NTAQ1_DROWI
ID NTAQ1_DROWI Reviewed; 205 AA.
AC B4MQL4;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=GK21898;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH963849; EDW74403.1; -; Genomic_DNA.
DR RefSeq; XP_002063417.1; XM_002063381.2.
DR AlphaFoldDB; B4MQL4; -.
DR SMR; B4MQL4; -.
DR STRING; 7260.FBpp0251041; -.
DR EnsemblMetazoa; FBtr0252549; FBpp0251041; FBgn0223883.
DR GeneID; 6640630; -.
DR KEGG; dwi:6640630; -.
DR eggNOG; KOG3261; Eukaryota.
DR HOGENOM; CLU_091083_1_0_1; -.
DR InParanoid; B4MQL4; -.
DR OMA; GWGTVYS; -.
DR OrthoDB; 1337506at2759; -.
DR PhylomeDB; B4MQL4; -.
DR ChiTaRS; Zasp52; fly.
DR Proteomes; UP000007798; 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_0000381832"
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; 23971 MW; D0312749ED37F47F CRC64;
MTTDFLFPKI ADCSYVSCYC EENVWKLCEQ VKRTRPEELA KCYAVFVSNE GRTVPLWRQK
AGRGDDQVVI WDYHVFFMHN PLPNRCLVFD LDTTLPFPTY FHKYVTETFR SDLALRPEHH
RFFRVIPADT YLIEFSSDRR HMRRPDGSWI KPPPSYPPIL SNTNTHCLGD FICMSAGKGP
GAVYSLSEFV HNFYKQPNMV AQNNK