ID   YR519_MIMIV             Reviewed;         615 AA.
AC   Q5UQ76;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Putative zinc metalloproteinase R519;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=MIMI_R519;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC   Mimivirus bradfordmassiliense.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01233, ECO:0000305}.
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DR   EMBL; AY653733; AAV50783.1; -; Genomic_DNA.
DR   RefSeq; YP_003987033.1; NC_014649.1.
DR   SMR; Q5UQ76; -.
DR   GeneID; 9925152; -.
DR   KEGG; vg:9925152; -.
DR   OrthoDB; 36309at10239; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1380.10; Neutral endopeptidase , domain2; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR042089; Peptidase_M13_dom_2.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733:SF227; FI12805P-RELATED; 1.
DR   PANTHER; PTHR11733; ZINC METALLOPROTEASE FAMILY M13 NEPRILYSIN-RELATED; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51885; NEPRILYSIN; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..615
FT                   /note="Putative zinc metalloproteinase R519"
FT                   /id="PRO_0000309202"
FT   DOMAIN          1..611
FT                   /note="Peptidase M13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   ACT_SITE        455
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        517
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   BINDING         454
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         458
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         513
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
SQ   SEQUENCE   615 AA;  73508 MW;  70D4A16942930F2E CRC64;
     MTYRSCIPQN DLECYYNPNK TKYKSTNILS SIQHKIDKEL TAYITDKTID DTFGNRMIVF
     RDSFYDKPKN SKIFRQIIHM IETSNCWYSV KFLMDNGISS LFSLGITPHH TYPKKYYPMI
     ISPILSLESK NDYQDYLALV RLKNFIGYSY DYITKYWNYK LSNKQNFIND VMEMESQLSL
     VTLTIEQQNN PFVIYNSLKW REFLEKYDVD NFWSSILGSY LKKEDYVIFD NIQYLSYLRE
     YLKNTSKNSI KNYLVYSLVK KFGLYTDLLE FYNDIVIESI NHDQIFLNMF SQYFGIYLET
     VFETRYHDKD KKEYITKMFY DMKLYLRNYF IECKFTDKTK REISLKIDNL HMVIGRQNYQ
     YDLENFPLMG NDFYENVLNL ERYYFHESIK LIGSTINKEW FSINGGMYSF EVNAYYDPIC
     NVLYIPTSII NDMTISLERD DVYNYGSIGT ILAHEIMHSL DNFGLQVNCD LSIGNKWDIS
     DYKFYLSDLR KIIQHRIKLS NYDIASSIDA LSEDISDTLG LKLSFKTYLS KFNKKIEPDN
     LSTNDKIHLQ KFFYSWTETF KNINNNNQDD HSPSYIRINA PLAHLDEFYY LYGVESQHLN
     YLDPQLRSRI LDKIN
//