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Database: UniProt
Entry: A0A1H7LKG6_STIAU
LinkDB: A0A1H7LKG6_STIAU
Original site: A0A1H7LKG6_STIAU 
ID   A0A1H7LKG6_STIAU        Unreviewed;       472 AA.
AC   A0A1H7LKG6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=SAMN05444354_103265 {ECO:0000313|EMBL:SEK99386.1};
OS   Stigmatella aurantiaca.
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=41 {ECO:0000313|EMBL:SEK99386.1, ECO:0000313|Proteomes:UP000182719};
RN   [1] {ECO:0000313|Proteomes:UP000182719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17044 {ECO:0000313|Proteomes:UP000182719};
RA   Varghese N., Submissions S.;
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}.
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DR   EMBL; FOAP01000003; SEK99386.1; -; Genomic_DNA.
DR   RefSeq; WP_075005861.1; NZ_FOAP01000003.1.
DR   AlphaFoldDB; A0A1H7LKG6; -.
DR   OrthoDB; 9769665at2; -.
DR   Proteomes; UP000182719; 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; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
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   ECO:0000313|EMBL:SEK99386.1};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SEK99386.1};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:SEK99386.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182719};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..472
FT                   /note="Carboxypeptidase Q"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010350772"
FT   DOMAIN          260..446
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   472 AA;  49484 MW;  37D8E42F7D97B24C CRC64;
     MPVSTFLVPS HLMLQLLTAA APAPAPQAAP ALPVAERLVG AALTEGHAWT RLAELTDGVG
     ARLSGSEGAA AAVQWALRSF KADGVKAWLE PVKVPHWVRG EERAELLGSE RFRGRPLSVM
     ALGGSGATPP EGVTGEVVEV RSLEELGALG ERVKGRIVLF NHIMQKPEDY GRFASLRSRG
     PAAAAKAGAV AALVRSLATA SLATPHTGAT RFEEGDPRIA AASVTVEDAE LLSRLVAAGG
     PVRVKLVLGC QELPDADSFN VVAEVKGREK PQEVVLLGAH LDSWDVGTGA HDDGAGVVMV
     MEAARLLAKQ RPAPRRTVRV VLFMNEENGL RGARAYAEAH AAELPRHVAA LELDSGGGRP
     VGVVLRAGAG AAEKVRPWLS PLRTVGAGAL MEGEAGGADL IPLMPARVPF FGLRQDASRY
     FDVHHTHADT LDKVDPVALA QSTAAVTWLA YAMAEMPELL PRPEVPTPSA GH
//
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