ID M0JS49_HALVA Unreviewed; 442 AA.
AC M0JS49;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=C437_02217 {ECO:0000313|EMBL:EMA10809.1};
OS Haloarcula vallismortis ATCC 29715.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662477 {ECO:0000313|EMBL:EMA10809.1, ECO:0000313|Proteomes:UP000011534};
RN [1] {ECO:0000313|EMBL:EMA10809.1, ECO:0000313|Proteomes:UP000011534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29715 {ECO:0000313|EMBL:EMA10809.1,
RC ECO:0000313|Proteomes:UP000011534};
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:EMA10809.1}.
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DR EMBL; AOLQ01000007; EMA10809.1; -; Genomic_DNA.
DR RefSeq; WP_004515246.1; NZ_AOLQ01000007.1.
DR AlphaFoldDB; M0JS49; -.
DR PATRIC; fig|662477.6.peg.428; -.
DR OrthoDB; 18376at2157; -.
DR Proteomes; UP000011534; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:EMA10809.1};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000313|EMBL:EMA10809.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000313|EMBL:EMA10809.1}.
FT DOMAIN 96..191
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 215..395
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 442 AA; 47205 MW; E3DF0241EE2A8C6D CRC64;
MDDTDWIGET FTSTVGWDHL ETLVDIGNRM AGSDGERRAA EATRDALAAY TRDARLSEFE
IQGWERGDSA VLVGGSPVAT QAHECIALPR SPSGEVTGEL VDVGHGLPAD FEDADCEGQI
VLARSDVPDW YDRYIHRREK YYRAVEAGAV GFIYCNHVEG VLPPTGSVGT AEAPIGEVPA
VGVASETGAR LARRYAGDAV TLSVDCETPA ATSQNVHAEL GPDTEERLLV TCHIDAHDIA
EGAMDNGAGT AMVVEAARAL AGREDELATR VEFVAFGAEE VGLVGSNRLA AETALDDVTA
VLNFDGVVQG RTLKCYTHGF DALTAAAESV ADRLDHPISL TPEQGPHSDH WPFVRRGVPG
YHVTSETGGD GRGWGHTHAD TLDKLEPRTF REQAILLTEL AVTLADRSAQ PAHKDPAEIA
DALEAQNLAE GMRSTGDWPF DD
//
