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Database: UniProt
Entry: A0A372RBS0_9GLOM
LinkDB: A0A372RBS0_9GLOM
Original site: A0A372RBS0_9GLOM 
ID   A0A372RBS0_9GLOM        Unreviewed;       246 AA.
AC   A0A372RBS0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   08-NOV-2023, entry version 18.
DE   RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE            EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
DE   Flags: Fragment;
GN   ORFNames=C1646_606514 {ECO:0000313|EMBL:RGB37422.1};
OS   Rhizophagus sp. MUCL 43196.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB37422.1, ECO:0000313|Proteomes:UP000263633};
RN   [1] {ECO:0000313|EMBL:RGB37422.1, ECO:0000313|Proteomes:UP000263633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB37422.1,
RC   ECO:0000313|Proteomes:UP000263633};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) 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:RGB37422.1}.
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DR   EMBL; QKKE01000121; RGB37422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372RBS0; -.
DR   STRING; 1803374.A0A372RBS0; -.
DR   InParanoid; A0A372RBS0; -.
DR   Proteomes; UP000263633; 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:UP000263633}.
FT   DOMAIN          22..246
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51975"
FT   BINDING         28
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         29
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         135
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RGB37422.1"
FT   NON_TER         246
FT                   /evidence="ECO:0000313|EMBL:RGB37422.1"
SQ   SEQUENCE   246 AA;  28144 MW;  EC7799AD747FC1DC CRC64;
     PMTESYTYHS PTPTILLETQ KPCILGVDEA GRGPVLGPMC FGVAYCAISE YEELIDEEYK
     DSKKLDEKKR ESLLQRIINN QDNVGWGVRS LSPQDISTMT IRDKINLNVQ SHSSTIQLIN
     DVIITGVNIK KIYVDTVGPP EKYKDLLAAQ FPQQEIVVEK AADDKFPIVS AASICAKVTR
     DHILRDWSFI EENLTDPDLY KYGSGYPNEK TRLWLERNVY PNLFGFYPSI VRWHWKPARQ
     ILYNKG
//
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