ID   A0A1H7L2X9_9BURK        Unreviewed;       499 AA.
AC   A0A1H7L2X9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=SAMN05216319_0663 {ECO:0000313|EMBL:SEK92627.1};
OS   Duganella sp. CF402.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1855289 {ECO:0000313|EMBL:SEK92627.1, ECO:0000313|Proteomes:UP000198529};
RN   [1] {ECO:0000313|Proteomes:UP000198529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF402 {ECO:0000313|Proteomes:UP000198529};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homodimer. The monomeric form is inactive while the homodimer
CC       is active. {ECO:0000256|ARBA:ARBA00025833}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC       {ECO:0000256|ARBA:ARBA00004555}. Lysosome
CC       {ECO:0000256|ARBA:ARBA00004371}.
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DR   EMBL; FOBG01000001; SEK92627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7L2X9; -.
DR   STRING; 1855289.SAMN05216319_0663; -.
DR   Proteomes; UP000198529; Unassembled WGS sequence.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR039866; CPQ.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12053:SF3; CARBOXYPEPTIDASE Q; 1.
DR   PANTHER; PTHR12053; PROTEASE FAMILY M28 PLASMA GLUTAMATE CARBOXYPEPTIDASE-RELATED; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000256|ARBA:ARBA00022645}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..48
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           49..499
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011474175"
FT   DOMAIN          290..479
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   499 AA;  52720 MW;  AA3E11423A1E7B7C CRC64;
     MDDKIIMIGY RFWLIPLNLY RNRMKSVLQK SLSLTVLATS LLSVGVSAAP NDPATLGQIR
     DNAIQSDWAY ERLADLTDLV GPRLSGSAGA AAAVDQVAAA MRKIGATVTL QPVKVPHWVR
     GAETAELVEY TGRPAGITQK VVLTALGGSG ATPAAGLTAP VIIVRSFDEL KAKGAQVKGS
     IVLFDVAFDQ EMADRGHAGP AYGRGAGFRF AGPKLAADMG AAAALVRSVG GANYRIAHTG
     ATGVVDGARI PAAAVTAEDA MLMSRLSARG PLKMHLTLTP QTLPEADSYN VIADLPGTDK
     ADEVVIVSGH LDSWDLATGA HDDGTGVAGA MAVIDTLKKL NLKPRRTIRV IAWMNEENGT
     RGGKAYFEAN KDKLDKHFAA IESDSGGGRP FGFIGSVTPP MVKYFAPLKT ALEPIGAGIF
     ERHDIAGAAD TGPLERAGVP VFEPLVDSSS YFSYHHTPAD TLDKVSPLEL KRHVAVLTAL
     TWYLANMEEN IGRVPQQPE
//