ID   A0A0Q8V8T1_9ACTN        Unreviewed;       649 AA.
AC   A0A0Q8V8T1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Peptidase M3 {ECO:0000313|EMBL:KRC53563.1};
GN   ORFNames=ASE19_14645 {ECO:0000313|EMBL:KRC53563.1};
OS   Nocardioides sp. Root79.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC53563.1, ECO:0000313|Proteomes:UP000051414};
RN   [1] {ECO:0000313|EMBL:KRC53563.1, ECO:0000313|Proteomes:UP000051414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root79 {ECO:0000313|EMBL:KRC53563.1,
RC   ECO:0000313|Proteomes:UP000051414};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC53563.1, ECO:0000313|Proteomes:UP000051414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root79 {ECO:0000313|EMBL:KRC53563.1,
RC   ECO:0000313|Proteomes:UP000051414};
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:KRC53563.1}.
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DR   EMBL; LMIP01000011; KRC53563.1; -; Genomic_DNA.
DR   RefSeq; WP_056896939.1; NZ_LMIP01000011.1.
DR   AlphaFoldDB; A0A0Q8V8T1; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000051414; 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; cd06455; M3A_TOP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
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; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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   Reference proteome {ECO:0000313|Proteomes:UP000051414};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          213..641
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   COILED          139..166
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   649 AA;  72986 MW;  8C398177246BADCF CRC64;
     MTLDPLVLPT APDAWPDWIR DRSSAELARA TELVDGLRST TPSDPIDVLR QWDRAGSHLG
     NVAAFGSLLG NVHPDERARE LADAAEQEAS RLGTQWSLDR ELYDVFAAID PGAVAGDPLA
     VRLLEKVRAD FRRSGVDKDE ATRERIAAVR ERITELDQEF SRVTRDDVRT IRVRPEQLAG
     MPADWLEAHP ADDDGLVTVT TDYPDSVPVR MFAHDQDVRR DITIAFLERG WPATEELLTE
     LFDLRHELAT TVGYADWPSY DADVKMIGEG PAIPAFIDRI TEAAEEPMQR DLGQLLERYR
     RDFPSATEVP GYDYQYYAEL VRSERYDVDS QRVRTFFDFG KVRQGLLEVT GRLFDLSYEP
     VDVPVWHEDV TAYEVVRAGG RIGRIYLDLH PREGKYKHAA QFTLTDGVAG EQLPEGVLVC
     NFSRGLMEHD HVVTLFHEFG HLLHHVLAGH GDWFRFAGVA TEWDFVEAPS QMLEEWAWHA
     DVLRSFASDE SGEPIPADLV AAMRAADDYG KGIYARTQMF YAAMSYWFHA DRGLAQVPDL
     TERMIELQGR YAALPYLPGT HMFASFGHLG GYSSAYYTYM WSLVIAKDMF SAFDPDGTGD
     LFAAAAIDMA HRYRDAVLAR GGEADAADLV ADFLGRPFAF DAYAAWLAR
//