ID C1ACX3_GEMAT Unreviewed; 457 AA.
AC C1ACX3;
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_3308 {ECO:0000313|EMBL:BAH40350.1};
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:BAH40350.1, 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; BAH40350.1; -; Genomic_DNA.
DR RefSeq; WP_015895119.1; NC_012489.1.
DR AlphaFoldDB; C1ACX3; -.
DR STRING; 379066.GAU_3308; -.
DR KEGG; gau:GAU_3308; -.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..457
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002904264"
FT DOMAIN 258..442
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 457 AA; 48891 MW; A52907EFF7919A81 CRC64;
MHTRFRRTVA ALSLAACPSA LLAQPADAIP AKYRDIANRI IAAAQADSAG AWNRIAELSD
RFGHRFSGSQ SLEQAIDWTV TTMKGDGLDN VRKERVMVPH WVRGTESLEL VAPRRQLLPM
LGLGGSIATP AAGITAEVMV VASFEELTQR AAEAKGKIVL YDAEWRDYGY NGAFRRQGAV
AAAKAGAVAS LARSAGPYSM RTPHTGNMAY DSTVAKIPHA SVTAEDAMMM RRMIARGEKV
RVTLKMSARM LPDAVSHNVM GELKGREKPA EIVVMGGHID SWDVGQGAMD DAGGVVAAWE
AIRLLKKLGL TPRRTIRVVG WTNEENGGRG GQAYRDAHQN EVHQLAIESD GGVFSPLGFG
FTGSAEARKL VEAVGTLLTP IGAGRIGPNG GGADIGPIMQ TGVPGMGLDV DGSRYFWFHH
TDADTPDKLD PKEVQRCVAA MAIMAYIVAD LEQGLPR
//
