ID A0A218P1M5_THECE Unreviewed; 339 AA.
AC A0A218P1M5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Glucanase {ECO:0000313|EMBL:ASI98830.1};
GN ORFNames=A3L02_04270 {ECO:0000313|EMBL:ASI98830.1};
OS Thermococcus celer Vu 13 = JCM 8558.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1293037 {ECO:0000313|EMBL:ASI98830.1, ECO:0000313|Proteomes:UP000197156};
RN [1] {ECO:0000313|EMBL:ASI98830.1, ECO:0000313|Proteomes:UP000197156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vu 13 {ECO:0000313|EMBL:ASI98830.1,
RC ECO:0000313|Proteomes:UP000197156};
RA Oger P.M.;
RT "Complete genome sequence of Thermococcus celer.";
RL Submitted (MAR-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; CP014854; ASI98830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218P1M5; -.
DR KEGG; tce:A3L02_04270; -.
DR OrthoDB; 84932at2157; -.
DR Proteomes; UP000197156; 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; cd05657; M42_glucanase_like; 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:SF7; AMINOPEPTIDASE YHFE-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 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 339 AA; 37565 MW; 6243A9A552BAB9DF CRC64;
MERVIEILRE ILEIPSPTGY TREVMEHIEG KLNEAGIKTR YTNKGALIAH NHPEPELVIA
AHVDTLGAMV KGILPDGHLS FTRVGGLNLP AFEGEYCTVI TRSGRRYRGT LLLKNPSVHV
NKDAGKKERK EENMYIRLDE PVEKREDTEK LGIRPGDFIA FDPKFEYVNG FVKAHFLDDK
ASAAILIDLM LDMGAETLER LPVAFFFSPY EEVGHGGSAG YPESMRELLV VDMGVVGEGV
AGKETAVSIA AKDSSGPYDY EMTTKLIELA EKRDIPYVVD VFPYYGSDGS AALRAGWDVR
VALIGQGVHA SHGMERTHIK GILATKELIR AYIEERFEG
//
