ID   A0A1W2CNZ8_9SPHN        Unreviewed;       442 AA.
AC   A0A1W2CNZ8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=SAMN06272759_10931 {ECO:0000313|EMBL:SMC86348.1};
OS   Novosphingobium sp. B1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1938756 {ECO:0000313|EMBL:SMC86348.1, ECO:0000313|Proteomes:UP000192500};
RN   [1] {ECO:0000313|Proteomes:UP000192500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|Proteomes:UP000192500};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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; FWXL01000009; SMC86348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2CNZ8; -.
DR   STRING; 1938756.SAMN06272759_10931; -.
DR   OrthoDB; 9769665at2; -.
DR   Proteomes; UP000192500; 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: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..442
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012619329"
FT   DOMAIN          243..424
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   442 AA;  46129 MW;  705E858752904E62 CRC64;
     MRNHARALAL LATLSASTAY AQDPKGDVAW DVLAGLTSEV GPRLPGSEAE ARARVWAEAR
     LKALGFSKVA VEPFRIRGYV RGRDEASILA PIPFRLAVTA LGYSGTTPEQ GIEGEVAYFP
     TLDALKAAPA GSLNGKIAFI DHAMKRAQDG SGYGPYGQVR RVGPAIASGK GAIGVVIRSI
     GTDSHRNPHT GGTTFADGVK PIPAGAVSNP DADLIAHIAR SGKPIRLSLT LTGKTTDNLP
     SGNVIGELPG RDPSLPPILL GCHLDSWDLG TGAIDDAAGC AIITAAALKA QEGGAPLRTI
     RVLWAGSEEL GGFGGKAYAE KHNERHALAM ESDFGAARVW RVQFNMADKA LTDRIAAALS
     PMGIVRGAGL ADGGTDVEPV IEKQKLAVVD LNQDGTHYFD LHHTPDDTLD KVDPAELAQN
     VTAWTEVLKI VANEPGAIAA KP
//