ID A0A1I1GTA6_9SPHI Unreviewed; 537 AA.
AC A0A1I1GTA6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=SAMN05421747_10565 {ECO:0000313|EMBL:SFC14532.1};
OS Parapedobacter composti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=623281 {ECO:0000313|EMBL:SFC14532.1, ECO:0000313|Proteomes:UP000199577};
RN [1] {ECO:0000313|EMBL:SFC14532.1, ECO:0000313|Proteomes:UP000199577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22900 {ECO:0000313|EMBL:SFC14532.1,
RC ECO:0000313|Proteomes:UP000199577};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOLL01000005; SFC14532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1GTA6; -.
DR STRING; 623281.SAMN05421747_10565; -.
DR Proteomes; UP000199577; 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; 3.50.30.30; -; 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:UP000199577};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..537
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011698447"
FT DOMAIN 300..482
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 516..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 59707 MW; 7F547986B73D19C1 CRC64;
MRLYMNIFQV SRYRGVKRTS LAILLGLSST WADAQPGGTS EAHTLDPVVA QIVKEAHEHS
QLQQLAHELL DVVGPRLVGT PQMKHAHDWA VAKYNTWGIE ARYEEFGEWR GWERGISHID
MVHPRVKTLA GTQLAWSPTT GGKAVEAEVI VLPQVKDSLA FKAWLPHVKG KYVMVSMPQP
TGRPDHNWEQ YARPESFEKM KRERDSLTKA WNANIDAMGI SSRSLPRILE EAGAAGILEC
YWSREFGSNK IFGARTTSVP SLDISLEDYG VLYRLAENGH KPRIKVETDS KHLGTVPTFN
TIAEIKGSEK PDEYVILSAH FDSWEGGSGA TDNGTGTITM MEVARILKKV LPHPKRTILI
GHWGSEEQGL NGSRAFVLDH PEIVQKTQAV FNQDNGTGRV ASINGSGFLH AYDFMGRWLS
AAPREITRDI NTDFPGLPSS GGSDHASFAA AGIPAFMLSS LSWGYSTITW HTNLDTYDKL
IFDDLTSNVV LIATLAYKAS EEPELVNREK RVMPLGRDGQ PQQWPVIRQP RRTGVGY
//
