QPCT_DICDI
ID QPCT_DICDI Reviewed; 360 AA.
AC Q54B14;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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; ORFNames=DDB_G0293986;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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; AAFI02000224; EAL60492.1; -; Genomic_DNA.
DR RefSeq; XP_628902.1; XM_628900.1.
DR AlphaFoldDB; Q54B14; -.
DR SMR; Q54B14; -.
DR STRING; 44689.DDB0266352; -.
DR PaxDb; Q54B14; -.
DR EnsemblProtists; EAL60492; EAL60492; DDB_G0293986.
DR GeneID; 8629518; -.
DR KEGG; ddi:DDB_G0293986; -.
DR dictyBase; DDB_G0293986; qpct.
DR eggNOG; KOG3946; Eukaryota.
DR HOGENOM; CLU_045003_1_0_1; -.
DR InParanoid; Q54B14; -.
DR OMA; AFTAEWM; -.
DR PhylomeDB; Q54B14; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54B14; -.
DR Proteomes; UP000002195; Chromosome 6.
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 3: Inferred from homology;
KW Acyltransferase; Glycoprotein; Metal-binding; Reference proteome; Secreted;
KW Signal; Transferase; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..360
FT /note="Glutaminyl-peptide cyclotransferase"
FT /id="PRO_0000327730"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT ACT_SITE 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 360 AA; 42046 MW; B2E05CAADF87D0A9 CRC64;
MKYLKILIIV TIFFFLLINV INCIDRKEIV QKEVKIKFKN LKSTLIKKYS ESNMEKIQKH
LKHILVERVA DTPNHKKVRE YIISQFDQLY WDIELDSFKD NTPFGEKTFT NIIVTSKFVN
DDDEDDIDTK ESNGNISSEP PKTLVLSAHY DSKYFKEFKF FGATDSAVPC SMLIDLAISL
QSEIKKSKKK LMIIFFDGEE AFKEWSDTDS LYGSRHLANL LLDKKVITKD NEDLPISSSF
YNTVEAFILL DLLGTPNPRF YMFNKKTESL FKKLSDIEDK LSLKRFISPK ANKYFQNHFI
GSDIQDDHIP FLNYVPTLHI IPYPFPNVWH TEKDDESCLD KNTIEDLSKI FKIFVGSYLI
