ID A0A1H8WWH3_9EURY Unreviewed; 459 AA.
AC A0A1H8WWH3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=SAMN04487948_1492 {ECO:0000313|EMBL:SEP31996.1};
OS Halogranum amylolyticum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=660520 {ECO:0000313|EMBL:SEP31996.1, ECO:0000313|Proteomes:UP000199126};
RN [1] {ECO:0000313|EMBL:SEP31996.1, ECO:0000313|Proteomes:UP000199126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10121 {ECO:0000313|EMBL:SEP31996.1,
RC ECO:0000313|Proteomes:UP000199126};
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; FODV01000049; SEP31996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8WWH3; -.
DR OrthoDB; 34215at2157; -.
DR Proteomes; UP000199126; 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:SEP31996.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SEP31996.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SEP31996.1}.
FT DOMAIN 97..189
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 241..418
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 207..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 49014 MW; 7830DC42A9572179 CRC64;
MDDTLHAALG RAWLDDIGWN LLTDLTAIDG RMGGSDGERR AADRVADALR AAGVDDVRLQ
PFETNRWTRG SATLDLLAPD DRSFEALALP YCPAGEVEAD LVDVGHGTPS EVDDCDVAGK
VAVASTTTPE GGRFVHRMEK FGHAVEAGAV GFVFVNHVPG QLPPTGALRF DEEADAVAVG
VSKETGAWLT EYAERGGRVR LSVDARTDPA ESQNVVGRLG GGPGRTHGGD EHDRTDGTDG
SDVDGDLLLV AHYDAHDVGE GALDNGCGVA VVVAAARILA ELSPRLDRDV RVAAVGCEET
GLVGSERLAS AVDRDDLAAV VNVDGAGRFR DLVAMTHTSE ATADVAETVA DETGRPIRVV
SEPHPFSDQW PFVREGVPAL QLHSDSGERG RGWAHTSADT REKVDRRNLR EHAMLTALFV
LELAGRDVAR LDRDDLVAAF RDADFERGMR AADLWPDDW
//
