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   SMART; SM00248; ANK; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          6..96
FT                   /note="Glutaminase EF-hand"
FT                   /evidence="ECO:0000259|Pfam:PF17959"
SQ   SEQUENCE   551 AA;  61744 MW;  9EAD3441EE61CB32 CRC64;
     DNTPSTEDML FDMFKTEDSD LLSVGKFLAA LRQTGLRKND PRLAGLMENL RIVHRESGRE
     GGSPETQKLN REAFKRVISA NLILISRAFR HHFIIPDFSD FSKHIEEFYW KCKTNTEGKV
     TSYIPQLARA NPDHWGVSVC TIDGQRFSIG DVTIPFTLQS TSKPLTYGIA LDQLGQEVVH
     QYVGQEPSGR NFNELVLDHN KKPHNPMINA GAILVCSLLK TLIHPDMTLA EKFDFTMDYF
     KRLAGGEYLG FNNAIFLSER EAADRNYALG FFMREHKCFP DKTNLKEAMD FYFQCCSMEA
     NCESMSVMAA TLANGGICPV TEEKVLKPDS IRDVLSLMHS CGMYDYSGQF AFKVGLPAKS
     GVSGGMLIVI PNVMGISTWS PPLDPLGNSC RGVQFCQELV SVFNFHRYDN LKHATNKKDP
     RRHKYETKGL SIVNLLFSAA SGDVATLRRH RLSGLDMSLS DYDGRTALHL AAAEGHLDCV
     SFLLEQCNVP YDIQDRWGNS PLDEAKTFGR VQVVQFINDW SQKHAAQPAK SEKIEGTVEK
     PKISEDNSPL P
//
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