ID   A0A239CUM5_9BACT        Unreviewed;       486 AA.
AC   A0A239CUM5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=SAMN05421770_10186 {ECO:0000313|EMBL:SNS23053.1};
OS   Granulicella rosea.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=474952 {ECO:0000313|EMBL:SNS23053.1, ECO:0000313|Proteomes:UP000198356};
RN   [1] {ECO:0000313|EMBL:SNS23053.1, ECO:0000313|Proteomes:UP000198356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18704 {ECO:0000313|EMBL:SNS23053.1,
RC   ECO:0000313|Proteomes:UP000198356};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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; FZOU01000001; SNS23053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239CUM5; -.
DR   OrthoDB; 9762302at2; -.
DR   Proteomes; UP000198356; 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:UP000198356};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..486
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013031710"
FT   DOMAIN          255..459
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   486 AA;  50831 MW;  0EAFD6F0FB831CB0 CRC64;
     MHRFRAALLS ASALLSTAAL AQQPSLAVTY KSAADKLIAD SLADTEGYAN LAYLCDHIGK
     RITGGEPLGR AVAWSADLMR RDGLANVTVQ PVMVPHWVRG HESASIVEPV AKPMHMLGLG
     MSVATPVGGI TAPVVVVKDF DELKKLGRAG VAGKIVLYNV AYKGYGQTVM YRVAGPSQAA
     ALGAVATLVR SITPLAVQLP HTGVTSYDEK QPKIPAAAIS LEDALMLERL AAEGKPPVVH
     LDMEAHMEAE VESANVFGEI VGSEHPEQVV TLGGHIDSWD VGQGAQDDGS GIMATLEAVN
     VIKRSGLKPK RTIRIVFWVS EENGGVGGQV YLKKLTGKLE DHVAVIEMDG GAEQPVGYGY
     GASFPGLRAV AGGAALAASG GLSAGEQRSL ALLQQIGTLL KPVGADTMRA GGGGSDIEPM
     MGAGVPGLGE MTTGAHYFDW HHTEADTLDK VDPQDFRKNI ASLSVMTYIL ADMPERLAGH
     KGAGEE
//