ID J2J326_FLASC Unreviewed; 463 AA.
AC J2J326;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=PMI10_02869 {ECO:0000313|EMBL:EJL62490.1};
OS Flavobacterium sp. (strain CF136).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1144313 {ECO:0000313|EMBL:EJL62490.1, ECO:0000313|Proteomes:UP000007287};
RN [1] {ECO:0000313|EMBL:EJL62490.1, ECO:0000313|Proteomes:UP000007287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF136 {ECO:0000313|EMBL:EJL62490.1,
RC ECO:0000313|Proteomes:UP000007287};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL62490.1}.
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DR EMBL; AKJZ01000044; EJL62490.1; -; Genomic_DNA.
DR RefSeq; WP_007808987.1; NZ_AKJZ01000044.1.
DR AlphaFoldDB; J2J326; -.
DR PATRIC; fig|1144313.4.peg.2845; -.
DR eggNOG; COG2234; Bacteria.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000007287; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:EJL62490.1};
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:EJL62490.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000313|EMBL:EJL62490.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..463
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003749237"
FT DOMAIN 259..442
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 463 AA; 50919 MW; DBE6C47D60E2750F CRC64;
MKKTILLTAL ILSGLTSFAQ SNDEKNIKLF YKKALTDSKC YTWLEYLSND IGSRLSGSDN
AAKAVQYCKA QLENLGLDKV YLQEVTVPHW VRGEKETAYI LDNKTKTVVP ICALGGSVAT
PKTGVTAEVV EVKSIKELND LGEKVKGKIV FYNRPMDPEN IETFISYGGA GDQRRVGAQE
AAKFGAVGTI VRSLNLRLDD FPHTGAQSYG DLPKEKYIPT AAISTNGAEL LSESLKNNPT
LKFYFKQSCE TLPDVLSYNV IGELTGKEHP ENIMVVGGHL DSWDLADGSH DDGAGVVQSM
EVVHILKNLN YKPKNTIRVV LFMNEENGGK GGAKYEEVSK QKNENHIFAL ESDSGGFTPR
GFSIEADDAN FKKIQGFKDL FEPYLIHSFT LGHSGSDIEH LTSKTIVKAG LKPDSQRYFD
YHHAANDKFD AVNKRELELG AATMTTLLYL VDQTGIILPS ASN
//
