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Database: UniProt
Entry: A0A1T1CDS3_9FLAO
LinkDB: A0A1T1CDS3_9FLAO
Original site: A0A1T1CDS3_9FLAO 
ID   A0A1T1CDS3_9FLAO        Unreviewed;       456 AA.
AC   A0A1T1CDS3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-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=BXU11_12625 {ECO:0000313|EMBL:OOV26548.1};
OS   Flavobacterium sp. LM5.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1938610 {ECO:0000313|EMBL:OOV26548.1, ECO:0000313|Proteomes:UP000189962};
RN   [1] {ECO:0000313|EMBL:OOV26548.1, ECO:0000313|Proteomes:UP000189962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM5 {ECO:0000313|EMBL:OOV26548.1,
RC   ECO:0000313|Proteomes:UP000189962};
RA   Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT   "Genome sequences of bacteria isolated from the littoral zone of southern
RT   Lake Michigan.";
RL   Submitted (JAN-2017) 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:OOV26548.1}.
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DR   EMBL; MUFX01000004; OOV26548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1CDS3; -.
DR   OrthoDB; 9769665at2; -.
DR   Proteomes; UP000189962; 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}.
FT   DOMAIN          259..445
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   456 AA;  50387 MW;  0DEE71AE4A6F4F9D CRC64;
     MKKTFFTALL LSLGGVIFSQ TSDELQLKAI YQSALTKGQG YQWLDYLSNQ IGHRLSGSDN
     AEKAVQYTKA QLEALGLDRV FLQEVMVPKW VRGAKETAYI KDGKNKIEVP ICALGSSVAT
     PKKGLLAPVI EVHSIKELES LGTALKGKIV FYNRPMEAEY IETFNAYGHC VDQRSSGARE
     AAKYGAVGTI VRSMNLRLDD FPHTGNQSYG DLPQAQWIPT AAISTNGAEL LSKKLKENPQ
     LQFYFKQSCE QMADVLSYNV VGELKGSETP ENIMVVGGHL DSWDLADGSH DDGAGVVQSM
     EALRILKQLN YKPKNTIRVV LFMNEENGNR GGKKYAELAQ TNKENHVFAL ESDSGGFSPR
     GFSFECNDEE FAKFSSWKGL FEPYLIHSFV KGHSGTDIGP LASKHIVKAG LKPDSQRYFD
     YHHAANDTFD AVNKRELELG AATMASLLFL MDQKGL
//
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