ID   A0A0Q9T955_9ACTN        Unreviewed;       694 AA.
AC   A0A0Q9T955;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN   ORFNames=ASG94_01075 {ECO:0000313|EMBL:KRF36111.1};
OS   Nocardioides sp. Soil805.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736416 {ECO:0000313|EMBL:KRF36111.1, ECO:0000313|Proteomes:UP000051356};
RN   [1] {ECO:0000313|EMBL:KRF36111.1, ECO:0000313|Proteomes:UP000051356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil805 {ECO:0000313|EMBL:KRF36111.1,
RC   ECO:0000313|Proteomes:UP000051356};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF36111.1, ECO:0000313|Proteomes:UP000051356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil805 {ECO:0000313|EMBL:KRF36111.1,
RC   ECO:0000313|Proteomes:UP000051356};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KRF36111.1}.
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DR   EMBL; LMSU01000001; KRF36111.1; -; Genomic_DNA.
DR   RefSeq; WP_056924600.1; NZ_LMSU01000001.1.
DR   AlphaFoldDB; A0A0Q9T955; -.
DR   STRING; 1736416.ASG94_01075; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000051356; Unassembled WGS sequence.
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; 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   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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          264..691
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   694 AA;  75916 MW;  4392D446A55768A2 CRC64;
     MTNTLLSPST LPFGLPDYAH LTDADYREAI EQGMSEHLAE LDAVATDDSP ATVANVLEAW
     ERSGALLTRA MNAFWVAKSA DTNDARDAIE EDMAPRLAQH SDAILLDARL YGRLTSLAAR
     RDAGEVTLDE QETHLLTERL KDFERGGIAL PEDEQARLRE LNTELATLST RFDQMLVAGR
     NAAAVHVTDE AELDGLDDGQ RAAAHEAAQD AGQDGWLLTI TNTTGQPVLG SLTHRPTRER
     VFRASAQRGL GAAGAHADDH ADDHAAATDT RAVLLTMARL RHERAVLLGY PHHAAYAAED
     GCAGSTEAVN EILGRLGPAA YGLVRARGEQ LQAHLDATDP GTTLEPWDWA YVDGQLRREE
     AALDPGALRP YLEFDRVLVE GVFAAAGALY GITFHRREDL VGYTDVARVY EVREEDGSHL
     GVVVIDPYTR PSKQGGAWMT SIVDQSHLLD DAPVVTNTCN FPPPAPGAPS LLSWDNVITL
     FHEFGHDLHG LLSDVRFPSR SGTSVPRDFV EFPSQVNEIW AYEPSLLARY AVHHETGEPM
     PAAWVEQLLA TSGKETYRYA ELLSAMLLDQ AWHQTPPDEL PSDAAGVEAF ELAALERAGV
     RYAPVPPRYR SAYFHHIFGG GYSAAYYSYL WSEIMDADTV AWFGEQGGMD RRAGEHFRRT
     LLGPGGSVDA MESYRGFRGG DPDLAHLLRR IGAE
//