ID   NTAQ1_CAEBR             Reviewed;         185 AA.
AC   A8Y183;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 60.
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;
GN   ORFNames=CBG21918;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAP38644.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; HE600952; CAP38644.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002629881.1; XM_002629835.1.
DR   AlphaFoldDB; A8Y183; -.
DR   SMR; A8Y183; -.
DR   STRING; 6238.CBG21918; -.
DR   GeneID; 8573057; -.
DR   KEGG; cbr:CBG_21918; -.
DR   CTD; 8573057; -.
DR   WormBase; CBG21918; CBP39913; WBGene00040587; -.
DR   eggNOG; KOG3261; Eukaryota.
DR   HOGENOM; CLU_091083_2_0_1; -.
DR   InParanoid; A8Y183; -.
DR   OrthoDB; 1337506at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
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..185
FT                   /note="Protein N-terminal glutamine amidohydrolase"
FT                   /id="PRO_0000381820"
FT   ACT_SITE        14
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  22107 MW;  D7D60FA2286E4EBF CRC64;
     MLSAEEAPYQ SCYCEENVYK LLEKLKPNLD DFFAVLISND IKMIPLWKQK AERDPDVLWD
     YHVITISKNS DGSAKVYDFD SWIDWGVDFQ TYWNQTMNED EMKQFREKYR RKFRIIPARI
     YLSLLSSDRS HMLNPDGTYM KPPPEWPLIQ NSTNSNLMNL IDMKLEFPET MVMDETEIRR
     FFSDA