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Database: UniProt
Entry: Q5JHA5_THEKO
LinkDB: Q5JHA5_THEKO
Original site: Q5JHA5_THEKO 
ID   Q5JHA5_THEKO            Unreviewed;       337 AA.
AC   Q5JHA5;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Deblocking aminopeptidase {ECO:0000313|EMBL:BAD84964.1};
GN   OrderedLocusNames=TK0775 {ECO:0000313|EMBL:BAD84964.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD84964.1, ECO:0000313|Proteomes:UP000000536};
RN   [1] {ECO:0000313|EMBL:BAD84964.1, ECO:0000313|Proteomes:UP000000536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC   {ECO:0000313|Proteomes:UP000000536};
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD84964.1; -; Genomic_DNA.
DR   RefSeq; WP_011249726.1; NC_006624.1.
DR   AlphaFoldDB; Q5JHA5; -.
DR   STRING; 69014.TK0775; -.
DR   EnsemblBacteria; BAD84964; BAD84964; TK0775.
DR   GeneID; 78447290; -.
DR   KEGG; tko:TK0775; -.
DR   PATRIC; fig|69014.16.peg.755; -.
DR   eggNOG; arCOG01518; Archaea.
DR   HOGENOM; CLU_053520_0_0_2; -.
DR   InParanoid; Q5JHA5; -.
DR   OrthoDB; 84932at2157; -.
DR   PhylomeDB; Q5JHA5; -.
DR   BRENDA; 3.4.11.B6; 5246.
DR   Proteomes; UP000000536; 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   ECO:0000313|EMBL:BAD84964.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000536}.
FT   ACT_SITE        210
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         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   337 AA;  37202 MW;  074F8682EBF98F13 CRC64;
     MERVVEILKE ILEIPSPTGY TREVMEHIEK KLTEAGIKTY YTNKGALIAG NHPEPELVIA
     AHVDTLGAMV KGILPDGHLS FTRIGGLLLP AFEGEYCTII TRSGKRYRGT LLLKNPSVHV
     NKEAGKKERT EENMYIRLDA EVEKKEDTEK LGIRPGDFIA FDPKFEYVNG FVKAHFLDDK
     ASVAVLIDLM LDLSQTLEKL PVAFFFSPYE EVGHGGSAGY PKSTKELLVV DMGVVGEGVA
     GKETAVSIAA KDSSGPYDYE MTTKLIELAE KRGIPYTVDV FPYYGSDGSA ALRAGWDFRV
     ALIGQGVHAS HGMERTHVKG MLATKELIRA YIEEKFL
//
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