GenomeNet

Database: UniProt
Entry: M1JDR7_9CREN
LinkDB: M1JDR7_9CREN
Original site: M1JDR7_9CREN 
ID   M1JDR7_9CREN            Unreviewed;       490 AA.
AC   M1JDR7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=SacRon12I_08070 {ECO:0000313|EMBL:AGE73845.1};
OS   Sulfolobus acidocaldarius Ron12/I.
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=1028567 {ECO:0000313|Proteomes:UP000011280};
RN   [1] {ECO:0000313|EMBL:AGE73845.1, ECO:0000313|Proteomes:UP000011280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ron12/I {ECO:0000313|EMBL:AGE73845.1,
RC   ECO:0000313|Proteomes:UP000011280};
RX   PubMed=22418622; DOI=10.1038/ismej.2012.20;
RA   Mao D., Grogan D.;
RT   "Genomic evidence of rapid, global-scale gene flow in a Sulfolobus
RT   species.";
RL   ISME J. 6:1613-1616(2012).
CC   -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC       sequentially from the C-terminus, including neutral, aromatic, polar
CC       and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity,
CC         except for -Pro.; EC=3.4.17.19;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC   -!- SIMILARITY: Belongs to the peptidase M32 family.
CC       {ECO:0000256|PIRNR:PIRNR006615}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002818; AGE73845.1; -; Genomic_DNA.
DR   RefSeq; WP_011278473.1; NC_020247.1.
DR   AlphaFoldDB; M1JDR7; -.
DR   GeneID; 78442002; -.
DR   KEGG; sacr:SacRon12I_08070; -.
DR   PATRIC; fig|1028567.7.peg.1586; -.
DR   HOGENOM; CLU_032916_1_1_2; -.
DR   Proteomes; UP000011280; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd06460; M32_Taq; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF02074; Peptidase_M32; 1.
DR   PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR   PRINTS; PR00998; CRBOXYPTASET.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000313|EMBL:AGE73845.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000256|PIRSR:PIRSR006615-1};
KW   Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW   Protease {ECO:0000256|PIRNR:PIRNR006615};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        264
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   490 AA;  57339 MW;  B7EA868BE63240AA CRC64;
     MKRFENLKEL LAEYKKLWSL QYAESLMGWD IETYMPEDDA MTRGEVISTF SEIKREIYQK
     LGKIIERYEG KEGLNDEERG ILRVLGRDYK YYSKIPLEII QQIERVRSEA TVVWRQAKAK
     SDYSMFKPYL EKIKDLQIKI AEYWGYEDHP YNALLDLNEE GFSIRDGDRI FSRLLPELSD
     IMKKVSEKGY FPKSHELEEV SYDIGRMKVV NEEVIKILEM PKGKFRLDIS AHPFTVRISA
     DDVRITTRYE GKDFRSTLFS VVHECGHAIY ELGIDRELEG TPIGGGVSMG IHEAQSRFWE
     NIIGRSREFV SLIYPKLKQN LDFLSKYNED DIYRYFNIVR PSFIRVDADE VTYNFHIAVR
     YEIEKRLIGG EIKVDEIPSL WSELMEKYLG ITPKNDAEGA LQDIHWTGGF GYFPAYTLGN
     VVSGIVYSKT PNLYNLLREG KIGEIKTIMT EKIYKYGATY SPKDLLRKTF GEEYNPEGLI
     LYLRHKYLKS
//
DBGET integrated database retrieval system