ID A0A3P0XBL8_9BACT Unreviewed; 564 AA.
AC A0A3P0XBL8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=D1Y84_07710 {ECO:0000313|EMBL:RRA50025.1};
OS Acidipila sp. EB88.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidipila.
OX NCBI_TaxID=2305226 {ECO:0000313|EMBL:RRA50025.1, ECO:0000313|Proteomes:UP000279598};
RN [1] {ECO:0000313|EMBL:RRA50025.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA50025.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Pold G., Deangelis K.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRA50025.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA50025.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Horta L.;
RT "Genome sequence of EB88, a novel member of the group I Acidobacteria.";
RL Submitted (DEC-2018) 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:RRA50025.1}.
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DR EMBL; QWEV01000005; RRA50025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P0XBL8; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000279598; 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; 3.40.630.10; Zn peptidases; 2.
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:0000313|EMBL:RRA50025.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Reference proteome {ECO:0000313|Proteomes:UP000279598}.
FT DOMAIN 316..528
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 60354 MW; 4608773025610BEF CRC64;
MGVAQKSVVK PGDGTRQASA AMPEAVDLGM YARIRDEGLN HSRVMEYASA LNDDIGPRLT
GSPGMARANA WTRDTLTAMG CANAHLEDWG EFGMGWEQEA SSLRMVLPAP GMFIAQAAPW
SPSTVGADGK PGPVQGEAVR IHIDTGKNAP SLETQMAEYK GKLRGKVVLL GNTPELGEVD
KALVDRYSDE ELAKLEVVPL GPVSEYAGLD DYFIKVMVER ERLGQMLKDE GVAAVVVPSS
NGSKHGGSGG TIFDDSNSNF SWFSYQRAHA TPLPLLVASI ENFGRVARLL DAKVPVTLAA
DVDAKFTGDH EHGFDTIAEI PGTDPLLKDQ VVMVGGHLDS WASATGATDN GAGSVVAMEV
MRILLALHVQ PRRTIRIGLW SGEEQGIFGS AGYVAQHFGT LTLGGNAKLP DFVREPSGPP
VLKPEQAKLS GYFNLDNGSG KIRGVYTQGN AAMAPIFTEW IAPLKDLGVS TVTNANTGGT
DHLSFDAVGI PGFQFIQDAL DYDTRTHHSN MDVYEGLRAD DLRQAAVVEA TFVYNTAMRD
AMLPRKATPE YGERKVVQFP GAVK
//