ID A0A1M6E630_9CLOT Unreviewed; 256 AA.
AC A0A1M6E630;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02745975_00663 {ECO:0000313|EMBL:SHI80901.1};
OS Geosporobacter subterraneus DSM 17957.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Geosporobacter.
OX NCBI_TaxID=1121919 {ECO:0000313|EMBL:SHI80901.1, ECO:0000313|Proteomes:UP000184536};
RN [1] {ECO:0000313|EMBL:SHI80901.1, ECO:0000313|Proteomes:UP000184536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17957 {ECO:0000313|EMBL:SHI80901.1,
RC ECO:0000313|Proteomes:UP000184536};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQZV01000007; SHI80901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6E630; -.
DR STRING; 1121919.SAMN02745975_00663; -.
DR OrthoDB; 9803420at2; -.
DR Proteomes; UP000184536; 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}.
FT DOMAIN 75..256
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
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 82
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 173
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 256 AA; 28856 MW; 3459BB8431B83CF8 CRC64;
MNFRAMTGKQ IEDFIKTQGM ESYGLFVPQL IEDERAAVQK LGQKLQKKLV KYEDERKRVA
GLWTYEMELA KEGYRMIAGL DEAGRGPLAG PVVAAAVILP SDLFIEGIND SKKISEKKRD
ELFDIIYEHA LAVGVGIVNH DVIDEINILR ATERAMVEAV QNLKIKPDSL LIDAVKVADI
NIRQQSIIKG DQKSISIAAA SVIAKVTRDR IMNQYHEAYP QYGFASHKGY GTKEHYESIH
RYGIIPIHRR SFLSNL
//