ID A0A2A4JKC7_HELVI Unreviewed; 265 AA.
AC A0A2A4JKC7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=glutaminyl-peptide cyclotransferase {ECO:0000256|ARBA:ARBA00012012};
DE EC=2.3.2.5 {ECO:0000256|ARBA:ARBA00012012};
GN ORFNames=B5V51_1074 {ECO:0000313|EMBL:PCG72178.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG72178.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG72178.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG72178.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG72178.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glutaminyl-peptide cyclotransferase family.
CC {ECO:0000256|ARBA:ARBA00006014}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCG72178.1}.
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DR EMBL; NWSH01001193; PCG72178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4JKC7; -.
DR STRING; 7102.A0A2A4JKC7; -.
DR Proteomes; UP000218220; Unassembled WGS sequence.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR040234; QC/QCL.
DR PANTHER; PTHR12283; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR PANTHER; PTHR12283:SF6; 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:UP000218220};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..265
FT /note="glutaminyl-peptide cyclotransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013308826"
FT DOMAIN 140..255
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 265 AA; 30757 MW; AD6EC7E45E14F40A CRC64;
MFKSLLNLVV VILCFASVNT KKRLKFYEEK NIHEAQELTD QNVSDLAALS DMTHFRKVLD
EILVPRVVGT PNHDKVGNFI SQQMRDLGWD VTENVFSDTT PIFGTLNFKN IIAKLNPNAE
RFLVLACHYD SKYMREHVFD VLVLLDLLGA PDPVFFSYFQ STEKWYVRLA VAEQRLAELN
QFEAYSRGKV EQTYFRLRSS GAVIEDDHIP FMRRNVDILH VIPSPFPSVW HTPEDNMAAL
DFKTIENLNK IFRVFVAEYL HIQPK
//
