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Database: UniProt
Entry: A0A1P8RZ49_9FLAO
LinkDB: A0A1P8RZ49_9FLAO
Original site: A0A1P8RZ49_9FLAO 
ID   A0A1P8RZ49_9FLAO        Unreviewed;       473 AA.
AC   A0A1P8RZ49;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=BWZ20_13010 {ECO:0000313|EMBL:APY09166.1};
OS   Winogradskyella sp. J14-2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1936080 {ECO:0000313|EMBL:APY09166.1, ECO:0000313|Proteomes:UP000187462};
RN   [1] {ECO:0000313|EMBL:APY09166.1, ECO:0000313|Proteomes:UP000187462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J14-2 {ECO:0000313|EMBL:APY09166.1,
RC   ECO:0000313|Proteomes:UP000187462};
RA   Kim J.H., Chi W.-J.;
RT   "Genome sequence of Winogradskyella sp. J14-2 isolated from seawater in
RT   Jeju island.";
RL   Submitted (JAN-2017) 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; CP019388; APY09166.1; -; Genomic_DNA.
DR   RefSeq; WP_076620564.1; NZ_CP019388.1.
DR   AlphaFoldDB; A0A1P8RZ49; -.
DR   STRING; 1936080.BWZ20_13010; -.
DR   KEGG; wij:BWZ20_13010; -.
DR   OrthoDB; 9769665at2; -.
DR   Proteomes; UP000187462; Chromosome.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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; IPR046450; PA_dom_sf.
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; SSF52025; PA domain; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187462};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..473
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012049249"
FT   DOMAIN          265..450
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   473 AA;  52441 MW;  AE279438B96C699C CRC64;
     MNRILNIQLK IIVLGIMLSS FCVSAQSDES VLKAVYKTSL TNGKSYEWLD YLSNTIGGRL
     SGSTNAELAV QYTKQELEKL GLDKVWLQPV MVPKWVRGEK EMAYFVSNNE FNKVNICALG
     GSIATPENGL KAKVIEISSF KDLESLGEDK IKGKIVFINR ALQPDLINTF EAYGGCSVER
     YRGAAEASKY GAVGTIVRSL SSRQDDYPHT GSMSYGDLPI EKRIPSAAIS TNDAVKLSQA
     LKANRDLEFF FEMSCQQFDD VESYNVIGEI TGSEFPNEYI VVGGHLDSWD LGDGAHDDGA
     GVVQSMDVLR LLKESGIKPR RSIRVVLFMN EENGLRGGRK YAEVAKAKGE KHVFALESDA
     GGFTPRGFSF DGSDLMLQKI DTWRPLFKPY LIHYFEKGYS GADISPLKNN GILLAGLRPD
     SQRYFDHHHA ANDTFEHVNK RELELGAATM TALIYLVDKY GVETSLKAND IKD
//
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