RNH2_STAA8
ID RNH2_STAA8 Reviewed; 255 AA.
AC Q2FZ38;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ribonuclease HII {ECO:0000255|HAMAP-Rule:MF_00052};
DE Short=RNase HII {ECO:0000255|HAMAP-Rule:MF_00052};
DE EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00052};
GN Name=rnhB {ECO:0000255|HAMAP-Rule:MF_00052};
GN OrderedLocusNames=SAOUHSC_01215;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000255|HAMAP-Rule:MF_00052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
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:0000255|HAMAP-Rule:MF_00052};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00052}.
CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000255|HAMAP-
CC Rule:MF_00052}.
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DR EMBL; CP000253; ABD30320.1; -; Genomic_DNA.
DR RefSeq; WP_000176394.1; NZ_LS483365.1.
DR RefSeq; YP_499752.1; NC_007795.1.
DR PDB; 5Y9P; X-ray; 2.20 A; A=1-255.
DR PDBsum; 5Y9P; -.
DR AlphaFoldDB; Q2FZ38; -.
DR SMR; Q2FZ38; -.
DR STRING; 1280.SAXN108_1246; -.
DR EnsemblBacteria; ABD30320; ABD30320; SAOUHSC_01215.
DR GeneID; 3919481; -.
DR KEGG; sao:SAOUHSC_01215; -.
DR PATRIC; fig|93061.5.peg.1114; -.
DR eggNOG; COG0164; Bacteria.
DR HOGENOM; CLU_036532_2_1_9; -.
DR OMA; YPTKLHL; -.
DR PRO; PR:Q2FZ38; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR Gene3D; 3.30.420.10; -; 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; PTHR10954; 1.
DR PANTHER; PTHR10954:SF18; PTHR10954:SF18; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Manganese; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..255
FT /note="Ribonuclease HII"
FT /id="PRO_1000031209"
FT DOMAIN 72..255
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 78
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT BINDING 79
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00052"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:5Y9P"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5Y9P"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5Y9P"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:5Y9P"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:5Y9P"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5Y9P"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5Y9P"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 191..214
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:5Y9P"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:5Y9P"
SQ SEQUENCE 255 AA; 28513 MW; 6564DE7024653463 CRC64;
MTLTIKEVTQ LINAVNTIEE LENHECFLDE RKGVQNAIAR RRKALEKEQA LKEKYVEMTY
FENEILKEHP NAIICGIDEV GRGPLAGPVV ACATILNSNH NYLGLDDSKK VPVTKRLELN
EALKNEVTAF AYGIATAEEI DEFNIYKATQ IAMQRAIDGL SVQPTHLLID AMTLDNALPQ
VSLIKGDARS VSIAAASIMA KVFRDDYMTQ LSKDYPEYGF EKNAGYGTKQ HLLAIDDIGI
MKEHRKSFEP IKSLL
