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Database: UniProt
Entry: A0A3P0XBL8_9BACT
LinkDB: A0A3P0XBL8_9BACT
Original site: A0A3P0XBL8_9BACT 
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
//
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