ID   AMZA_NANEQ              Reviewed;         170 AA.
AC   Q74M83;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Archaemetzincin {ECO:0000255|HAMAP-Rule:MF_01842};
DE            EC=3.4.-.- {ECO:0000255|HAMAP-Rule:MF_01842};
GN   Name=amzA {ECO:0000255|HAMAP-Rule:MF_01842}; OrderedLocusNames=NEQ451;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
CC   -!- FUNCTION: Probable zinc metalloprotease whose natural substrate is
CC       unknown. {ECO:0000255|HAMAP-Rule:MF_01842}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01842};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the
CC       other seems to have a structural role. {ECO:0000255|HAMAP-
CC       Rule:MF_01842};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01842}.
CC   -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01842}.
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DR   EMBL; AE017199; AAR39295.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74M83; -.
DR   SMR; Q74M83; -.
DR   EnsemblBacteria; AAR39295; AAR39295; NEQ451.
DR   KEGG; neq:NEQ451; -.
DR   HOGENOM; CLU_108521_1_0_2; -.
DR   OMA; KDRGQYH; -.
DR   Proteomes; UP000000578; Chromosome.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd11375; Peptidase_M54; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   HAMAP; MF_01842; Archaemetzincin; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR012962; Pept_M54_archaemetzincn.
DR   InterPro; IPR012091; Pept_M54_archaemetzncn_arc/bac.
DR   PANTHER; PTHR15910; PTHR15910; 1.
DR   Pfam; PF07998; Peptidase_M54; 1.
DR   PIRSF; PIRSF005785; Zn-prot_arch; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..170
FT                   /note="Archaemetzincin"
FT                   /id="PRO_0000159628"
FT   ACT_SITE        111
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
SQ   SEQUENCE   170 AA;  20198 MW;  2606C6A1DD08944B CRC64;
     MLLYLVNFQS MWANYVLELL KDAFAFKIKA KELDIPLAAY NPFRKQFSAQ LLLDYVVERY
     KDGLVFAIID EDIYDSNYNF VFGLAYPFRG AIVSTYRLKN FERIKKEVLH EMGHVFGLGH
     CNNYCVMRFS NSVFEVDEKP DKYCENCYRE ILNNGFYVNP KYVIFKENYN