ID A0A1J5WZG6_9MICR Unreviewed; 322 AA.
AC A0A1J5WZG6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN ORFNames=A8A55_1061 {ECO:0000313|EMBL:OIR58169.1};
OS Amphiamblys sp. WSBS2006.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Amphiacanthidae;
OC Amphiamblys.
OX NCBI_TaxID=1866961 {ECO:0000313|EMBL:OIR58169.1, ECO:0000313|Proteomes:UP000182028};
RN [1] {ECO:0000313|EMBL:OIR58169.1, ECO:0000313|Proteomes:UP000182028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSBS2006 {ECO:0000313|EMBL:OIR58169.1};
RX PubMed=27694476;
RA Mikhailov K.V., Simdyanov T.G., Aleoshin V.V.;
RT "Genomic survey of a hyperparasitic microsporidian Amphiamblys sp.
RT (Metchnikovellidae).";
RL Genome Biol. Evol. 0:0-0(2016).
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=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.
CC {ECO:0000256|RuleBase:RU003515}.
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:OIR58169.1}.
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DR EMBL; MKPU01000037; OIR58169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5WZG6; -.
DR VEuPathDB; MicrosporidiaDB:A8A55_1061; -.
DR Proteomes; UP000182028; 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 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; 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 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:UP000182028}.
FT DOMAIN 17..257
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT REGION 280..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 23
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 132
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 322 AA; 37407 MW; A350F5D32F1FAA7C CRC64;
MGNEIVREKW TTDTLSRYVV GVDESGRGPV FGPLVYCGFF CDEGKYNEVL REMGVKDSKK
VSESKRKEIH TKLLDEPGVG WVVSCFSSRE LSEAMFHHEK ENVNLLSYKI VGSIITKIWR
RLNKPPSKVY LDIVGLEETY RKNITPYTGE AEVVIESDAD STYLPVSASS IIAKLVFDEE
LQRLGDIYGG YTGRDRDEYQ GGAGEREGDD QYGSGVLSDE RTKKWLDTHY DALFGYPCEF
VRLSWEPIVT LMKKNCFEVQ WFSDSTYRYS EEYFEKEKEQ KEKNRLKNKK NSERRKVKRA
EEREIKEKEK PVSQFIIPPR QK
//
