ID   A0A1I5F0Y6_9SPHN        Unreviewed;       467 AA.
AC   A0A1I5F0Y6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=SAMN05428984_2490 {ECO:0000313|EMBL:SFO17266.1};
OS   Sphingomonas sp. OK281.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1881067 {ECO:0000313|EMBL:SFO17266.1, ECO:0000313|Proteomes:UP000199378};
RN   [1] {ECO:0000313|EMBL:SFO17266.1, ECO:0000313|Proteomes:UP000199378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK281 {ECO:0000313|EMBL:SFO17266.1,
RC   ECO:0000313|Proteomes:UP000199378};
RA   de Groot N.N.;
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; FOVZ01000003; SFO17266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5F0Y6; -.
DR   STRING; 1881067.SAMN05428984_2490; -.
DR   OrthoDB; 9769665at2; -.
DR   Proteomes; UP000199378; 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:SFO17266.1};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SFO17266.1};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SFO17266.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..467
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011487775"
FT   DOMAIN          262..447
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   467 AA;  48398 MW;  FBE2CB38CAFB6916 CRC64;
     MMKRTLLAAL AASALTSPLS AQRTAAPATA VDAKVAALRD KALTDDTAYK IVEGITTEVG
     PRMTGTEAAP RARAWSVAKL KALGFKNVRI EPYQLPVWSR GTESGELVAP YAQTLHLVGL
     GNSGATPPGG LTLPIVYFAT YNDLALAADG SLKGKIAFVS NAMQPTQDGS SYGSQGTARF
     VGPNVAAKKG AAAIVIRSIG TDHGRGPHAG NTNFEAGVTP IPAAALSVAD AEHVERLVKL
     GKPVTLKLVL QDKQAGMQES GNVVAEVPGT DPKAGIVLVG GHLDSWDLGT GAIDDGAGIA
     ITAAAAKIVM DGGQRPRRTI RVVWFGDEES GGFGGLAYAK AHAGERHATA AESDFGADRV
     WRFESSLPAA AKPIEDRLAV ALAPLGIIRG NDAPHGGTDV GPTIATGVAG IDLNQSGLRY
     FDYHHTPEDT LDRIDPEQLR QNVAAWTAMI ATVANAPEEI GPIVLQK
//