ID   NTAQ1_DROPS             Reviewed;         205 AA.
AC   Q28WL0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Protein N-terminal glutamine amidohydrolase;
DE            EC=3.5.1.122 {ECO:0000250|UniProtKB:Q80WB5};
DE   AltName: Full=Protein NH2-terminal glutamine deamidase;
DE            Short=N-terminal Gln amidase;
DE            Short=Nt(Q)-amidase;
DE   AltName: Full=Protein tungus;
GN   Name=tun; ORFNames=GA20933;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine
CC       residues to glutamate, an important step in N-end rule pathway of
CC       protein degradation. Conversion of the resulting N-terminal glutamine
CC       to glutamate renders the protein susceptible to arginylation,
CC       polyubiquitination and degradation as specified by the N-end rule. Does
CC       not act on substrates with internal or C-terminal glutamine and does
CC       not act on non-glutamine residues in any position.
CC       {ECO:0000250|UniProtKB:Q80WB5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-terminal L-glutaminyl-[protein] = N-terminal L-
CC         glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:50680, Rhea:RHEA-
CC         COMP:12668, Rhea:RHEA-COMP:12777, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:64721, ChEBI:CHEBI:64722;
CC         EC=3.5.1.122; Evidence={ECO:0000250|UniProtKB:Q80WB5};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96HA8}.
CC   -!- SIMILARITY: Belongs to the NTAQ1 family. {ECO:0000305}.
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DR   EMBL; CM000071; EAL26657.1; -; Genomic_DNA.
DR   RefSeq; XP_001362077.1; XM_001362040.3.
DR   AlphaFoldDB; Q28WL0; -.
DR   SMR; Q28WL0; -.
DR   STRING; 7237.FBpp0275730; -.
DR   EnsemblMetazoa; FBtr0277292; FBpp0275730; FBgn0080922.
DR   GeneID; 117183176; -.
DR   KEGG; dpo:Dpse_GA20933; -.
DR   eggNOG; KOG3261; Eukaryota.
DR   HOGENOM; CLU_091083_1_0_1; -.
DR   InParanoid; Q28WL0; -.
DR   OMA; GWGTVYS; -.
DR   PhylomeDB; Q28WL0; -.
DR   ChiTaRS; Zasp52; fly.
DR   Proteomes; UP000001819; Chromosome 3.
DR   Bgee; FBgn0080922; Expressed in insect adult head and 2 other tissues.
DR   GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:InterPro.
DR   GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IEA:InterPro.
DR   Gene3D; 3.10.620.10; -; 1.
DR   InterPro; IPR037132; N_Gln_amidohydro_ab_roll_sf.
DR   InterPro; IPR039733; NTAQ1.
DR   InterPro; IPR023128; Prot_N_Gln_amidohydro_ab_roll.
DR   PANTHER; PTHR13035; PTHR13035; 1.
DR   Pfam; PF09764; Nt_Gln_amidase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..205
FT                   /note="Protein N-terminal glutamine amidohydrolase"
FT                   /id="PRO_0000381828"
FT   ACT_SITE        20
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   205 AA;  23916 MW;  DCC3632632B71D00 CRC64;
     MTTDFLFPKI ADCSYVSCYC EENVWKLCEQ VKRTRPEELG TCYAVFVSNE GRTVPLWRQK
     AGRGDDQVVI WDYHVFFMHN PSPNRCLVFD LDTTLPFPTY FHKYVTETFR SDLALRPEHH
     RFFRVIPADT YLIEFSSDRR HMRRPDGSWI KPPPSYPPIL SNTNMHCLGD FICMSAGKGP
     GAVYSLSEFV HNFYKSPNMV AQHNK