RNH2_METJA
ID RNH2_METJA Reviewed; 230 AA.
AC Q57599;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ribonuclease HII;
DE Short=RNase HII;
DE EC=3.1.26.4;
GN Name=rnhB; OrderedLocusNames=MJ0135;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP COFACTOR, AND MUTAGENESIS OF ASP-7; GLU-8; ASP-112 AND ASP-149.
RX PubMed=12534291; DOI=10.1021/bi026960a;
RA Lai B., Li Y., Cao A., Lai L.;
RT "Metal ion binding and enzymatic mechanism of Methanococcus jannaschii
RT RNase HII.";
RL Biochemistry 42:785-791(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10997908; DOI=10.1016/s0969-2126(00)00179-9;
RA Lai L., Yokota H., Hung L.-W., Kim R., Kim S.-H.;
RT "Crystal structure of archaeal RNase HII: a homologue of human major RNase
RT H.";
RL Structure 8:897-904(2000).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids.
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; L77117; AAB98116.1; -; Genomic_DNA.
DR PIR; G64316; G64316.
DR RefSeq; WP_010869628.1; NC_000909.1.
DR PDB; 1EKE; X-ray; 2.00 A; A/B=1-230.
DR PDBsum; 1EKE; -.
DR AlphaFoldDB; Q57599; -.
DR SMR; Q57599; -.
DR STRING; 243232.MJ_0135; -.
DR PRIDE; Q57599; -.
DR EnsemblBacteria; AAB98116; AAB98116; MJ_0135.
DR GeneID; 1450976; -.
DR KEGG; mja:MJ_0135; -.
DR eggNOG; arCOG04121; Archaea.
DR HOGENOM; CLU_036532_0_4_2; -.
DR InParanoid; Q57599; -.
DR OMA; REECRFF; -.
DR OrthoDB; 105421at2157; -.
DR PhylomeDB; Q57599; -.
DR EvolutionaryTrace; Q57599; -.
DR Proteomes; UP000000805; 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 Gene3D; 1.10.10.460; -; 1.
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; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
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; Magnesium; Manganese;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..230
FT /note="Ribonuclease HII"
FT /id="PRO_0000111663"
FT DOMAIN 1..224
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 112
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT MUTAGEN 7
FT /note="D->N: Reduces activity 800-fold."
FT /evidence="ECO:0000269|PubMed:12534291"
FT MUTAGEN 8
FT /note="E->Q: Reduces activity 700-fold."
FT /evidence="ECO:0000269|PubMed:12534291"
FT MUTAGEN 112
FT /note="D->N: Reduces activity 600-fold."
FT /evidence="ECO:0000269|PubMed:12534291"
FT MUTAGEN 149
FT /note="D->N: Reduces activity 800-fold."
FT /evidence="ECO:0000269|PubMed:12534291"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1EKE"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1EKE"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1EKE"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:1EKE"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:1EKE"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:1EKE"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:1EKE"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1EKE"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 153..176
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1EKE"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:1EKE"
SQ SEQUENCE 230 AA; 26506 MW; C454324C0C801299 CRC64;
MIIIGIDEAG RGPVLGPMVV CAFAIEKERE EELKKLGVKD SKELTKNKRA YLKKLLENLG
YVEKRILEAE EINQLMNSIN LNDIEINAFS KVAKNLIEKL NIRDDEIEIY IDACSTNTKK
FEDSFKDKIE DIIKERNLNI KIIAEHKADA KYPVVSAASI IAKAERDEII DYYKKIYGDI
GSGYPSDPKT IKFLEDYFKK HKKLPDIART HWKTCKRILD KSKQTKLIIE
