ID   QPCT_BOTJA              Reviewed;         368 AA.
AC   Q9YIB5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Glutaminyl-peptide cyclotransferase;
DE            EC=2.3.2.5;
DE   AltName: Full=Glutaminyl cyclase;
DE            Short=QC;
DE   AltName: Full=Glutaminyl-tRNA cyclotransferase;
DE   Flags: Precursor;
GN   Name=QPCT;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Murayama N., Ohnuma M.;
RT   "Bothrops jararaca mRNA for glutaminyl cyclase.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides.
CC       Has a bias against acidic and tryptophan residues adjacent to the N-
CC       terminal glutaminyl residue and a lack of importance of chain length
CC       after the second residue. Also catalyzes N-terminal pyroglutamate
CC       formation (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-glutaminyl-[peptide] = N-terminal 5-oxo-L-prolyl-
CC         [peptide] + NH4(+); Xref=Rhea:RHEA:23652, Rhea:RHEA-COMP:11736,
CC         Rhea:RHEA-COMP:11846, ChEBI:CHEBI:28938, ChEBI:CHEBI:64722,
CC         ChEBI:CHEBI:87215; EC=2.3.2.5;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the glutaminyl-peptide cyclotransferase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is unclear whether this protein requires a metal cofactor
CC       for catalysis. It was originally proposed to be a Zn(2+)-dependent
CC       metalloenzyme based on structural similarities to bacterial
CC       aminopeptidases and the observation that it can bind Zn(2+) ions,
CC       typically in a 1:1 stoichiometry (By similarity). However, a recent
CC       study suggests a Zn(2+)-independent catalytic mechanism (By
CC       similarity). {ECO:0000250|UniProtKB:B7QK46,
CC       ECO:0000250|UniProtKB:Q16769}.
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DR   EMBL; AB014769; BAA34290.1; -; mRNA.
DR   AlphaFoldDB; Q9YIB5; -.
DR   SMR; Q9YIB5; -.
DR   MEROPS; M28.974; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0017186; P:peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase; ISS:UniProtKB.
DR   CDD; cd03880; M28_QC_like; 1.
DR   InterPro; IPR037457; M28_QC.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR040234; QC/QCL.
DR   PANTHER; PTHR12283; PTHR12283; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Disulfide bond; Glycoprotein; Metal-binding; Secreted;
KW   Signal; Transferase; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..368
FT                   /note="Glutaminyl-peptide cyclotransferase"
FT                   /id="PRO_0000407858"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   ACT_SITE        254
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..169
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
SQ   SEQUENCE   368 AA;  42204 MW;  1970B0B45C413D10 CRC64;
     MARERRDSKA ATFFCLAWAL CLALPGYPQH VSGREDRADW TQEKYSHRPT ILNATCILQV
     TSQTNVSRMW QNDLHPILIE RYPGSPGSYA VRQHIKHRLQ GLQAGWLVEE DTFQSHTPYG
     YRTFSNIIST LNPLAKRHLV IACHYDSKYF PPQLDGKVFV GATDSAVPCA MMLELARSLD
     RPLSFLKQSS LPPKADLSLK LIFFDGEEAF VRWSPSDSLY GSRSLAQKMA STPHPPGARN
     TYQIRGIDLF VLLDLIGARN PVFPVYFLNT ARWFGRLEAI ERNLNDLGLL NNYSSERQYF
     RSNLRRHPVE DDHIPFLRRG VPILHLIPSP FPRVWHTMED NEENLDKPTI DNLSKILQVF
     VLEYLNLG