ID A0A1I0NLH9_9EURY Unreviewed; 433 AA.
AC A0A1I0NLH9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=SAMN04487945_0964 {ECO:0000313|EMBL:SEW02088.1};
OS Halobacterium jilantaiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=355548 {ECO:0000313|EMBL:SEW02088.1, ECO:0000313|Proteomes:UP000198518};
RN [1] {ECO:0000313|EMBL:SEW02088.1, ECO:0000313|Proteomes:UP000198518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5337 {ECO:0000313|EMBL:SEW02088.1,
RC ECO:0000313|Proteomes:UP000198518};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOJA01000001; SEW02088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0NLH9; -.
DR STRING; 355548.SAMN04487945_0964; -.
DR OrthoDB; 18376at2157; -.
DR Proteomes; UP000198518; 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 CDD; cd04819; PA_2; 1.
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 ECO:0000313|EMBL:SEW02088.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SEW02088.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SEW02088.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198518}.
FT DOMAIN 97..184
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 208..385
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 433 AA; 46411 MW; 0FFABE1C333670CE CRC64;
MADWIGDTFT SDTGWTHLER LVDVRNRMAG SDGEREAAVA TRDALAEHAD DAWLDEFDIQ
GWTRGDSGVE TPAGVEDSIA LPRSPSGDAA GEFVDLGHGL PEDFEDADLD GKVVMVASDV
PDWYDRYLHR REKYYHAVEA GAAAFVYENH VEGCLPPTGS VGTSDAPIGD IPAVGVSREV
GARLSRRFEG DEVTVSVNAD VHDATSQNVH ATLGPDTDEE LLVTSHVDAH DIAEGAMDNG
AGTAMVVEVA RALAAREDEL DTRIHFVCYG AEEVGLVGAA HDADERDLAS VRAVLNFDGV
VRGRTLKFYA HGFDALADAA RGVGDDFGHP VSVTPKLGPH SDHWEYVQHG VPGYHVASET
GGAGRGWGHT YADTLEKLEV RNFREQAVLL TDLAVRLADD GFAVAHASEA DIAAALEDED
LAEGMKITGD WPY
//
