ID A0A0J1BJX9_9SPHI Unreviewed; 515 AA.
AC A0A0J1BJX9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-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=AB669_11010 {ECO:0000313|EMBL:KLT65593.1};
OS Pedobacter sp. BMA.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT65593.1, ECO:0000313|Proteomes:UP000036014};
RN [1] {ECO:0000313|EMBL:KLT65593.1, ECO:0000313|Proteomes:UP000036014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMA {ECO:0000313|EMBL:KLT65593.1,
RC ECO:0000313|Proteomes:UP000036014};
RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT "Pedobacter sp. BMA.";
RL Submitted (JUN-2015) 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:KLT65593.1}.
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DR EMBL; LECU01000005; KLT65593.1; -; Genomic_DNA.
DR RefSeq; WP_047799355.1; NZ_LECU01000005.1.
DR AlphaFoldDB; A0A0J1BJX9; -.
DR STRING; 1663685.AB669_11010; -.
DR PATRIC; fig|1663685.3.peg.2309; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000036014; 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:UP000036014};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..515
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005248723"
FT DOMAIN 277..463
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 484..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 56504 MW; 99C76D57B6B645EC CRC64;
MNKKLLLPTL LLFTSSIAFA QDSKLIDNIV KEVNENSQLE KLAHELLDVV GPRLVGSPQM
KQANDWAVKK YSDWGISAKN EKWGEWRGWE RGVSHIDLVS PRLRTLEGTQ LAWSPSTNGK
AINAEAIVLP AITDSVSFQR WLPNVKGKLV LISMNQISGR PEKNWEEFAT KDLFEKYKKE
KTEAGKAWSA GMAKTGLTGK NLALAIEGAG AAGIIINNWS QGFGVDKIFG ANTTKIPTLD
LSVEDYGLVY RLATSGNKPM LRIESESKEL GVVPTFNTIA EIKGKQKPKE YVMLSAHFDS
WDGASGATDN GSGTIMMMEA MRILKKFYPN PKRTILVGHW GSEEQGLNGS RAFVEDHPEI
VGNLQALFNQ DNGTGRVVNI GGQGFAKSKD YITRWLAAVP DTIKNQIKTS FPGTPGAGGS
DFASFVAAGA LGYSLSATSW DYGTYTWHTN RDSYDKLVFD EIRSNVILAA IMVYMACEDP
EKTSTEKAAD LPVNERTGKQ ATWPEVKKAT RKGGL
//
