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Database: UniProt
Entry: A0A1S2VDE4_9BACT
LinkDB: A0A1S2VDE4_9BACT
Original site: A0A1S2VDE4_9BACT 
ID   A0A1S2VDE4_9BACT        Unreviewed;       502 AA.
AC   A0A1S2VDE4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=BLX24_23290 {ECO:0000313|EMBL:OIN56709.1};
OS   Arsenicibacter rosenii.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Arsenicibacter.
OX   NCBI_TaxID=1750698 {ECO:0000313|EMBL:OIN56709.1, ECO:0000313|Proteomes:UP000181790};
RN   [1] {ECO:0000313|EMBL:OIN56709.1, ECO:0000313|Proteomes:UP000181790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM-1 {ECO:0000313|EMBL:OIN56709.1,
RC   ECO:0000313|Proteomes:UP000181790};
RA   Huang K.;
RT   "Arsenicibacter rosenii gen. nov., sp. nov., an efficient arsenic-
RT   methylating bacterium isolated from an arsenic-contaminated paddy soil.";
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}.
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:OIN56709.1}.
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DR   EMBL; MORL01000019; OIN56709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S2VDE4; -.
DR   Proteomes; UP000181790; 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   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:OIN56709.1};
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:OIN56709.1};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000313|EMBL:OIN56709.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000181790}.
FT   DOMAIN          148..236
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          265..455
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   502 AA;  55300 MW;  6AEEEA8D1CA2B756 CRC64;
     MHLYFYRKSR LTTVLLISAV GMLTAFTFTG PNNRRSSLEK VFGKINEEVL KNGKAYTTLA
     DASQQIGHRL TGSPNGSKAE TYAYDLLRSY GFKEVRYEPF EVESWMRDTV TLSVVPNKSD
     NFRDLKVVSL AHSPVSAHVR GEIIDVGNGL EGDFGAVKDK IKGKIALVNI GLAGAKGARN
     LHRSEKTALA IQHGAVGVIM VNLVPGDVLL TGTASVTGKL IPIPAVCISY ESGVALRKWI
     EEEKEDKLHA VIDMTNKSRK IRARNVVATL RGTDFPNEKI IIGGHLDSWD LATGAIDNGI
     GSFSVLDIAR TFKALNIKPR RTIEFVMFMG EEQGLLGSKA MASALKNSGQ MDKVRYMMNL
     DMTNNPGGIN AFGREEMVSF FKSIGEVIQK VDPAFANTSA NQAGLHSDHQ PFMIEGIPVV
     GMSGSLTKEV LDCYHANCDR INLVNKDHMT NTVRYTSMVL YALADADDIP TKRLDDTKTR
     DYLIAQGLRT PLQIANEWRW KE
//
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