AMZ2_MACFA
ID AMZ2_MACFA Reviewed; 360 AA.
AC Q4R684;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Archaemetzincin-2;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8TXW1};
DE AltName: Full=Archeobacterial metalloproteinase-like protein 2;
GN Name=AMZ2; ORFNames=QtsA-18820;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE01391.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB169305; BAE01391.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q4R684; -.
DR SMR; Q4R684; -.
DR STRING; 9541.XP_005584824.1; -.
DR MEROPS; M54.002; -.
DR eggNOG; ENOG502QVTZ; Eukaryota.
DR Proteomes; UP000233100; 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_0000159618"
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; 41169 MW; 50A67E01A43C6A3B CRC64;
MQIIRHSEQT LKTALISKNP VLVSQYEKLD AGEQRLMNEA FQPASDLFGP ITLHSPSDWI
TSHPEAPQDF EQFFSDPYRK TPSPDKRSVY IQAIGSLGNT RIISEEYIKW LTGYCKAYFY
GLRVKLLEPV PVSATRCSFR VNENTQNLQI HAGDILKFLK KKKPEDAFCI VGITMIDLYP
RDSWNFVFGQ ASLTDGVGIF SFARYGSDFY SMRYEGKVKK LKKTSSSDYS IFNNYYIPEI
TSVLLLRSCK TLTHEIGHIF GLRHCQWLAC LMQGSNHLEE SDRRPLNLCP ICLRKLQCAV
GFSIVERYKA LVRWIDDESS GTPGATPEHS REGNGNLPKP VEAFKEWKEW IIKCLAVLQK