ID   A0A1I5NWX9_9SPHN        Unreviewed;       449 AA.
AC   A0A1I5NWX9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=SAMN04488060_2126 {ECO:0000313|EMBL:SFP25826.1};
OS   Qipengyuania nanhaisediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Qipengyuania.
OX   NCBI_TaxID=604088 {ECO:0000313|EMBL:SFP25826.1, ECO:0000313|Proteomes:UP000199331};
RN   [1] {ECO:0000313|Proteomes:UP000199331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7715 {ECO:0000313|Proteomes:UP000199331};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOWZ01000003; SFP25826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5NWX9; -.
DR   STRING; 604088.SAMN04488060_2126; -.
DR   OrthoDB; 9769665at2; -.
DR   Proteomes; UP000199331; 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   ECO:0000313|EMBL:SFP25826.1};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SFP25826.1};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SFP25826.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..449
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011785409"
FT   DOMAIN          246..432
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   449 AA;  47611 MW;  5357552E03014FE3 CRC64;
     MKKQLLALAA LILATPAHAD RADEALAGDT IAWDFVEGIT TEVGPRMPGT DAEARGRVWA
     MDWLRRNGFS NVADEPFEME TWVRGQEMAW VVAPATQPMA ITALSTTSST GSEGIEAEVV
     YFPTYADLVA ADAGSLDGKI AFVSHDMRQT QDGSSYGFAG PARWMAPSMA ASKGAVATVI
     RSVGTDSHRV PHTGTTTFTE GIQPIPAGAL SNPDADNLER LFARGGEVRM KLILTPRDLG
     MTKSGNVVGE IVGSDPSLEP VLLACHLDSW DLGTGAIDDG AGCGIIAAAA KHVAAQGQPL
     RTVRVLFAGA EETGLWGSAA YAEAHSDEPV YVGLESDFGA DRIWRIETNF TASDPDLYRE
     LAGAVARFGV APTRIVATGG ADLNLVREQG GALIDLQQDG TRYFDLHHTA DDTLDKIDPA
     QLRQNVAVWT AVVGILANRS APIVRDSEE
//