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Database: UniProt
Entry: A0A1U7GBD9_9BACT
LinkDB: A0A1U7GBD9_9BACT
Original site: A0A1U7GBD9_9BACT 
ID   A0A1U7GBD9_9BACT        Unreviewed;       602 AA.
AC   A0A1U7GBD9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=BGO49_27095 {ECO:0000313|EMBL:OJW05833.1};
OS   Planctomycetales bacterium 71-10.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX   NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW05833.1, ECO:0000313|Proteomes:UP000185848};
RN   [1] {ECO:0000313|EMBL:OJW05833.1, ECO:0000313|Proteomes:UP000185848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=71-10 {ECO:0000313|EMBL:OJW05833.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJW05833.1}.
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DR   EMBL; MKTT01000147; OJW05833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7GBD9; -.
DR   STRING; 1895807.BGO49_27095; -.
DR   Proteomes; UP000185848; 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   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR039866; CPQ.
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; PF04389; Peptidase_M28; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..602
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013024661"
FT   DOMAIN          363..572
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   REGION          29..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..251
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   602 AA;  65458 MW;  AC6249A3BE3E2504 CRC64;
     MLRILGTAAT LAVAGLIGLV PHAWAQAPVP TPPAAEAEKK AEPEKKTEPE APKSPADPIE
     RIKEEGEKRS QVMATLGTLT DVIGPRLSGS PGLKRANEWT RYQMEKWGME NAHLEAWGPF
     GRGWTLKRFS AQVIEPQCIP LIAVPKAWSP SLDGVLTAEV VHFDVKAEAD FEKYKGKLKG
     AIVLTAPAPD VSARFEPLAR RRSDKDLLDL ADAPEPGGPR EGRPRQVTPQ VPPVPGAPAP
     PQAPQPPRPP MGDMRAQMEL AAKKSKFLAD EGAALLIDPS RNGDGGTLFV QSASVPGPPS
     FLGVTLPGRR PQAWDKDVKV IPQLVMAKEH YNRLVRMLAV GEAIKMAVDL AVEFQDEDLN
     CYNTVAEIPG TDLKDEVVML GGHLDSWHGG TGATDNAVGC SVAMEAARIL KALDLKPRRT
     VRVALWTGEE QGIFGSKAYV DEHFRKRGPG GESAAEEKDE TKPEYDKLSG YFNLDNGTGK
     IRGVYLQGNE AVRPIFRRWL RPFKEMGAQT LSIANTGGTD HLSFDAVGLP GFQFIQDEIE
     YDTRTHHSNM DVYDRAQADD LKQASIIMAA FVYNAAMMDE KLPRKPARPA RPEGRPSAAA
     GN
//
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