ID A0A3M0FW16_9FLAO Unreviewed; 473 AA.
AC A0A3M0FW16;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EAX61_15415 {ECO:0000313|EMBL:RMB56157.1};
OS Dokdonia sinensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Dokdonia.
OX NCBI_TaxID=2479847 {ECO:0000313|EMBL:RMB56157.1, ECO:0000313|Proteomes:UP000281985};
RN [1] {ECO:0000313|EMBL:RMB56157.1, ECO:0000313|Proteomes:UP000281985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH27 {ECO:0000313|EMBL:RMB56157.1,
RC ECO:0000313|Proteomes:UP000281985};
RA Zhou L.Y., Du Z.J.;
RT "Dokdonia luteus sp. nov., isolated from sea water.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMB56157.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; REFV01000021; RMB56157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0FW16; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000281985; 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:UP000281985};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..473
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018290307"
FT DOMAIN 264..449
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 473 AA; 52017 MW; E90A849F3598F0F2 CRC64;
MNKVLKHFLL FLFLLGGYAF AKAQQDSIQI RKIYDEALKN GHSYQWLDYL SNQIGSRLSG
SSGAEEAVQW TKEQLDSIGL DKVWLQPVMV PKWVRGTPEY AFIESGLGNT TQVPICALGG
SVATPNGGIK AQVVEVQGIE ELKQLGIEVV KDKIVFFNRP MQDELILTFQ AYGGCVDQRY
AGAMEAAKLG AAGVLVRSVT HSIDDYPHTG SMSYGDLPNS KRIPAAAIST KGAELLSTLL
KLNKETKFFY SMSCKNYADV QSYNVIGEIT GTQFSDKFMV VGGHLDSWDL GDGSHDDGAG
VVQSMEVLRL MKAVGYRPKH SIRVVLFMNE ENGLRGGNKY AAVARAKGEK HVFALESDSG
GFTPRGFSFD SDDRNFNLVL QWKTLFEPYL IHSFTRGGSG ADIGPLKGDG TVLAGLRPDS
QRYFDYHHAA NDTFDAVNKR ELELGAATMT SLVYLMDNYI MKPAQIIEAP LKD
//