ID H8KXE5_SOLCM Unreviewed; 459 AA.
AC H8KXE5;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN OrderedLocusNames=Solca_3469 {ECO:0000313|EMBL:AFD08474.1};
OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB
OS 12057 / USAM 9D) (Flexibacter canadensis).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD08474.1, ECO:0000313|Proteomes:UP000007590};
RN [1] {ECO:0000313|Proteomes:UP000007590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D
RC {ECO:0000313|Proteomes:UP000007590};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Kopitz M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Solitalea canadensis DSM 3403.";
RL Submitted (FEB-2012) 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; CP003349; AFD08474.1; -; Genomic_DNA.
DR RefSeq; WP_014681697.1; NC_017770.1.
DR AlphaFoldDB; H8KXE5; -.
DR STRING; 929556.Solca_3469; -.
DR KEGG; scn:Solca_3469; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_033697_1_1_10; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000007590; Chromosome.
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; IPR046450; PA_dom_sf.
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; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:AFD08474.1};
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:AFD08474.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000313|EMBL:AFD08474.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007590};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..459
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003614683"
FT DOMAIN 260..448
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 459 AA; 50185 MW; A030EB692DAE58A0 CRC64;
MKKKSLLFLV AVAMFTTGSY ASNPDSMVVS KIYEEVLGNG KVYENLHYLC KNIGPRLSGS
ANAQNAVEWT RSLMESYGFD RVYLQEVMVP HWERGAKEKA WFATGGKKIN VEIAALGGSV
ATSEKGIETT IIEVFNFDQL KELGEEKIKG KIVFFNRPMN PKTLHTFNAY GAAVNQRVQG
AIEAAKYGAI GVIVRSMTTK IDEFPHTGTM RYDEKLTKIP AAAISTKDAN SLSAALKTDP
SLKFFYQMNC KTLPDVLSYN VIGEIKGSEQ PEKIITVGGH LDSWDLAEGA HDDGAGTMQS
VEVLRTIKAL GIKPKHTVRA VMFMNEENGT KGGLKYAENA KVTNEQHYAA IESDSGGLTP
RGFSIDASTE VVNRIMSWSP IFDEYGLKEI GGGGGAGSDI GPLKSLGTAL FGFRPDSQRY
FDYHHAKTDV FENVNERELK LGAAAMATLV YLIDQNGLN
//
