ID V4XZK3_9ARCH Unreviewed; 481 AA.
AC V4XZK3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=A07HR67_01058 {ECO:0000313|EMBL:ESS04072.1};
OS uncultured archaeon A07HR67.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412871 {ECO:0000313|EMBL:ESS04072.1, ECO:0000313|Proteomes:UP000030660};
RN [1] {ECO:0000313|Proteomes:UP000030660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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; KI543165; ESS04072.1; -; Genomic_DNA.
DR AlphaFoldDB; V4XZK3; -.
DR STRING; 1412871.A07HR67_01058; -.
DR PATRIC; fig|1412871.3.peg.1100; -.
DR Proteomes; UP000030660; Unassembled WGS sequence.
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; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
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; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:ESS04072.1};
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:ESS04072.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000313|EMBL:ESS04072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030660}.
FT DOMAIN 135..223
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 255..437
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 51005 MW; 7BCAC3AEF16416ED CRC64;
MSDEAADDAA TSDADGEYTG TDTDAVERVR ERCAEFAPAL GRTWTDDDPW RFLTDLTALG
SRMAGSDGER RAAAVVADAF ERAGLEDVRT DPFELTAWER GDADLRVRVQ SRDDTERTRE
FEALALPYSP SGRIEGELVD VGDGTPAEVD AADVAGRIAV ASTTTPPGSR FVHRMEKFGH
AIEAGAKGFV FANHLDGQLP PTGSLTFGDE AEAVAVGVST ETGGWLREYA ANTPGPAASV
ELDVTAATHV AESQNVIGRA GPETDERLLL LAHYDGHDIA EAALDNGCGI ATAVTAAGIL
TEATLPIGVD VVAVGCEEVG LLGAERLAAT TALDRVRGVV NVDGAGRFRT LRALTHTSTA
ARSVAEAVST ATRQPIEVKT EPHPFSDQWP FVRQGVPALQ LHSDSGERGR GWGHTHADTR
DKVDDRNVRE HGMLAALLVA EFAAADRDPA RLDTDALADA FRDAGFETGM RAADLWPAAW
E
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