ID A0A0C1CWL7_9FLAO Unreviewed; 463 AA.
AC A0A0C1CWL7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=OA85_10915 {ECO:0000313|EMBL:KIA85765.1};
OS Flavobacterium sp. AED.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA85765.1, ECO:0000313|Proteomes:UP000031403};
RN [1] {ECO:0000313|EMBL:KIA85765.1, ECO:0000313|Proteomes:UP000031403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AED {ECO:0000313|EMBL:KIA85765.1,
RC ECO:0000313|Proteomes:UP000031403};
RA Gale A.N., Newman J.D.;
RT "Flavobacterium sp. AED Genome.";
RL Submitted (OCT-2014) 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}.
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:KIA85765.1}.
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DR EMBL; JSYM01000002; KIA85765.1; -; Genomic_DNA.
DR RefSeq; WP_039109780.1; NZ_JSYM01000002.1.
DR AlphaFoldDB; A0A0C1CWL7; -.
DR STRING; 1423323.OA85_10915; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000031403; 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..463
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002129505"
FT DOMAIN 259..446
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 463 AA; 51042 MW; 1BAB7A8E7B46641C CRC64;
MKKSILSVIL FLSGIVLFAQ TKDEQTLKEI YKSSLTNSKC YSWLDYLSNK IGSRLSGSAS
AEKAVQYTKA QLETLGLDRV YLQEVMVPKW VRGEKETAYI QDNKTKINVP ICALGGSVAT
SKNGLTAEVI EVHSIKELEA LGNKIKGKIV FFNRPMEDAQ IEAFNAYSGC VDQRYAGAME
ASKFGALGTI VRSMNLRLDD FPHTGAQSYG DISKSQYIPS AAISTNGAEL LSKKLKNNPK
LKFYFKQSCK QMDDVLSYNV IGEIKGSEHP ENIMVVGGHL DSWDLADGSH DDGAGVVQSM
EVVNIFKNLG YKPKNTIRVV LFMNEENGGK GGKKYEELAQ ANNENHIFAL ESDSGGFSPR
GFSLESDDAN FNKILGWKNL FEPYLIHSFV KGHAGSDIGP LTSKTLVKAG LKPDSQRYFD
YHHALNDTFD AVNKRELELG AATMASLMYL IDQNGTQASK EVQ
//
