ID   AMZ2_PONAB              Reviewed;         360 AA.
AC   Q5R4A6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Archaemetzincin-2;
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:Q8TXW1};
DE   AltName: Full=Archeobacterial metalloproteinase-like protein 2;
GN   Name=AMZ2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable zinc metalloprotease.
CC       {ECO:0000250|UniProtKB:Q8TXW1}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q8TXW1};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the
CC       other seems to have a structural role. {ECO:0000250|UniProtKB:Q8TXW1};
CC   -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000305}.
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DR   EMBL; CR861349; CAH93410.1; -; mRNA.
DR   RefSeq; NP_001127001.1; NM_001133529.1.
DR   AlphaFoldDB; Q5R4A6; -.
DR   SMR; Q5R4A6; -.
DR   MEROPS; M54.002; -.
DR   GeneID; 100174024; -.
DR   KEGG; pon:100174024; -.
DR   CTD; 51321; -.
DR   InParanoid; Q5R4A6; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd11375; Peptidase_M54; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR012962; Pept_M54_archaemetzincn.
DR   Pfam; PF07998; Peptidase_M54; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..360
FT                   /note="Archaemetzincin-2"
FT                   /id="PRO_0000159620"
FT   ACT_SITE        255
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT   BINDING         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TXW1"
FT   BINDING         292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TXW1"
SQ   SEQUENCE   360 AA;  41229 MW;  2329D5B0AEDF9D0E CRC64;
     MQIIRHSEQT LKTALISKNP VLVSQYEKLD AGEQRLMNEA FQPASDLFGP ITLHSPSDWI
     TSHPEAPQDF EQFFSDPYRK TPSPNKRSIY IQSIGSLGNT RIISEEYIKW VTGYCKAYFY
     GLRVKLLEPV PVSATRCSFR VNENTHNLQI HAGDILKFLK KKKPEDAFCV VGITMIDLYP
     RDSWNFVFGQ ASLTDGVGIF SFARYGSDFY SMRYEGKVKK LKKTSSSDYS IFDNYYIPEI
     TSVLLLRSCK TLTHEIGHIF GLRHCQWLAC LMQGSNHLEE ADRRPLNLCP ICLRKLQCAI
     GFSTVERYKA LVRWIDDESS DTPGATPEHS CEDNGNLPKP VEAFKEWKEW IIKCLAVLQK