RNH2_PYRHO
ID RNH2_PYRHO Reviewed; 220 AA.
AC O59351;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ribonuclease HII;
DE Short=RNase HII;
DE EC=3.1.26.4;
GN Name=rnhB; OrderedLocusNames=PH1650;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}.
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DR EMBL; BA000001; BAA30762.1; -; Genomic_DNA.
DR PIR; B71045; B71045.
DR RefSeq; WP_010885718.1; NC_000961.1.
DR PDB; 1UAX; X-ray; 2.00 A; A/B=1-220.
DR PDBsum; 1UAX; -.
DR AlphaFoldDB; O59351; -.
DR SMR; O59351; -.
DR STRING; 70601.3258079; -.
DR EnsemblBacteria; BAA30762; BAA30762; BAA30762.
DR GeneID; 1442499; -.
DR KEGG; pho:PH1650; -.
DR eggNOG; arCOG04121; Archaea.
DR OMA; REECRFF; -.
DR OrthoDB; 105421at2157; -.
DR BRENDA; 3.1.26.4; 7183.
DR EvolutionaryTrace; O59351; -.
DR Proteomes; UP000000752; Chromosome.
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:InterPro.
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; -; 1.
DR HAMAP; MF_00052_A; RNase_HII_A; 1.
DR InterPro; IPR004649; RNase_H2_suA.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR020787; RNase_HII_arc.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00729; TIGR00729; 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.
FT CHAIN 1..220
FT /note="Ribonuclease HII"
FT /id="PRO_0000111670"
FT DOMAIN 1..210
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 7
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1UAX"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1UAX"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:1UAX"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:1UAX"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:1UAX"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 139..163
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:1UAX"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:1UAX"
SQ SEQUENCE 220 AA; 25283 MW; 77DB1BDEDB8881D0 CRC64;
MKVAGVDEAG RGPVIGPLVI GVAVIDEKNI ERLRDIGVKD SKQLTPGQRE KLFSKLIDIL
DDYYVLLVTP KEIDERHHSM NELEAEKFVV ALNSLRIKPQ KIYVDSADVD PKRFASLIKA
GLKYEATVIA EHKADAKYEI VSAASIIAKV TRDREIEKLK QKYGEFGSGY PSDPRTKEWL
EEYYKQYGDF PPIVRRTWET ARKIEERFRK NQLTLDKFLK
