ID A0A1H6J2G9_9FLAO Unreviewed; 513 AA.
AC A0A1H6J2G9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=SAMN02927937_00180 {ECO:0000313|EMBL:SEH56104.1};
OS Paenimyroides aquimaris.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=1159016 {ECO:0000313|EMBL:SEH56104.1, ECO:0000313|Proteomes:UP000199634};
RN [1] {ECO:0000313|EMBL:SEH56104.1, ECO:0000313|Proteomes:UP000199634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10825 {ECO:0000313|EMBL:SEH56104.1,
RC ECO:0000313|Proteomes:UP000199634};
RA de Groot N.N.;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNXE01000002; SEH56104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6J2G9; -.
DR STRING; 1159016.SAMN02927937_00180; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000199634; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199634};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..513
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011616521"
FT DOMAIN 281..468
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 487..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 58243 MW; 79D5820EDFB7206D CRC64;
MNKKYAFLGL TAFVSVTINA QNFQQNKQAV YNQIINEVET NNQLEHLAFE LLDEIGPRLV
GSPQMEQAHN WVVATYKKWN IKAENIPYGE WKSWQRGTTE ITMTSPRIKS IEGTQLAWNI
NSKKAVEAEV VAMPVFQSKN DFENWARSVK GKIVMISQYQ KSGRPENQWK EHATKEDFDT
YKKEKTDDLT AWNNSIKATE KSLRELVKYL ETKGAAGFVQ SYNTGTMGAN RIFYSFAQTV
PMVDVSLEDY GLLYRLAANG KSPKIKINTQ SKNLGTTKTF NTIATIPGKT KPNEYVMLSA
HLDSWDGAQG ATDNGTGTIL MMEVARLIQK YHPNNDRTIV IGHWGSEEQG LNGSRVYIMD
HPTEVQKIKV LFNQDSGTGR INYIGGQGFV NSYDYLGNWL QSVPEHIRKH IKTDFPGMPQ
SRGTDNASFV AAGIPAFNLN TQNWDYGQYT WHTNRDTYDK IVFEELEKNV ITTTLLTLEA
ANDPNEISNE KRVLPKDTEW PTVKEPKRSA EDY
//
