ID Q9U1D6_LEIMA Unreviewed; 241 AA. AC Q9U1D6; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 02-DEC-2020, entry version 49. DE RecName: Full=Protein N-terminal glutamine amidohydrolase {ECO:0000256|ARBA:ARBA00021247, ECO:0000256|RuleBase:RU367082}; DE EC=3.5.1.122 {ECO:0000256|ARBA:ARBA00012718, ECO:0000256|RuleBase:RU367082}; DE AltName: Full=Protein NH2-terminal glutamine deamidase {ECO:0000256|ARBA:ARBA00019330, ECO:0000256|RuleBase:RU367082}; GN Name=L1648.12 {ECO:0000313|EMBL:CAB55374.1}; OS Leishmania major. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania. OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAB55374.1}; RN [1] {ECO:0000313|EMBL:CAB55374.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Friedlin {ECO:0000313|EMBL:CAB55374.1}; RX PubMed=9477341; RA Ivens A.C., Lewis S.M., Bagherzadeh A., Zhang L., Chan H.M., Smith D.F.; RT "A physical map of the Leishmania major Friedlin genome."; RL Genome Res. 8:135-145(1998). RN [2] {ECO:0000313|EMBL:CAB55374.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Friedlin {ECO:0000313|EMBL:CAB55374.1}; RA Murphy L., Harris D., Ivens A.C., Lawson D., Quail M., Rajandream M.A., RA Barrell B.G.; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. 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:0000256|RuleBase:RU367082}. 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:0000256|ARBA:ARBA00001439, CC ECO:0000256|RuleBase:RU367082}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, CC ECO:0000256|RuleBase:RU367082}. CC -!- SIMILARITY: Belongs to the NTAQ1 family. CC {ECO:0000256|ARBA:ARBA00008985, ECO:0000256|RuleBase:RU367082}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL117260; CAB55374.1; -; Genomic_DNA. DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IEA:UniProtKB-UniRule. 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367082}. FT DOMAIN 7..240 FT /note="Nt_Gln_amidase" FT /evidence="ECO:0000259|Pfam:PF09764" SQ SEQUENCE 241 AA; 27674 MW; 08592391B7CB046D CRC64; MAHPLYYAFC YCEENVYKFL EMISAMGDLF DRSCAVFMTS FCCAPCDEAL NEWTSVVPYR PCESSELRKD ITTWDYHVIA LVRATRTGKW YVVDQDSRLS PTWDADLGSL APHCIDLDKY VAQVLFLDTA VTNTVCSELT ELLNRVRYRV IERDDYLSFL RSDRSHMQKE PGVYRTLPPQ WPLINGCSTC VRDEVRRRAE SALSSLPSTL RANNLVCFIN AANTTIPGVI IDRHSFADFF R //