ID A0A1Z2TN13_9EURY Unreviewed; 348 AA.
AC A0A1Z2TN13;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Peptidase M42 {ECO:0000313|EMBL:ASA77840.1};
GN ORFNames=CDI07_05860 {ECO:0000313|EMBL:ASA77840.1};
OS Thermococcus sp. 5-4.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=2008440 {ECO:0000313|EMBL:ASA77840.1, ECO:0000313|Proteomes:UP000196843};
RN [1] {ECO:0000313|EMBL:ASA77840.1, ECO:0000313|Proteomes:UP000196843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-4 {ECO:0000313|EMBL:ASA77840.1,
RC ECO:0000313|Proteomes:UP000196843};
RX PubMed=28628615; DOI=10.1371/journal.pgen.1006847;
RA Cossu M., Badel C., Catchpole R., Daniele G., Marguet E., Barbe V.,
RA Forterre P., Oberto J.;
RT "Flipping chromosomes in deep-sea archaea.";
RL PLoS Genet. 13:e1006847-e1006847(2017).
RN [2] {ECO:0000313|Proteomes:UP000196843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-4 {ECO:0000313|Proteomes:UP000196843};
RA Cossu M., Badel C., Catchpole R., Daniele G., Marguet E., Barbe V.,
RA Forterre P., Oberto J.;
RT "Flipping Chromosomes in Deep-Sea Archaea.";
RL PLoS Genet. 0:0-0(2017).
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; CP021848; ASA77840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2TN13; -.
DR KEGG; thh:CDI07_05860; -.
DR OrthoDB; 30642at2157; -.
DR Proteomes; UP000196843; 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; 38203 MW; 79EB1C17202DDBC3 CRC64;
MVDYELLKRI IEAPGVSGYE FLGVRDVVIE AFKPYVDEIT VDKLGNVIAH KKGKGPKVML
AGHMDQIGLM VTHIEKNGFL RVAPVGGVDP RTLIAQRFKV WIGPNEFVYG VGGSVPPHIQ
KPEQRNKAPT WDQVFIDIGA ESKEEAEEMG VRIGTVITWD GRLERLGKHR LVSIAHDDRI
AVYILVEAAR QLAETDADVY FVATVQEEVG LRGAKVSSFG IDPDYGFALD VTIAADVPGT
PEHKQISQLG KGVAIKIMDR SVICHPTIVR WMEEIAKKHE IPYQWDILTG GGTDAGAIHL
NKAGVPSGGI SIPARYIHSN TEVVDERDVD AAVKLTVKVL EEIPELKL
//
