LOCUS RNH2_ACIC1 307 aa linear BCT 27-NOV-2024
DEFINITION RecName: Full=Ribonuclease HII; Short=RNase HII.
ACCESSION A0LV66
VERSION A0LV66.1
DBSOURCE UniProtKB: locus RNH2_ACIC1, accession A0LV66;
class: standard.
created: May 20, 2008.
sequence updated: Dec 12, 2006.
annotation updated: Nov 27, 2024.
xrefs: CP000481.1, ABK53326.1
xrefs (non-sequence databases): AlphaFoldDB:A0LV66, SMR:A0LV66,
STRING:351607.Acel_1554, KEGG:ace:Acel_1554, eggNOG:COG0164,
HOGENOM:CLU_036532_1_0_11, InParanoid:A0LV66, OrthoDB:9803420at2,
Proteomes:UP000008221, GO:0005737, GO:0032299, GO:0030145,
GO:0003723, GO:0004523, GO:0043137, GO:0006298, CDD:cd07182,
FunFam:3.30.420.10:FF:000113, Gene3D:3.30.420.10, HAMAP:MF_00052_B,
InterPro:IPR022898, InterPro:IPR001352, InterPro:IPR024567,
InterPro:IPR012337, InterPro:IPR036397, PANTHER:PTHR10954,
PANTHER:PTHR10954:SF18, Pfam:PF01351, SUPFAM:SSF53098,
PROSITE:PS51975
KEYWORDS Cytoplasm; Endonuclease; Hydrolase; Manganese; Metal-binding;
Nuclease; Reference proteome.
SOURCE Acidothermus cellulolyticus 11B
ORGANISM Acidothermus cellulolyticus 11B
Bacteria; Bacillati; Actinomycetota; Actinomycetes; Acidothermales;
Acidothermaceae; Acidothermus.
REFERENCE 1 (residues 1 to 307)
AUTHORS Barabote,R.D., Xie,G., Leu,D.H., Normand,P., Necsulea,A.,
Daubin,V., Medigue,C., Adney,W.S., Xu,X.C., Lapidus,A.,
Parales,R.E., Detter,C., Pujic,P., Bruce,D., Lavire,C.,
Challacombe,J.F., Brettin,T.S. and Berry,A.M.
TITLE Complete genome of the cellulolytic thermophile Acidothermus
cellulolyticus 11B provides insights into its ecophysiological and
evolutionary adaptations
JOURNAL Genome Res 19 (6), 1033-1043 (2009)
PUBMED 19270083
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
STRAIN=ATCC 43068 / DSM 8971 / 11B
COMMENT [FUNCTION] Endonuclease that specifically degrades the RNA of
RNA-DNA hybrids. {ECO:0000255|HAMAP-Rule:MF_00052}.
[CATALYTIC ACTIVITY] Reaction=Endonucleolytic cleavage to
5'-phosphomonoester.; EC=3.1.26.4;
Evidence={ECO:0000255|HAMAP-Rule:MF_00052}.
[COFACTOR] Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_00052}; Name=Mg(2+);
Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer
in the absence of substrate. May bind a second metal ion after
substrate binding. {ECO:0000255|HAMAP-Rule:MF_00052}.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00052}.
[SIMILARITY] Belongs to the RNase HII family.
{ECO:0000255|HAMAP-Rule:MF_00052}.
FEATURES Location/Qualifiers
source 1..307
/organism="Acidothermus cellulolyticus 11B"
/db_xref="taxon:351607"
gene 1..307
/gene="rnhB"
/locus_tag="Acel_1554"
Protein 1..307
/product="Ribonuclease HII"
/EC_number="3.1.26.4"
/note="RNase HII"
/UniProtKB_evidence="Inferred from homology"
Region 1..307
/region_name="Mature chain"
/note="Ribonuclease HII. /id=PRO_0000334852."
Region 27..226
/region_name="rnhB"
/note="ribonuclease HII; Validated; PRK00015"
/db_xref="CDD:234574"
Region 44..235
/region_name="Domain"
/note="RNase H type-2.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01319."
Site order(50..55,83,118..120,144..146,159..160,162,176,
197..199,201..203,223)
/site_type="other"
/note="RNA/DNA hybrid binding site [nucleotide binding]"
/db_xref="CDD:260003"
Region 241..307
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
1 mgasttarlg parvrserrs caaerhrlvd lyryerrlar lglepvagvd eagrgacagp
61 lvvaavilgs drrnriagla dskqltpaar esiyneiisr alawsvvvip ssevdelgvh
121 aanitgmrra vaglavrpay vltdgfsiag lnapglavck gdeavaciaa asvvakvtrd
181 rlmvelhekf pmyefathkg yvtaghraal arhgpcpehr rsfvtvrrag grmelritel
241 adsddspgfa sgpaeavpgp agsagaasaa arpaaagpag rlvdqnraad lrdngdvsrp
301 aelleip
//