GenomeNet

Database: UniProt
Entry: F1KQG8_ASCSU
LinkDB: F1KQG8_ASCSU
Original site: F1KQG8_ASCSU 
ID   F1KQG8_ASCSU            Unreviewed;       339 AA.
AC   F1KQG8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY40122.1};
RN   [1] {ECO:0000313|EMBL:ADY40122.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
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   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JI164215; ADY40122.1; -; mRNA.
DR   AlphaFoldDB; F1KQG8; -.
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; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF51; GLUTAMINASE 3-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   REGION          315..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   339 AA;  37443 MW;  C074522653FE7C2D CRC64;
     MREHKCFPAN TSIQDTLDLY FQLCSIETNA DTLAVMAATL ANGGVSPLSE QRVVCNRAVR
     DTLSLMYSCG MYDYSGQFAF TVGLPAKSGV SGDMIIVVPN VMGICIYSPA LDPLGNTVRG
     VKFAEQLVEK FNFHNYDSLV YSETHKIDPR KTVREARHES ISNMMYAARA GDISAIQRYI
     LLGVSIHDRD YDERTVLHIA AAEGNDYVLK FLLDRWKESP DPVDRYGRTP LDDAKEFGRV
     KCVELLEKTL LREGIPISSP TRKKNADTNI ASLNATTLNP KTGSLLTETD HISLDTTTSL
     PTCTNLQSTI GNSSLEHKRS LSSDHKNAPS SESNLPLND
//
DBGET integrated database retrieval system