ID W7QLJ4_9ALTE Unreviewed; 477 AA.
AC W7QLJ4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=DS2_14529 {ECO:0000313|EMBL:EWH08998.1};
OS Catenovulum agarivorans DS-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH08998.1, ECO:0000313|Proteomes:UP000019276};
RN [1] {ECO:0000313|EMBL:EWH08998.1, ECO:0000313|Proteomes:UP000019276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH08998.1,
RC ECO:0000313|Proteomes:UP000019276};
RX PubMed=24604650;
RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL Genome Announc. 2:e00144-14(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:EWH08998.1}.
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DR EMBL; ARZY01000031; EWH08998.1; -; Genomic_DNA.
DR RefSeq; WP_035015559.1; NZ_ARZY01000031.1.
DR AlphaFoldDB; W7QLJ4; -.
DR STRING; 1328313.DS2_14529; -.
DR eggNOG; COG2234; Bacteria.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000019276; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019276}.
FT DOMAIN 260..444
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 477 AA; 52796 MW; D1A2933509D63AFE CRC64;
MQKLLKTKTA WLSLISIISL VKVSFAAESL QMIEKIKNQA LSDDYAYHQI EAITTEIGAR
PLGSAKELNA LKWLEQQLTE LSVGHLSKQP LKVRNWQRIS ASAQVISPYK HELVIESLGG
SVATPAEGLE AEVIKINNFD HLNSVEADKL KDKIVYISRK LDEHSPAEDY LNMQRIRQKG
AIIAANKGAK ALIIRSQTTD KSRTAHTGAV RYHSNSPQIP AAAISPADAD LLDRLFARNL
PVALLINLQN SESRWVDTYN LIATLSADHS QNNPNKVVFI AHIDSWDLGT GALDNAAGIG
IGLGIIKQLI QFQDKLKHDI EIVFVTAAQF NQLGIKTYIK HLNDKHIVVA TEADLGGESI
FRLDTNIDES ALKLADKIHT LTTDLAIERG HNASGGATNT QHMLALDIPI FNWVQKTDNY
FKYLHSANDT FDKISLESIQ QNVATYSIFL FSVANEGLIF SNKVTEHEQP TETTVTQ
//
