ID A0A1U7S2Q3_ALLSI Unreviewed; 380 AA.
AC A0A1U7S2Q3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glutaminyl-peptide cyclotransferase {ECO:0000256|ARBA:ARBA00016861};
DE EC=2.3.2.5 {ECO:0000256|ARBA:ARBA00012012};
DE AltName: Full=Glutaminyl cyclase {ECO:0000256|ARBA:ARBA00033159};
DE AltName: Full=Glutaminyl-tRNA cyclotransferase {ECO:0000256|ARBA:ARBA00042699};
GN Name=QPCT {ECO:0000313|RefSeq:XP_006024561.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006024561.1};
RN [1] {ECO:0000313|RefSeq:XP_006024561.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00000001};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glutaminyl-peptide cyclotransferase family.
CC {ECO:0000256|ARBA:ARBA00006014}.
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 RefSeq; XP_006024561.1; XM_006024499.3.
DR AlphaFoldDB; A0A1U7S2Q3; -.
DR STRING; 38654.A0A1U7S2Q3; -.
DR GeneID; 102377565; -.
DR KEGG; asn:102377565; -.
DR CTD; 25797; -.
DR eggNOG; KOG3946; Eukaryota.
DR InParanoid; A0A1U7S2Q3; -.
DR OrthoDB; 3091175at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IEA:UniProtKB-EC.
DR CDD; cd03880; M28_QC_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR037457; M28_QC.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR040234; QC/QCL.
DR PANTHER; PTHR12283; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR PANTHER; PTHR12283:SF5; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 140..371
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 380 AA; 43073 MW; E7F0554453D1800F CRC64;
MTRRNSSGNC RRGMAGGSRG KTQAVATFCQ AWALCLAAVT LSQLVDGREA IKDWTREKYS
HQPNILNSTS IQQIAANTNV SLMWQSDLHP MLIERYSGSP GNYAVRQHIK HRLQRLQAGW
VIEEDTFQRY TPYGYRTFSN IISTLDSTAK RHLVLACHYD SKYFGPQWDG RVFVGATDSA
VPCAMLLELA RALDSQLYTM ENSSTSRPDL SLQLIFFDGE EAFVQWSPFD SLYGSQHLAQ
KMASTPHPPG TTTTSQLQGI DLLVLLDLIG APNPTFPNYF PKTARWFNRL QATERKLHGL
GLLKNHPFER QYFQGNSHQG MIEDDHVPFL IRGVPVLHLI PSPFPSVWHT MEDTEENLDK
TIIDNLNKIL QVFVLEYLNL
//
