ID M4NJX5_9GAMM Unreviewed; 477 AA.
AC M4NJX5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
DE Flags: Precursor;
GN ORFNames=R2APBS1_3328 {ECO:0000313|EMBL:AGG90392.1};
OS Rhodanobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG90392.1, ECO:0000313|Proteomes:UP000011859};
RN [1] {ECO:0000313|EMBL:AGG90392.1, ECO:0000313|Proteomes:UP000011859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2APBS1 {ECO:0000313|EMBL:AGG90392.1,
RC ECO:0000313|Proteomes:UP000011859};
RG US DOE Joint Genome Institute;
RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Peters L., Pitluck S., Woyke T., Prakash O., Elkins J., Brown S.,
RA Palumbo A., Hemme C., Zhou J., Watson D., Jardine P., Kostka J., Green S.;
RT "Complete genome of Rhodanobacter sp. 2APBS1.";
RL Submitted (APR-2012) 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; CP003470; AGG90392.1; -; Genomic_DNA.
DR RefSeq; WP_015448744.1; NZ_CP088918.1.
DR AlphaFoldDB; M4NJX5; -.
DR STRING; 666685.R2APBS1_3328; -.
DR KEGG; rhd:R2APBS1_3328; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_033697_1_0_6; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000011859; Chromosome.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:AGG90392.1};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000313|EMBL:AGG90392.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000313|EMBL:AGG90392.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..477
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004056256"
FT DOMAIN 262..451
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 477 AA; 50048 MW; 2BF236A583362A52 CRC64;
MRRLPLTLLA AGLLASGIAS AVTTTIPTTA VKTAEQLRDR ALHDDTAYQV TASLTTEVGA
RLAGSEADRR AVDWAVAKFK ELGYDKVYTE PVTYPLWVRR SERAAIVAPF PQPLALTALG
YSPATPKGGL RAEVVRFDSL DALKAADPAA IKGKIVYVDY HMERAKDGHG YGMGSAVRVA
GPVLAAEKGA AGYLLRSAGT DAHERAPHTG VTGFRDPAKA IPAAALSNPD ADQLTRVLAY
GKPVTLKLDL DCGIVGEYTG ANVIGEITGR RHPEQVVAIG GHLDSWDLGT GAIDDGAGVA
IAMAAGKLIH DLPQRPDRTI RVIAFANEEM GLWGGRAYAE KHAGEVAKFQ LGTESDFGAG
PIWRMSASVK PEARDAIGQI AKVLQPLGVA YDAGRPGGGG SDLSQMHAKG MAALSLTQDG
TKYFDWHHTP NDTLDKIDPA ELAQNVAVYA AFSYMAAQAN GDFGSAPGAF AKDGAGE
//
