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Database: UniProt
Entry: A0A0P7BAV2_9HYPO
LinkDB: A0A0P7BAV2_9HYPO
Original site: A0A0P7BAV2_9HYPO 
ID   A0A0P7BAV2_9HYPO        Unreviewed;       331 AA.
AC   A0A0P7BAV2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE            EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN   ORFNames=AK830_g7119 {ECO:0000313|EMBL:KPM39441.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM39441.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM39441.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM39441.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000256|RuleBase:RU003515}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|PROSITE-
CC         ProRule:PRU01319, ECO:0000256|RuleBase:RU003515};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC       Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC       the absence of substrate. May bind a second metal ion after substrate
CC       binding. {ECO:0000256|PROSITE-ProRule:PRU01319};
CC   -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC       {ECO:0000256|ARBA:ARBA00007058}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPM39441.1}.
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DR   EMBL; LKCW01000107; KPM39441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7BAV2; -.
DR   STRING; 78410.A0A0P7BAV2; -.
DR   OrthoDB; 117476at2759; -.
DR   Proteomes; UP000050424; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07181; RNase_HII_eukaryota_like; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 1.10.10.460; Ribonuclease hii. Domain 2; 1.
DR   InterPro; IPR004649; RNase_H2_suA.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00729; ribonuclease HII; 1.
DR   PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR   PANTHER; PTHR10954:SF7; RIBONUCLEASE H2 SUBUNIT A; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS51975; RNASE_H_2; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW   ProRule:PRU01319};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01319};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01319};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW   ProRule:PRU01319}; Reference proteome {ECO:0000313|Proteomes:UP000050424}.
FT   DOMAIN          50..285
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51975"
FT   BINDING         56
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         57
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         170
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ   SEQUENCE   331 AA;  35218 MW;  C34B91AEDFBD2F94 CRC64;
     MADSQSSAST FIPPSVHRPE LLSGASFSHF SAVPAALLPA DASDPASAPP CCLGVDEAGR
     GPVLGPMVYG VFYLPLPLSD PLLRDTHHFD DSKVLTPAVR SDLMRALCEP GSDLHDSCGW
     ATASLSARDI SANMLRPSAY NLNAQAMDAT VDLIKAVYAM GVNVQEIYVD TIGQPAPYQA
     KLQRIFPTAK ITVAKKADSL YPSVSAASVC AKVTRDAALE VMYEARALED GVVTEEGGMA
     WGSGYPSDGR CVGWMRGNVH PVFGWGPECR FSWGTAKDML EAKGSGVKVE WPAEDDGETS
     RLTDFFLSGD EDKESSELGS WFGTPAGLEA F
//
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