ID   NTAQ1_ANOGA             Reviewed;         211 AA.
AC   Q7Q968;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 3.
DT   03-AUG-2022, entry version 98.
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=AGAP004865;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
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; AAAB01008905; EAA09695.3; -; Genomic_DNA.
DR   RefSeq; XP_314323.3; XM_314323.3.
DR   AlphaFoldDB; Q7Q968; -.
DR   SMR; Q7Q968; -.
DR   STRING; 7165.AGAP004865-PA; -.
DR   PaxDb; Q7Q968; -.
DR   GeneID; 1275093; -.
DR   KEGG; aga:AgaP_AGAP004865; -.
DR   CTD; 1275093; -.
DR   VEuPathDB; VectorBase:AGAP004865; -.
DR   eggNOG; KOG3261; Eukaryota.
DR   HOGENOM; CLU_091083_1_0_1; -.
DR   InParanoid; Q7Q968; -.
DR   OMA; GWGTVYS; -.
DR   OrthoDB; 1337506at2759; -.
DR   PhylomeDB; Q7Q968; -.
DR   Proteomes; UP000007062; Chromosome 2L.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:InterPro.
DR   GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IBA:GO_Central.
DR   GO; GO:0036211; P:protein modification process; IBA:GO_Central.
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..211
FT                   /note="Protein N-terminal glutamine amidohydrolase"
FT                   /id="PRO_0000381822"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   211 AA;  24783 MW;  7B61889EAC811B1F CRC64;
     MSTNDANFML FSNINDCSYV SCYCEENVWK LCEQVKKTYP SELPKCYAVF VSNERRTVPL
     WRQKAGRGDE KLVIWDYHVF FMHNPSPNRC LVFDLDTTLP FPTYFHKYVT ETFRSDYALT
     PEHHRFFRVI PAEKYLAEFS SDRRHMRRPD GSWIKPPPSY PPIQTSASTH SLDDFICMKP
     GKGPGAVYDL LHFVQQFYKP PDRNIGTKTQ N