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Database: UniProt
Entry: A0A085Z3D9_9FLAO
LinkDB: A0A085Z3D9_9FLAO
Original site: A0A085Z3D9_9FLAO 
ID   A0A085Z3D9_9FLAO        Unreviewed;       452 AA.
AC   A0A085Z3D9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=IX38_19075 {ECO:0000313|EMBL:KFE98952.1};
OS   Chryseobacterium luteum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=421531 {ECO:0000313|EMBL:KFE98952.1, ECO:0000313|Proteomes:UP000028703};
RN   [1] {ECO:0000313|EMBL:KFE98952.1, ECO:0000313|Proteomes:UP000028703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18605 {ECO:0000313|EMBL:KFE98952.1,
RC   ECO:0000313|Proteomes:UP000028703};
RA   Stropko S.J., Pipes S.E., Newman J.D.;
RT   "Genome of Chryseobacterium luteum DSM 18605.";
RL   Submitted (JUL-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:KFE98952.1}.
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DR   EMBL; JPRO01000021; KFE98952.1; -; Genomic_DNA.
DR   RefSeq; WP_034707315.1; NZ_JPRO01000021.1.
DR   AlphaFoldDB; A0A085Z3D9; -.
DR   STRING; 421531.IX38_19075; -.
DR   eggNOG; COG2234; Bacteria.
DR   OrthoDB; 9769665at2; -.
DR   Proteomes; UP000028703; 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}.
FT   DOMAIN          258..434
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   452 AA;  50371 MW;  0C070768DBD45AC4 CRC64;
     MKKPVTFSLL MVSMAVFGQS GEDSLQFSRI STEILNNGKS YNELKDLTKN IGNRLSGTEA
     YEKSVKWAEQ KLREAGADKV WLQEVMIPVW VRGKESLQIK TADSQWRKLK MLSLGNSEGT
     GGKDISGEII MVRSLEEYDR LPADQVKDKI VFFNYPFNQS NVQTFLSYRE AGAYRRSAAN
     LTARKGGKFA VVRSLSSAFD DVPHTGNMRY DDNISKVPAV TIGNTTADEL ETLLKTKKIT
     AKLNSNCGMK GGKLSHSVIG EITGKKDQSV IVVGGHLDSW DVGEGAHDDG SGIVQSIEVL
     RTFKKLGIKN NHTIRAVCFA NEENGTKGGI QYGKTAKEKN EKHLFAIESD AGGFSPRGIS
     LEMDDKSRKQ IQSWASLFLP YGVYNFEEKY SGSDIAPLHE MAVPTAELVP DPQRYFDIHH
     TEEDTFEKVN RRELLLGATV MTQLIYMIDK NW
//
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