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Database: UniProt
Entry: A0A410G3F4_9FLAO
LinkDB: A0A410G3F4_9FLAO
Original site: A0A410G3F4_9FLAO 
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
//
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