ID   U2VJY1_9ACTN            Unreviewed;       587 AA.
AC   U2VJY1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Carboxypeptidase Taq M32 metallopeptidase {ECO:0000313|EMBL:ERL12851.1};
DE            EC=3.4.17.19 {ECO:0000313|EMBL:ERL12851.1};
GN   ORFNames=HMPREF1248_1606 {ECO:0000313|EMBL:ERL12851.1};
OS   Coriobacteriaceae bacterium BV3Ac1.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae.
OX   NCBI_TaxID=1111135 {ECO:0000313|EMBL:ERL12851.1, ECO:0000313|Proteomes:UP000016652};
RN   [1] {ECO:0000313|EMBL:ERL12851.1, ECO:0000313|Proteomes:UP000016652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3AC1 {ECO:0000313|Proteomes:UP000016652};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:ERL12851.1}.
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DR   EMBL; AWUP01000006; ERL12851.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2VJY1; -.
DR   PATRIC; fig|1111135.3.peg.720; -.
DR   eggNOG; COG2317; Bacteria.
DR   Proteomes; UP000016652; Unassembled WGS sequence.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   PRINTS; PR00998; CRBOXYPTASET.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ERL12851.1};
KW   Hydrolase {ECO:0000313|EMBL:ERL12851.1};
KW   Protease {ECO:0000313|EMBL:ERL12851.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016652}.
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  65939 MW;  11EB2B6C81A49B4A CRC64;
     MSNKLPSFMK QSHDEQKNAQ HTDEEKLQQT AEVMSASQQS LDLDEPDSMA ITTEEKPHRE
     VPAGSLPTLP GIPGIPPLAA DAAVPNPRAD LEALDKLERH LYAHRYATVG MSCYGMSIDP
     EDATADRGEA LAILQEEAQE LLCSPATGAL LDRLSTATAL ELENDTQRAQ VRILKRDRVQ
     LVDVPADEQA AFTRLVTESD DVWHKAKAAN DWGSFAPYLD RITESMRRLA NYKKPGVNAY
     DVWLDEFEQG SSTAFYDRFF EQVKELVVPL LAEVSAARRK PSHRLVEGHF DERRQWEVAT
     DLARIEGLSF QSLFLTKTEH PFSDALTTNY AVIAAHVYED DVFSNVFTML HEGGHALYEQ
     GVNPEYNYTS LKGGTSSGMH EAQSRFFENY VGRSEAFSGP LLEILRRHFP GHFNRVSARQ
     LYLAANVVMP QPIRVEADEL TYPLHILVRY ELEQLLMSGE AKAADIPDLW AQKYREYLGV
     RVPDATHGAL QDTHWADGLI GYFPTYALGG AYGAQFRAAM ISEGMDWEGV IASGNLAPIR
     EWLRSHIWHY GRSRDPKDII LAATGEPFVT RHYTDYLTQK FSSIYGL
//