ID M0DYK5_9EURY Unreviewed; 461 AA.
AC M0DYK5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=C472_02604 {ECO:0000313|EMBL:ELZ39893.1};
OS Halorubrum tebenquichense DSM 14210.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227485 {ECO:0000313|EMBL:ELZ39893.1, ECO:0000313|Proteomes:UP000011523};
RN [1] {ECO:0000313|EMBL:ELZ39893.1, ECO:0000313|Proteomes:UP000011523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14210 {ECO:0000313|EMBL:ELZ39893.1,
RC ECO:0000313|Proteomes:UP000011523};
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:ELZ39893.1}.
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DR EMBL; AOJD01000023; ELZ39893.1; -; Genomic_DNA.
DR RefSeq; WP_006628223.1; NZ_AOJD01000023.1.
DR AlphaFoldDB; M0DYK5; -.
DR PATRIC; fig|1227485.3.peg.497; -.
DR OrthoDB; 18376at2157; -.
DR Proteomes; UP000011523; 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 102..197
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 235..419
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 461 AA; 48973 MW; DD7BFBA9B9F8F3EC CRC64;
MTELPDRVAG DARTSDFGWN LLTDLTDIGN RMAGSAGERR GAERVVEAFE AAGLRNAGLD
EFEIPGWWRG ESSLSVSGPV ERHHEHSHEV IALPGTPSGE ATAPLVDVGD GTDEEFAAAG
DALEGAVAMA SSRTPDSHDR WIHRMEKYVA AAERGAVGFV FRNHIEGALP PTGEIGYHNR
PGPIPAVGVS KEVGDRLSRL AKGAGTEGDG DSADDERPTV SLDVDCRNEP TTSVNAVAEV
GPDTDEAVYL TAHVDAHDVS DGANDNGAGS ALVAEVGRLL ATVEDDLDTR VRLVTFGSEE
IGLWGAYHAA ETTPREEIAC VVNLDGACSS RNLRVGTNGF DGMRSVFESV TDAFDAPLAT
GETISPHGDQ WAFVQEGIPA VMVSTTSDQS GRGWGHTHAD TLDKLDSRDL GEVATLVAAS
VYRFATGDIE ATHRSRESIR DAIDEGYVEE LKTGGRWPYE E
//
