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Database: UniProt
Entry: R4W836_9EURY
LinkDB: R4W836_9EURY
Original site: R4W836_9EURY 
ID   R4W836_9EURY            Unreviewed;       433 AA.
AC   R4W836;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=L593_01605 {ECO:0000313|EMBL:AGN00274.1};
OS   Salinarchaeum sp. Harcht-Bsk1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Natronoarchaeaceae; Salinarchaeum.
OX   NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00274.1, ECO:0000313|Proteomes:UP000014072};
RN   [1] {ECO:0000313|EMBL:AGN00274.1, ECO:0000313|Proteomes:UP000014072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00274.1};
RX   PubMed=23868130;
RA   Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA   Toshchakov S.V.;
RT   "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT   Isolated from Hypersaline Lake Baskunchak, Russia.";
RL   Genome Announc. 1:E00505-13(2013).
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; CP005962; AGN00274.1; -; Genomic_DNA.
DR   RefSeq; WP_020445168.1; NC_021313.1.
DR   AlphaFoldDB; R4W836; -.
DR   STRING; 1333523.L593_01605; -.
DR   GeneID; 16179873; -.
DR   KEGG; sali:L593_01605; -.
DR   PATRIC; fig|1333523.5.peg.326; -.
DR   eggNOG; arCOG02959; Archaea.
DR   HOGENOM; CLU_033697_0_0_2; -.
DR   OrthoDB; 18376at2157; -.
DR   Proteomes; UP000014072; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014072}.
FT   DOMAIN          91..184
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          208..392
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   433 AA;  47043 MW;  8EEE8F3B05A1A8E1 CRC64;
     MTNWIGEAFT SDAGWNHLET LVDVGDRMAG SEGEREAAAA TRDALAEVGA RDAHLESFDV
     QGWTRGTSEL RAGDTSQECI ALPRSPSGEA TGELIDVGYG LPSDFEQDLE GAVVMAASNV
     PGWYDRFLHR REKYYHAVEA GAAAFVFRNH VEGCLAPTGS VGTEDDPIGD VPAIGVSKEV
     GDRLLRRWEG DSVTVDVEAE ISDATSRNVH ATLGPDTDEE VLLTSHVDAH DIAEGAGDNG
     AGTAVVVEAA KALAAREDEL DTKVHLLVYG AEEVGLCGSA YDSDQRDHDD IKAIVNSDGV
     VRGRTLRCYT HDFDELEAAA ETVADRFDHP IETTPKLNPH SDHWPYVQWG VPGFHLMSET
     DYEGRGWGHT RADTLDKLEQ RTLREQSILI ADLVDHLADS DTTIEHRTPE SIAAQLEDDD
     LAEGMKVIGD WPY
//
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