RNH1_RAT
ID RNH1_RAT Reviewed; 285 AA.
AC Q5BK46;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ribonuclease H1;
DE Short=RNase H1;
DE EC=3.1.26.4;
GN Name=Rnaseh1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. Plays a role in RNA polymerase II (RNAp II) transcription
CC termination by degrading R-loop RNA-DNA hybrid formation at G-rich
CC pause sites located downstream of the poly(A) site and behind the
CC elongating RNAp II. {ECO:0000250|UniProtKB:O60930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC regulatory site, or after substrate binding. {ECO:0000250};
CC -!- ACTIVITY REGULATION: In the presence of magnesium, manganese is
CC inhibitory. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR EMBL; BC091209; AAH91209.1; -; mRNA.
DR RefSeq; NP_001013115.1; NM_001013097.2.
DR RefSeq; NP_001273867.1; NM_001286938.1.
DR AlphaFoldDB; Q5BK46; -.
DR SMR; Q5BK46; -.
DR STRING; 10116.ENSRNOP00000011819; -.
DR PhosphoSitePlus; Q5BK46; -.
DR PaxDb; Q5BK46; -.
DR Ensembl; ENSRNOT00000011819; ENSRNOP00000011819; ENSRNOG00000008584.
DR GeneID; 298933; -.
DR KEGG; rno:298933; -.
DR CTD; 246243; -.
DR RGD; 1309012; Rnaseh1.
DR eggNOG; KOG3752; Eukaryota.
DR GeneTree; ENSGT00390000003466; -.
DR HOGENOM; CLU_030894_0_2_1; -.
DR InParanoid; Q5BK46; -.
DR OMA; ELWYGLY; -.
DR OrthoDB; 1434144at2759; -.
DR PhylomeDB; Q5BK46; -.
DR TreeFam; TF313356; -.
DR PRO; PR:Q5BK46; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008584; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5BK46; RN.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; ISS:UniProtKB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006264; P:mitochondrial DNA replication; ISO:RGD.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.970.10; -; 1.
DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR InterPro; IPR017067; RNase_H1_euk.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01693; Cauli_VI; 1.
DR Pfam; PF00075; RNase_H; 1.
DR PIRSF; PIRSF036852; Ribonuclease_H1_euk; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55658; SSF55658; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..285
FT /note="Ribonuclease H1"
FT /id="PRO_0000195435"
FT DOMAIN 135..281
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT REGION 72..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
SQ SEQUENCE 285 AA; 31773 MW; DC065C7F06EA1807 CRC64;
MRWLLPLFRT VTLAVVRVRR GVCGLGMFYA VRRGRRTGVF LSWSECKAQV DRFPAARFKK
FATEDEAWAF VRSSSSPDGS KGQESAHVQK LQVKTSKRPR EPLGEEEEPP EPGAKHTRQD
TEPAALVSKD AFSYMGESVV VYTDGCCSSN GRKRARAGIG VYWGPGHPLN VGIRLPGRQT
NQRAEIHAAC KAITQAKAQN ISKLVLYTDS MFTINGITNW VQGWKKNGWR TSTGKDVINK
EDFMELDELT QGMDIQWMHI PGHSGFVGNE EADRLAREGA KQSEG
