ID W0AAI9_9SPHN Unreviewed; 464 AA.
AC W0AAI9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=NX02_04715 {ECO:0000313|EMBL:AHE52685.1};
OS Sphingomonas sanxanigenens DSM 19645 = NX02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE52685.1, ECO:0000313|Proteomes:UP000018851};
RN [1] {ECO:0000313|EMBL:AHE52685.1, ECO:0000313|Proteomes:UP000018851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NX02 {ECO:0000313|EMBL:AHE52685.1,
RC ECO:0000313|Proteomes:UP000018851};
RA Ma T., Huang H., Wu M., Li X., Li G.;
RT "Completed genome of Sphingomonas sanxanigenens NX02.";
RL Submitted (JUL-2013) 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; CP006644; AHE52685.1; -; Genomic_DNA.
DR RefSeq; WP_025290981.1; NZ_CP006644.1.
DR AlphaFoldDB; W0AAI9; -.
DR STRING; 1123269.NX02_04715; -.
DR KEGG; ssan:NX02_04715; -.
DR PATRIC; fig|1123269.5.peg.916; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_033697_1_0_5; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000018851; Chromosome.
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:UP000018851};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..464
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004785390"
FT DOMAIN 261..444
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 464 AA; 47632 MW; 79F4913DDF5A135E CRC64;
MKQRAILPAL ALPLILAGQP ARSAPADDPV ATAATLRDKA LAGDTVAWDL VEGLTTEVGP
RMAGTEAEAR ARAWAVPRLK ALGFSNVRIE TCDMPVWTRG AERAAVTAPF PAKLAVTALG
NSAATPAEGI EAEVVAFETL ADLDAAPAGS LAGKIAFVSH AMTATQDGSS YGVFGAVRRR
GPAVAAAKGA IAIVIRSVGT DHHRNPHAGG TVFPAGSTAI PAAALSIPDA ENLQRILKRG
KPVTMRLVLT PTFSATGQSG NVIAEVPGSD PAAGIITIGG HLDSWDLATG AIDDASGVAI
TTAAAKMVMA AGKPRRTIRV VWYGAEEVGG CGGPSYLAAH RDEKHVLTAE SDFGADRVWA
VKFTLPAAAA PLGDRIARAL APIGIGRNPA PATGGADIAP LVKAGVPVID LEQDGTRYFD
IHHTPDDTLD KVDPAQLRQN VAAWTTMLWL AANAPETLAA APQK
//
