ID L9XVJ1_9EURY Unreviewed; 460 AA.
AC L9XVJ1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=C492_03971 {ECO:0000313|EMBL:ELY65441.1};
OS Natronococcus jeotgali DSM 18795.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronococcus.
OX NCBI_TaxID=1227498 {ECO:0000313|EMBL:ELY65441.1, ECO:0000313|Proteomes:UP000011531};
RN [1] {ECO:0000313|EMBL:ELY65441.1, ECO:0000313|Proteomes:UP000011531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18795 {ECO:0000313|EMBL:ELY65441.1,
RC ECO:0000313|Proteomes:UP000011531};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY65441.1}.
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DR EMBL; AOIA01000024; ELY65441.1; -; Genomic_DNA.
DR RefSeq; WP_008420612.1; NZ_AOIA01000024.1.
DR AlphaFoldDB; L9XVJ1; -.
DR STRING; 1227498.C492_03971; -.
DR PATRIC; fig|1227498.3.peg.816; -.
DR OrthoDB; 34215at2157; -.
DR Proteomes; UP000011531; 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; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
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; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 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 115..204
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 231..418
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 49449 MW; 2B37333190AB5C8D CRC64;
MSDDDSDLTA GRPDPTTARA LGRAWADDRS RELLTRLTAL PNRMGGSPGE RRAAALVRDG
LEEAGVADVR IDEFPMQRWQ RGTTEFAVTD VDDAPAGERS FEAIALPYCP PGDLEGPLVD
VGYGTPEEID EVDLRGAIAV ASTTTPSDRR FVHRMEKFGH AVAAGAEAFV FANHVSGQLP
PTGALKFDAE AAIPGVGVSA ETRDWLVEYA KRDARARLRV DAATTDGSSR NVHGTLGPET
DEELLVLAHY DAHDVAEGAL DNGCGIATVV GAASILADLE DVLECRVRIA GVGSEELGLL
GAEALAADLD LESVRAVVNV DGAGRFRNLT ALSHASEPLA TLAEDVTESV GQPIGHDREP
HPFSDHWPFL RAGVPAVQLH SEPTDGGERG RGWTHTAADT RDKVDPRNLR EHAMLTALLV
RELTRTEIPR VSTDELRERF EAQDYVAGMR AADIWPSTWD
//
