ID   RNH_MIMIV               Reviewed;         229 AA.
AC   Q5UPY1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Probable ribonuclease H;
DE            Short=RNase H;
DE            EC=3.1.26.4;
GN   Name=RNH1; OrderedLocusNames=MIMI_R299;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
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   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 divalent metal ion per subunit. May bind a second metal
CC       ion at a regulatory site, or after substrate binding. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50571.1; -; Genomic_DNA.
DR   SMR; Q5UPY1; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00075; RNase_H; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..229
FT                   /note="Probable ribonuclease H"
FT                   /id="PRO_0000195439"
FT   DOMAIN          42..164
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         60
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   229 AA;  26195 MW;  55B6DB4DBBD2780F CRC64;
     MLSLIVLLEK ETLRFSQMVL AWGNGRVGAS GGIGIHFPNG ELQDISLEFD KGCCTNQRTE
     LYAILYAIQY IDDNFDLNKC KVMIKTDSTY SVNSITKWAE GHSRNDWCKR TGEPIANREF
     IQEIYEYYQN FNIDFEWVEA HTGQTDSESI ANAQADFLAN SAAKRAARDK KICRPSSSGS
     KRNSREFYCE KSSKQVYNTP YRSKSRASIN GFPIDDDFEI ELVKRRSDN