ID L9YZ67_9EURY Unreviewed; 436 AA.
AC L9YZ67;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=C487_09354 {ECO:0000313|EMBL:ELY78223.1};
OS Natrinema pallidum DSM 3751.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1227495 {ECO:0000313|EMBL:ELY78223.1, ECO:0000313|Proteomes:UP000011618};
RN [1] {ECO:0000313|EMBL:ELY78223.1, ECO:0000313|Proteomes:UP000011618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3751 {ECO:0000313|EMBL:ELY78223.1,
RC ECO:0000313|Proteomes:UP000011618};
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:ELY78223.1}.
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DR EMBL; AOII01000046; ELY78223.1; -; Genomic_DNA.
DR RefSeq; WP_006185440.1; NZ_AOII01000046.1.
DR AlphaFoldDB; L9YZ67; -.
DR PATRIC; fig|1227495.3.peg.1892; -.
DR eggNOG; arCOG02959; Archaea.
DR OrthoDB; 18376at2157; -.
DR Proteomes; UP000011618; 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 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 92..185
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 209..390
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 436 AA; 47499 MW; 9F752E66418A5B78 CRC64;
MSDWIGTVFR SDAGWNHLEG LVDIGNRMAG SEGEREAAEL TRDALADAGA RNARLDSFEI
QGWTRDDSAI MAGDTTQDCI ALPRSPDDRV VAPLIDLGYG LPADFEATDV EDAIVMVRSD
VPDYYDRYIH RREKYHHAVE QGAVGFVYRN HVEGCLPPTG SVGWHDEPIG PIPAVGVSSE
VGARLGRRFD GESITVSVEA TIQPAESQNV HAELGPDTDE RVLVTSHVDA HDIAEGAMDN
GAGTAMLVEL ATALAAREDD LETRVEFVGF GAEEVGLLGS RRYAERADHD AIEAVVNSDG
VVRDRTLSIV THGFDALADA ANEVADRYDH PIGIVPKLGP HSDHWSFVKW GVPGCHVKSV
SDGAGRGWGH TFADTIEKLE PRTLREQAIL LTDYVMTLAR EDVTVARRDH EEIAADLESQ
DLAESMRITG DWPYDD
//
