ID T1A6V5_9ZZZZ Unreviewed; 333 AA.
AC T1A6V5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Oligopeptidase A {ECO:0000313|EMBL:EQD36619.1};
DE Flags: Fragment;
GN ORFNames=B1B_16450 {ECO:0000313|EMBL:EQD36619.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD36619.1};
RN [1] {ECO:0000313|EMBL:EQD36619.1}
RP NUCLEOTIDE SEQUENCE.
RA Mendez C., Richter M., Ferrer M., Sanchez J.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQD36619.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA Ferrer M.;
RT "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT along an acid mine drainage.";
RL ISME J. 8:1259-1274(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040}.
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:EQD36619.1}.
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DR EMBL; AUZY01010944; EQD36619.1; -; Genomic_DNA.
DR AlphaFoldDB; T1A6V5; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045666; OpdA_N.
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 Pfam; PF19310; TOP_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 2..79
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 153..330
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT NON_TER 333
FT /evidence="ECO:0000313|EMBL:EQD36619.1"
SQ SEQUENCE 333 AA; 36910 MW; BCEAA7E8ED4A3FF4 CRC64;
MAHLHAVADT AELRAAYAEA EQRMTKVQAR LGQHRGLHEA VRAVRERADF AQLGAAERAL
VEHTLRDFRL SGVALEEPAR TRFRAIAQEL SQLGTGFEEA VLDAGEAWHE HVTDERDLDG
LPPSARDILA SYAREAGLDG FLITLRQPAV QAVLTHADNR ALRERVYWAW NTRASDQGPQ
AGEYDNSARI AQILALRHEA AQLLGFADAA ELSLADKMAP DVATVRAFLD DLVQRARPRG
REEREALRAY AAAELALPNL ESWDVAWAAE KLRAARHALD EEQLKPYFPL PQVLDGLFAI
LARVFGISLR EPGGASVWHP DVRYAQVFDA DGR
//
