ID   NTAQ1_DROSE             Reviewed;         205 AA.
AC   B4HSF8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
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=GM21641;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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; CH480816; EDW48036.1; -; Genomic_DNA.
DR   RefSeq; XP_002034023.1; XM_002033987.1.
DR   AlphaFoldDB; B4HSF8; -.
DR   SMR; B4HSF8; -.
DR   STRING; 7238.B4HSF8; -.
DR   EnsemblMetazoa; FBtr0204626; FBpp0203118; FBgn0176521.
DR   GeneID; 6609334; -.
DR   KEGG; dse:6609334; -.
DR   HOGENOM; CLU_091083_1_0_1; -.
DR   OMA; GWGTVYS; -.
DR   PhylomeDB; B4HSF8; -.
DR   ChiTaRS; Zasp52; fly.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
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_0000381829"
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;  23974 MW;  178121459C9B4449 CRC64;
     MTTDFLFPKI ADCSYVSCYC EENVWKLCEQ VKRTRPEELS KCYAVFVSNE GRTVPLWRQK
     AGRGDDQVVI WDYHVFFIHN PLLNRCLVFD LDTTLPFPTY FHKYVTETFR SDLALRPEHH
     RFFRVIPADT YLIEFSSDRR HMRRPDGSWI KPPPSYPPIL SNSNMHCLGD FICMSAGKGP
     GAVYSLSEFV QNFYKSPHVM AQNNK