ID A0A0D1WAU2_ANEMI Unreviewed; 257 AA.
AC A0A0D1WAU2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Ribonuclease HII {ECO:0000256|HAMAP-Rule:MF_00052};
DE Short=RNase HII {ECO:0000256|HAMAP-Rule:MF_00052};
DE EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00052};
GN Name=rnhB {ECO:0000256|HAMAP-Rule:MF_00052};
GN ORFNames=AF333_09910 {ECO:0000313|EMBL:KON95745.1},
GN SAMN04487909_103212 {ECO:0000313|EMBL:SDI36322.1};
OS Aneurinibacillus migulanus (Bacillus migulanus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=47500 {ECO:0000313|EMBL:KON95745.1, ECO:0000313|Proteomes:UP000037269};
RN [1] {ECO:0000313|EMBL:KON95745.1, ECO:0000313|Proteomes:UP000037269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2895 {ECO:0000313|EMBL:KON95745.1,
RC ECO:0000313|Proteomes:UP000037269};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14205 dsm 2895.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SDI36322.1, ECO:0000313|Proteomes:UP000182836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2895 {ECO:0000313|EMBL:SDI36322.1,
RC ECO:0000313|Proteomes:UP000182836};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|ARBA:ARBA00004065, ECO:0000256|HAMAP-
CC Rule:MF_00052, 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|HAMAP-
CC Rule:MF_00052, ECO:0000256|PROSITE-ProRule:PRU01319,
CC 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|HAMAP-Rule:MF_00052,
CC ECO:0000256|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00052,
CC 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|HAMAP-Rule:MF_00052, ECO:0000256|PROSITE-
CC ProRule:PRU01319};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00052}.
CC -!- SIMILARITY: Belongs to the RNase HII family.
CC {ECO:0000256|ARBA:ARBA00007383, ECO:0000256|HAMAP-Rule:MF_00052,
CC ECO:0000256|RuleBase:RU003515}.
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DR EMBL; LGUG01000004; KON95745.1; -; Genomic_DNA.
DR EMBL; FNED01000003; SDI36322.1; -; Genomic_DNA.
DR RefSeq; WP_043066003.1; NZ_LGUG01000004.1.
DR AlphaFoldDB; A0A0D1WAU2; -.
DR STRING; 47500.AF333_09910; -.
DR PATRIC; fig|47500.8.peg.6875; -.
DR OrthoDB; 9803420at2; -.
DR Proteomes; UP000037269; Unassembled WGS sequence.
DR Proteomes; UP000182836; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
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; cd07182; RNase_HII_bacteria_HII_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_00052_B; RNase_HII_B; 1.
DR InterPro; IPR022898; RNase_HII.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF18; RIBONUCLEASE HII; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00052};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00052};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00052};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00052};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00052};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00052};
KW Reference proteome {ECO:0000313|Proteomes:UP000037269}.
FT DOMAIN 74..257
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 80
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00052,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00052,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00052,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 257 AA; 28386 MW; 242893A02B040528 CRC64;
MNPGEMTIKE VKEFLLTCEN LSEEAQALFA ADMRSGVQAA FKQWHRRMEK TQQLYQRWLD
MSKHEQELWK KGYAYIAGVD EVGRGPLAGP VVTAAVILPQ DFYLPGLNDS KKVPAARREE
MYEQIMKQAV AVSVALSDAA LIDEINIFQA TLRAMQIAVQ NLSVAPDITL NDAVTIPKVS
VEQRPIIGGD GKSISIAAAS IIAKVERDRM MKEYDVQYPG YGFASNMGYG TAEHLAALRA
LGPCQIHRRS FGGVLVP
//