RNH3_UREPA
ID RNH3_UREPA Reviewed; 316 AA.
AC Q9PQ93;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ribonuclease HIII;
DE Short=RNase HIII;
DE EC=3.1.26.4;
GN Name=rnhC; OrderedLocusNames=UU397;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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. RnhC subfamily.
CC {ECO:0000305}.
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DR EMBL; AF222894; AAF30807.1; -; Genomic_DNA.
DR RefSeq; WP_006689032.1; NC_002162.1.
DR AlphaFoldDB; Q9PQ93; -.
DR SMR; Q9PQ93; -.
DR STRING; 273119.UU397; -.
DR EnsemblBacteria; AAF30807; AAF30807; UU397.
DR GeneID; 29672376; -.
DR KEGG; uur:UU397; -.
DR eggNOG; COG1039; Bacteria.
DR HOGENOM; CLU_059546_1_0_14; -.
DR OMA; TGDYFGP; -.
DR Proteomes; UP000000423; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium 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_00053; RNase_HIII; 1.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR004641; RNase_HIII.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR PIRSF; PIRSF037748; RnhC; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..316
FT /note="Ribonuclease HIII"
FT /id="PRO_0000111709"
FT DOMAIN 101..316
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 107
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 316 AA; 36418 MW; E1BD5366CEA0F35B CRC64;
MAIVSVKLTS NQVDKFLILW RPYLVHNNHN YAKYTFKIDG TLIIIYNTNT CTINTHDINS
FLNTFLKRED LTLFNVIKQQ VNTKKNNQNV MSQSEIYESA QVIIGSDEVG VGDLFGGIVV
CAVSLKKSDF KKINHLKIID SKKLNDQQMQ EIYQQIKNQI SYTIVSYNPK EYNELIKEYN
NAHILKTILH YKALQSEIHK HAKYSIFSVV DAFSSLKNWN QYLQKVNFQP YEPNLLIPKA
ESIYTSVALA SIIARVMFLK MIAIIEEQFN VKIPLGSSNP LVNDVASNIF QKFGLKILKQ
VAKEHFSNFQ QIIKNK
