ID F0RG12_CELLC Unreviewed; 464 AA.
AC F0RG12;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN OrderedLocusNames=Celly_0137 {ECO:0000313|EMBL:ADY27972.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY27972.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY27972.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
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; CP002534; ADY27972.1; -; Genomic_DNA.
DR RefSeq; WP_013619720.1; NC_015167.1.
DR AlphaFoldDB; F0RG12; -.
DR STRING; 867900.Celly_0137; -.
DR KEGG; cly:Celly_0137; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_033697_1_1_10; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000007487; Chromosome.
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:UP000007487};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..464
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003257606"
FT DOMAIN 259..444
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 464 AA; 50988 MW; B3C21875AF126A71 CRC64;
MKKITVIFLL VCTTIFAQTA DEKQLRSIYD AALTDGMAYN WLDHLSNQIG GRLSGSVEAQ
QAVDYTKKEL EKLGVDRVYL QPVMVPRWVR GLPEYANILS EDGTTTSVPI CALGGSVATS
ALGLKANVIE VKSIKELEEL GKEKIEGKIV FFNRPMNPKD IVTFTAYGGC VDQRYSGAAE
AGKFGAVGVI VRSVNLRLDD YPHTGSMSYG DTPVKNRIPA AAISTNGAEL LATALKLNPN
TKFFFKQNCK QYDDVQSYNV IAEIKGSTYP NEIIVVGGHL DSWDLGDGSH DDGAGVVQSM
DVLRLIKASG YKPKRTIRAV LFMNEENGLR GGNKYAQVAK SKNENHIFAL ESDAGGFSPR
GFSFDCSTEN FEQVESWRNL FKPYLIHLFE KGGSGADVGP LKKDNIVLAG LRPDSQRYFD
HHHAANDTFE HVNKRELELG AATMTSLVYL FDKYGIVTSK KIKG
//
