ID A0A2J7QED5_9NEOP Unreviewed; 379 AA.
AC A0A2J7QED5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=glutaminyl-peptide cyclotransferase {ECO:0000256|ARBA:ARBA00012012};
DE EC=2.3.2.5 {ECO:0000256|ARBA:ARBA00012012};
GN Name=QPCT_1 {ECO:0000313|EMBL:PNF26931.1};
GN ORFNames=B7P43_G14811 {ECO:0000313|EMBL:PNF26931.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF26931.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF26931.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF26931.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-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:PNF26931.1}.
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DR EMBL; NEVH01015316; PNF26931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7QED5; -.
DR STRING; 105785.A0A2J7QED5; -.
DR InParanoid; A0A2J7QED5; -.
DR OrthoDB; 3091175at2759; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
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: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:UP000235965};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PNF26931.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..379
FT /note="glutaminyl-peptide cyclotransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014471308"
FT DOMAIN 112..341
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 379 AA; 43076 MW; 7F875F00D2A7C235 CRC64;
MMFKSAVLLL LTILSGIKEE EASVATRLAN EKNSHAPNLL SDEQIVKVAG LSNVNHFEYV
LDTILIPRVV GTANHEFVKQ FIIKTMQELD WRVESDPFEE NTPIFGRLQF ENVVATLNPN
ARRYLVLACH YDSKYYRENN FVGATDSAVP CAMMINLARV LAEPLKRTLA QNDVSLKFVF
FDGEEAFQQW GPTDSIYGAR HLAAKWEQSA YPKDNADGTN QLHRIDILVL LDLLGAPDPV
FYSYFKETEN WYRRMMAAER SLARLGQLVQ YSVGKPDQYY FQQMSRRGGI EDDHIPFMIR
GVPILHLIPV PFPSAWHTED DNRNAVDIAT VENLNKILRL FVAEYLHLQI PIVTMGASSS
PLLFLLPLLT PSRVLLAYA
//
