ID A0A7S6URH1_9GAMM Unreviewed; 472 AA. AC A0A7S6URH1; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 27-MAR-2024, entry version 10. DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116}; DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328}; GN ORFNames=INQ43_03695 {ECO:0000313|EMBL:QOW25163.1}; OS Lysobacter sp. H23M47. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=2781024 {ECO:0000313|EMBL:QOW25163.1, ECO:0000313|Proteomes:UP000593820}; RN [1] {ECO:0000313|EMBL:QOW25163.1, ECO:0000313|Proteomes:UP000593820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H23M47 {ECO:0000313|EMBL:QOW25163.1, RC ECO:0000313|Proteomes:UP000593820}; RA Bae J.-W., Lee S.-Y.; RT "complete genome sequencing of Lysobacter sp. H23M47."; RL Submitted (OCT-2020) 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; CP063658; QOW25163.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7S6URH1; -. DR Proteomes; UP000593820; Chromosome. 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}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..472 FT /note="Carboxypeptidase Q" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5032918563" FT DOMAIN 261..446 FT /note="Peptidase M28" FT /evidence="ECO:0000259|Pfam:PF04389" SQ SEQUENCE 472 AA; 49128 MW; 2CAC794DB79EE340 CRC64; MRIMPLLLTL AIGSLTGVAV AQDAPQTVIP DAAISAAPSL RQTALDSDLG YRITESLTTE VGPRLAGSEA DARAVAWAKA KFAELGYDKV WTEPVTFPKW ERRSESARVV GANAQPLVLT ALGGSPGGTV EAQVVRFDDL AALEAVKPGS LAGKIAFIDQ KMERSRDGSG YGIGSRVRSR GPSAAIRAGA SAYLMRSAGT DSQRMPHTGI TRFDEGLTPI PSAALSLPDA DQLSRLLALG RPVSVNLSLD CGWNGEATSH NVIGEMTGSS LPDEVVLIGG HLDSWDAGTG AIDDASGVGI TMAAGKLIGD LKQRPARSIR VIAFANEEQG LHGGYAYAKA HADQISNHLI AAESDFGAGR IYGFDTSAPA HAKAAAEQIA RALAPLGIEY MPGEGGPGPD VSPFARDGVA WGNLMQDGTD YFDYHHTPND TFDKIDPEAL AQNVAAYAVF AYLAASAEGD FGSKAKAADA AD //