ID A0A0H1AQI8_9GAMM Unreviewed; 478 AA.
AC A0A0H1AQI8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=WQ56_07005 {ECO:0000313|EMBL:KLJ00987.1};
OS Luteimonas sp. FCS-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1547516 {ECO:0000313|EMBL:KLJ00987.1, ECO:0000313|Proteomes:UP000035397};
RN [1] {ECO:0000313|EMBL:KLJ00987.1, ECO:0000313|Proteomes:UP000035397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCS-9 {ECO:0000313|EMBL:KLJ00987.1,
RC ECO:0000313|Proteomes:UP000035397};
RA Bala M., Kumar A., Kaur N., Mathan Kumar R., Kaur G., Singh N.K.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Luteimonas oceanisediminis
RT sp. nov., a novel gammaproteobacteria isolated from a marine sediment.";
RL Submitted (APR-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}.
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:KLJ00987.1}.
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DR EMBL; LASZ01000006; KLJ00987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H1AQI8; -.
DR STRING; 1547516.WQ56_07005; -.
DR PATRIC; fig|1547516.3.peg.1474; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000035397; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:KLJ00987.1};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000313|EMBL:KLJ00987.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000313|EMBL:KLJ00987.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035397};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..478
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002591362"
FT DOMAIN 266..455
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 478 AA; 49822 MW; C338FEF9775E8642 CRC64;
MRPAPLLNVL AVALLSGALL VPGAARARDA AAAPVAQASL DAAAQLRERA LQDATAYRLI
ESLTTEIGPR LPGSEADARA VEWAKARFAA LGYDRVWTEP VTFPKWERRS ERAAVLGAHA
QPLVLTALGG SPGGEVSAQI VRFDSLAALE AADPATLRGR IAFVDVPMAR SRDGSGYGAA
GPVRSRGPSI AARKGAAAYL MRSIGTSPHR VANTGITRFD ADVSPIPSAA LSLPDADQLA
RLLRLGPVEV ALALDCGWNG EYTSQNVIAE LTGRERPEEI VLIAGHLDSW DLGTGAVDDA
SGVGITMAAG HLIAQQPQRP RRSVRVVAFA NEEQGLLGAR AYAQAHGGAD AIARHVIGAE
SDFGAGRIYA FNTSAPTGQR ATSDAIAEVL RPLGIDYLQD KGGPGPDISP LAAKGAAWGW
LGQDGTDYFD LHHNADDTFD KVDPDAVAQN TAAYAVFAWL AAESAESFGS APKADTTP
//
