ID A0A0M4M7G8_9SPHN Unreviewed; 538 AA.
AC A0A0M4M7G8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=AMC99_01102 {ECO:0000313|EMBL:ALE16398.1};
OS Altererythrobacter epoxidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=361183 {ECO:0000313|EMBL:ALE16398.1, ECO:0000313|Proteomes:UP000057938};
RN [1] {ECO:0000313|EMBL:ALE16398.1, ECO:0000313|Proteomes:UP000057938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7731 {ECO:0000313|EMBL:ALE16398.1,
RC ECO:0000313|Proteomes:UP000057938};
RA Li Z., Cheng H., Huo Y., Xu X.;
RT "Complete genome sequence of a benzo[a]pyrene-degrading bacterium
RT Altererythrobacter epoxidivorans CGMCC 1.7731T.";
RL Submitted (SEP-2015) 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; CP012669; ALE16398.1; -; Genomic_DNA.
DR RefSeq; WP_061923779.1; NZ_CP012669.1.
DR AlphaFoldDB; A0A0M4M7G8; -.
DR STRING; 361183.AMC99_01102; -.
DR KEGG; aep:AMC99_01102; -.
DR PATRIC; fig|361183.4.peg.1075; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000057938; Chromosome.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:ALE16398.1};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000313|EMBL:ALE16398.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000313|EMBL:ALE16398.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000057938};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..538
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005798202"
FT DOMAIN 287..503
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 511..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 58877 MW; D475C7B4DD45FB9E CRC64;
MRNKRFVASL LAASTLLAVP GSLFAGEPDK TAQIIDEGLA RSEAQILAHE LLDQIGPRLT
NSTNMRKAEA WAVEKMQKLG LKNVHKEGFD FGRGWDLISS DVRMTSPRPI ELTAIPVAWT
PPTNGPVEAE IIVAPISKKE HFDAYRGQLN GKIVLLTIPG MGDEPTTPAF KRLDQSDISK
NDEIDLPSFD PGAIERWRKR SEFAQELDDF LASEGAVAWV KKARRDGKLL HGEGSGYEVG
KTPKLPGIEM AAEDYRRLAR LAKTGPAPKL TINSNVRFVD GDTQGYNIIG EIPGSDPKAG
YVMAGAHFDS WLAGDGAVDN GAGSITILEA ARILQETGVK PKRTIKFVLW SGEEQGLHGS
LGYVRRHLVA REGEEALTPG NVYREWRYLF PVTAKPGYSE MKAYFNMDNG SGKLRGIYAE
GNVGAERLLR SWLAPFGDLG ASSVVAGETG GTDHVFFNAI GLPAFQFIQD PLDYGARLHH
TNIDTFDHLR PDDLRQAATV MAGVLMAAAN DKEELPRKPL PEPQSASDPF KYDYPETD
//
