ID A0A218P9N7_9EURY Unreviewed; 348 AA.
AC A0A218P9N7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Peptidase M42 {ECO:0000313|EMBL:ASJ07488.1};
GN ORFNames=A3L08_09245 {ECO:0000313|EMBL:ASJ07488.1};
OS Thermococcus pacificus.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=71998 {ECO:0000313|EMBL:ASJ07488.1, ECO:0000313|Proteomes:UP000197418};
RN [1] {ECO:0000313|EMBL:ASJ07488.1, ECO:0000313|Proteomes:UP000197418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P-4 {ECO:0000313|EMBL:ASJ07488.1,
RC ECO:0000313|Proteomes:UP000197418};
RA Oger P.M.;
RT "Complete genome sequence of Thermococcus pacificus type strain P4.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; CP015102; ASJ07488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218P9N7; -.
DR KEGG; tpaf:A3L08_09245; -.
DR OrthoDB; 30642at2157; -.
DR Proteomes; UP000197418; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 348 AA; 38144 MW; CA990E179B97D8B5 CRC64;
MVDFELLKRI IEAPGVTGYE FLGVRDVVIE AFKPYVDEIK VDKLGNVIAH KKGSGPKVML
AGHMDQIGLM VTHIEKNGFL RVAPVGGVDP RTLIAQRFKV WVGPNEYIYG VGGSVPPHIQ
KPEERSKAPT WDQVFIDVGA ESKEEAEEMG VKIGTVITWD GRLERLGKHR LVSIAHDDRI
AVYILVEAAR QLAKTDADVY FVATVQEEVG LRGAKVSAFG IDPDYGFALD VTIAADVPGT
PEHKQVTQLG KGVAIKIMDR SVICHPTIVR WMEELAKKHE IPYQWDILLG GGTDAGAIHL
NKAGVPTGGI SIPARYIHSN TEVVDERDVD AAVKLTVKVL EEIPELKL
//