ID A0A1M5LYZ0_9EURY Unreviewed; 442 AA.
AC A0A1M5LYZ0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=SAMN05443636_0828 {ECO:0000313|EMBL:SHG70312.1};
OS Halobaculum gomorrense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halobaculum.
OX NCBI_TaxID=43928 {ECO:0000313|EMBL:SHG70312.1, ECO:0000313|Proteomes:UP000184357};
RN [1] {ECO:0000313|EMBL:SHG70312.1, ECO:0000313|Proteomes:UP000184357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9297 {ECO:0000313|EMBL:SHG70312.1,
RC ECO:0000313|Proteomes:UP000184357};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQWV01000002; SHG70312.1; -; Genomic_DNA.
DR RefSeq; WP_073307150.1; NZ_FQWV01000002.1.
DR AlphaFoldDB; A0A1M5LYZ0; -.
DR STRING; 43928.SAMN05443636_0828; -.
DR OrthoDB; 34215at2157; -.
DR Proteomes; UP000184357; 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:SHG70312.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SHG70312.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SHG70312.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184357}.
FT DOMAIN 100..191
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 216..397
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 442 AA; 47209 MW; BC4641A98EE5BA89 CRC64;
MNLDDDLAAA VGRVWTDTAP WEFITELTAL GGRMGASAGE ERAADLVADA FDERGLERVR
RQSFDAPAWR RGGTELRVTA PAERAFDAIA LPYSPAGDAA GELVDVGYGT PEEIDAVDVE
GKVAVASTTT PSESRFIHRM EKFGTAAEAG ADAFVFVNHV PGQLPPTGSL TFGEEAAIPA
VGVSKETGAW LTEYADEGGE IDLSVDAETV PDESQNVLAH TGPRTDEYVL VLAHYDGHDI
AEGALDNGCG VATLLAAASV LSAADLDIGV RFAAVGCEET GLLGSEHLAA TTDLDTVKAV
VNLDGAGRFR DLVAMTHTSE ATARTARRVA DRTRQPIAVH EEPHPFSDQW PFVRRGVASL
QFHSDSGERG RGWGHTHADT RDKVDDRCIR EHGVLAALLV RELADEATDV PVLDPYELEE
AFRNAEFEPG MKAAGLWPEG WE
//
