ID B8JGZ9_ANAD2 Unreviewed; 717 AA.
AC B8JGZ9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Peptidyl-dipeptidase Dcp {ECO:0000313|EMBL:ACL66636.1};
DE EC=3.4.15.5 {ECO:0000313|EMBL:ACL66636.1};
DE Flags: Precursor;
GN OrderedLocusNames=A2cp1_3302 {ECO:0000313|EMBL:ACL66636.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL66636.1, ECO:0000313|Proteomes:UP000007089};
RN [1] {ECO:0000313|EMBL:ACL66636.1, ECO:0000313|Proteomes:UP000007089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP001359; ACL66636.1; -; Genomic_DNA.
DR RefSeq; WP_015934447.1; NC_011891.1.
DR AlphaFoldDB; B8JGZ9; -.
DR KEGG; acp:A2cp1_3302; -.
DR HOGENOM; CLU_001805_4_0_7; -.
DR Proteomes; UP000007089; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:ACL66636.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..717
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002875069"
FT DOMAIN 256..703
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 717 AA; 78845 MW; 6BE8E6E6D2DAFB31 CRC64;
MSALVASALA QLVLLSSPPA APARAEVPVN NPLLAPWAGP HGGVPPFDVA RVDQLAPAIE
AGMAAKLAAV EAIAADPAAP TFDNTLAAME RSGRALDRAM TVFGVFSTSM STPEFQAVER
ELAPKLAAFD DRITQNEKLF ARIAAVYDAR ETSCRTPEQK RLAWLYYTTF VRAGAKLDPA
AKQRVAAINE RLATLYTKFA QDVLADESGY TLVLEDEAAL AGLPASVRAG MAAAAATRGK
AGKWAVLNTR SSVEPFLAYS ERRDLRERVW RDFTSRGDHG DAHDTKAAIT EILKLRAERA
KLLGYPTHAH WRLEDSMAKT PGRAMALMEA VWPAAVARVR EEVADMQAVA DREGAGITIE
PWDYRFYAEK VRKAKYDLDE NEVKPYLQLE KLREAMFWVA GRLFDLHFTP AKGVPVYHPD
VRVWEVKDGK GRHVGRWYFD PYARDGKRSG AWMNAYRAQE RFDGEIPTIV SNNANFVKGK
PGEPVLVSWT DAETLFHEFG HALHGLASSV GYPSLSGTAV ARDYVEFPSQ LLERWLETPE
VLDRFARHVK TGKPLPRALV AKIQKASTFN QGFGTVEYLS AALVDLKMHL AGSTEIDPAA
FEKDTLAALG MPREVVMRHR PPHFLHVFSG DGYSAGYYSY LWADTLSTDA YEAFTEAKGP
YDRAVAARLR EHVFSAGNTV DPADAYRAFR GRDPGIGALM RKRGFPVPAA EPGAAPR
//
