ID A0A0J7ISW9_9FLAO Unreviewed; 523 AA. AC A0A0J7ISW9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 27-NOV-2024, entry version 30. DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116}; DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328}; GN ORFNames=ACM39_06810 {ECO:0000313|EMBL:KMQ68981.1}; OS Chryseobacterium sp. FH2. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae; OC Chryseobacterium group; Chryseobacterium. OX NCBI_TaxID=1674291 {ECO:0000313|EMBL:KMQ68981.1, ECO:0000313|Proteomes:UP000036315}; RN [1] {ECO:0000313|EMBL:KMQ68981.1, ECO:0000313|Proteomes:UP000036315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FH2 {ECO:0000313|EMBL:KMQ68981.1, RC ECO:0000313|Proteomes:UP000036315}; RA Stropko S.J., Miller J.R., Newman J.D.; 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}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. 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:KMQ68981.1}. 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; LFNE01000003; KMQ68981.1; -; Genomic_DNA. DR RefSeq; WP_048510275.1; NZ_LFNE01000003.1. DR AlphaFoldDB; A0A0J7ISW9; -. DR STRING; 1674291.ACM39_06810; -. DR PATRIC; fig|1674291.3.peg.1424; -. DR OrthoDB; 9769665at2; -. DR Proteomes; UP000036315; 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:ARBA00023049}; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Protease {ECO:0000256|ARBA:ARBA00023049}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..523 FT /note="Carboxypeptidase Q" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5005289020" FT DOMAIN 285..471 FT /note="Peptidase M28" FT /evidence="ECO:0000259|Pfam:PF04389" FT REGION 491..523 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 523 AA; 58428 MW; 570BE4ABD0756B33 CRC64; MKVNRFFLMP AMVLATQFSW AQVTVDPKEK LNPIVQNFVN EVNTNSQLEG MAYELLDEIG PRLVGTPEML ASNEWTAKKL RSWDIEANLQ QFGTWKGWER GITHVDMTYP RIKSLSATQL AWSPATKKAV EAEVIILPKV NSKADFDTWL SSVKGKIVLI AQYQKIGRSD EQIKEFATPE LYEKLKKEKE QASKDFQNYV RNIGLDNSTL PEALEKAGVA GVAISNWTGI MGANRIFGAK TNKIPMIDID VEDYGMLYRM AENGAKPKIK IEIQSKILPD AKTFNTIGMI KGKEKPDEYV ILSAHLDSWD GAQGATDNGT GVLTMLETMR ILKKYYPNNK RTIVVGLWGS EEQGLNGSRG FVADNPEIIK GVQAVFNQDN GTGRVVNISG QGFVNSYDYI GKWLTAVPKN IKDQIKTDFP GMPGGGGSDH ASFVAAGVPG FSLSSLNWGY FGYTWHTTKD TYDKIVFDEV KSNVILTATL AYMASEDPEF TNREKREMPI NDKGEVAKWP EIKQPKRDSK DFK //