ID A0A2T2YPE0_9BACT Unreviewed; 516 AA.
AC A0A2T2YPE0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=AHMF7605_18010 {ECO:0000313|EMBL:PSR57358.1};
OS Adhaeribacter arboris.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Adhaeribacter.
OX NCBI_TaxID=2072846 {ECO:0000313|EMBL:PSR57358.1, ECO:0000313|Proteomes:UP000240357};
RN [1] {ECO:0000313|EMBL:PSR57358.1, ECO:0000313|Proteomes:UP000240357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF7605 {ECO:0000313|EMBL:PSR57358.1,
RC ECO:0000313|Proteomes:UP000240357};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Adhaeribacter sp. HMF7605 Genome sequencing and assembly.";
RL Submitted (MAR-2018) 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:PSR57358.1}.
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DR EMBL; PYFT01000001; PSR57358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2YPE0; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000240357; 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 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..516
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015771613"
FT DOMAIN 278..464
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 480..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 57524 MW; CDFE1765A6D61F39 CRC64;
MKKRVILFYL PFLFWGSFAV AQTKDPVVEA IVKEANENSQ LEKLAHELVD VIGPRLVGTP
QMQQANDWAV AKYKEWNINA HNEKWGEWRG WQRGISHIDL VYPRTESLEG MQLAWSPGMK
KAVTAELVII PDIADSVEFK KWLPTVKGKF VLISMNQPTG RPDYNWQEFA RKESFEKMKA
DRAAQTEAWR NRINKTGRTA RSLSVALEKA GAAGVVTCNW SNGFGVNKIF SAYTKKIPTI
DISLEDYGLL YRLTESGHKP KIRVQTEAKE KGIVPTFNTI AEIKGSEKPN EYVILSAHFD
SWDGGTGATD NGTGTLTMME AMRILKKVYP SPKRTILVGH WGSEEQGLNG SRAFVADHPE
IVPNVQAVFN QDNGTGRVVN LAGQGFLHSY EYLGRWLTQV PEEIRSPIQT SFPGAPGTGG
SDFASFVAAG VPAFSLSSLN WSYGTYTWHT NRDTYDKIVF DDVRSNAILT AILAYMASED
PNKTPRDKSV LPINPQTGQP GTWPEPRQPT RKGGLD
//
