ID A0A410G3F4_9FLAO Unreviewed; 521 AA.
AC A0A410G3F4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-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=EI546_08685 {ECO:0000313|EMBL:QAA81790.1};
OS Aequorivita sp. H23M31.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=2494375 {ECO:0000313|EMBL:QAA81790.1, ECO:0000313|Proteomes:UP000285517};
RN [1] {ECO:0000313|EMBL:QAA81790.1, ECO:0000313|Proteomes:UP000285517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H23M31 {ECO:0000313|EMBL:QAA81790.1,
RC ECO:0000313|Proteomes:UP000285517};
RA Bae J.-W.;
RT "Complete genome sequencing of Aequorivita sp. H23M31.";
RL Submitted (JAN-2019) 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; CP034951; QAA81790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410G3F4; -.
DR KEGG; aev:EI546_08685; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000285517; Chromosome.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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:QAA81790.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Reference proteome {ECO:0000313|Proteomes:UP000285517};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..521
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019046829"
FT DOMAIN 296..496
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 521 AA; 58334 MW; 8365FDC2F1571FAE CRC64;
MRKLTFVLWL FIFPAVLLAQ DAAVLQQIKK EGLENSQVMD IAFHLTEKSG PRLMNSPGFY
RAMDYSVKQL KEWGLDDVKK DEWGDFGKGW ELKKFYIAME SPWYKPLIAF PKAWTSGTNG
LKTASVILID PEADSTALVT KYRGKLAGKI LAMDKMIEYE LDDKSDLVRY SKAELDSMAS
IQLDKKKSDD SEMTERRKKW IQAWRDARKK AEVLGNLARE EGAVAIISSS PRNHDGTVFV
QQGGSHASDA PENFLDIAMA LEDYNMIVRL VRANEPVKLG LEVASKFYTD QEKGYNVVGE
ITGTDKKLKD EVVMIGGHLD SWQGSVGATD NAAGAAVMME AMRILKKLNI KPKRTIRIGL
WGGEEQGIYG SRGYVSKTFA DRKDMKLKPA HEKFDVYFNL DNGTGRINGI YLQENVAAHN
ILKKWLAPFE DLGATTITPG NTGGTDHLSF DSVGLPGFQF IQDEVEYNSR THHSNMDSYD
HLVEADLKQA ATVIAGLIYQ AAISDQKVPR KELPKAQNSE W
//