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
//