ID C1A7P3_GEMAT Unreviewed; 559 AA.
AC C1A7P3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN OrderedLocusNames=GAU_1211 {ECO:0000313|EMBL:BAH38253.1};
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH38253.1, ECO:0000313|Proteomes:UP000002209};
RN [1] {ECO:0000313|Proteomes:UP000002209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC {ECO:0000313|Proteomes:UP000002209};
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) 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; AP009153; BAH38253.1; -; Genomic_DNA.
DR AlphaFoldDB; C1A7P3; -.
DR STRING; 379066.GAU_1211; -.
DR KEGG; gau:GAU_1211; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_033697_1_1_0; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000002209; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002209}.
FT DOMAIN 308..497
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 559 AA; 59938 MW; D4C9CE272CC8391C CRC64;
MDLTLSSMNS RLSLVPRPLL GALALGLAVG TPAAPRLEAQ TPATFPTNDA TLKRIWTLGM
DSSHVERLAQ QLLDSIGPRL TGTARQKAAN DWVLSLYKQW GVDGKNEQTG TWRGWRRGHS
HIDLLTPRVR TLEGTMLAWS PGTNKKDLTA SVIVLPRFAD STEFVKWLPQ AKGKFVLVSA
PQPTCRPTDN WQQHATPASK ARMDSLRADV NREWGGISVR GTGYSNALGT GSLGVRLEEG
GAAGVISSRP KNAWGTIDVF ESYNLKAPAI ALSCEDYGLV FRLAENKQSP TVRLNLDADL
LGEQPIFNTI GMIKGTEKPN EYVVLSAHFD SFDGGSGATD NGTGSLTMLE AMRILSTVYP
KPKRTILIGH WTAEEHGLVG SRAFTEDHPE VVQGLQALFN QDGGTGRVQS VGAGGLIDAG
VHLRQWLSVM PTEVSSAITP RIPGAPSGGG SDDASFACHG APAFGLGGIG WDYGSYTWHT
NRDTYDKVVF DDLRWNATVT AMLAYLAAND ATTITRERAT AEQIRPQGGA GAAGAGGNAG
AFAWPTCQKA PRKTNPRLR
//
