ID A0A1G9XMY3_9EURY Unreviewed; 173 AA.
AC A0A1G9XMY3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Archaemetzincin {ECO:0000256|HAMAP-Rule:MF_01842};
DE EC=3.4.-.- {ECO:0000256|HAMAP-Rule:MF_01842};
GN Name=amzA {ECO:0000256|HAMAP-Rule:MF_01842};
GN ORFNames=SAMN05192554_11143 {ECO:0000313|EMBL:SDM98090.1};
OS Haloarchaeobius iranensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halorubellaceae; Haloarchaeobius.
OX NCBI_TaxID=996166 {ECO:0000313|EMBL:SDM98090.1, ECO:0000313|Proteomes:UP000199370};
RN [1] {ECO:0000313|EMBL:SDM98090.1, ECO:0000313|Proteomes:UP000199370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB21,IBRC-M 10013,KCTC 4048
RC {ECO:0000313|Proteomes:UP000199370};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable zinc metalloprotease whose natural substrate is
CC unknown. {ECO:0000256|HAMAP-Rule:MF_01842}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01842};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01842}.
CC -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000256|HAMAP-
CC Rule:MF_01842}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNIA01000011; SDM98090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9XMY3; -.
DR STRING; 996166.SAMN05192554_11143; -.
DR OrthoDB; 50281at2157; -.
DR Proteomes; UP000199370; Unassembled WGS sequence.
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; Collagenase (Catalytic Domain); 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 NCBIfam; NF033823; archmetzin; 1.
DR PANTHER; PTHR15910; ARCHAEMETZINCIN; 1.
DR PANTHER; PTHR15910:SF1; ARCHAEMETZINCIN-2; 1.
DR Pfam; PF07998; Peptidase_M54; 1.
DR PIRSF; PIRSF005785; Zn-prot_arch; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01842};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01842};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_01842}; Protease {ECO:0000256|HAMAP-Rule:MF_01842};
KW Reference proteome {ECO:0000313|Proteomes:UP000199370};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01842}.
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
SQ SEQUENCE 173 AA; 19352 MW; ADC6EE35B42170C3 CRC64;
MLVDIVPVGD VSAAVKRAAS EGLRSVYDCD VTIHEPQPLP SDAFDHGREQ YSAEEFIQLA
EQVGTGEKNI GVTPKDLFYR RRNYVFGLAY LDGSGSVVST YRLQTSSDGG FSNRSSEDIF
EDRIRKEIVH EIGHTMGLEH CDNKRCVMNF SPTVREVDVK EENLCGTCQR MVL
//
