GenomeNet

Database: UniProt
Entry: A0A0F5R9N3_9BACL
LinkDB: A0A0F5R9N3_9BACL
Original site: A0A0F5R9N3_9BACL 
ID   A0A0F5R9N3_9BACL        Unreviewed;       204 AA.
AC   A0A0F5R9N3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Ribonuclease HII {ECO:0000256|HAMAP-Rule:MF_00052};
DE            Short=RNase HII {ECO:0000256|HAMAP-Rule:MF_00052};
DE            EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00052};
GN   Name=rnhB {ECO:0000256|HAMAP-Rule:MF_00052};
GN   ORFNames=VE23_05995 {ECO:0000313|EMBL:KKC49718.1};
OS   Paenibacillus sp. D9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC49718.1, ECO:0000313|Proteomes:UP000036611};
RN   [1] {ECO:0000313|EMBL:KKC49718.1, ECO:0000313|Proteomes:UP000036611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D9 {ECO:0000313|EMBL:KKC49718.1,
RC   ECO:0000313|Proteomes:UP000036611};
RA   Sharma V., Lin J.;
RT   "Genome sequence of surfactant producing, diesel degrading Paenibacillus
RT   sp. D9, isolated from diesel contaminated soil.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000256|ARBA:ARBA00004065, ECO:0000256|HAMAP-
CC       Rule:MF_00052, ECO:0000256|RuleBase:RU003515}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|HAMAP-
CC         Rule:MF_00052, ECO:0000256|PROSITE-ProRule:PRU01319,
CC         ECO:0000256|RuleBase:RU003515};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00052,
CC         ECO:0000256|PROSITE-ProRule:PRU01319};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00052,
CC         ECO:0000256|PROSITE-ProRule:PRU01319};
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:0000256|HAMAP-Rule:MF_00052, ECO:0000256|PROSITE-
CC       ProRule:PRU01319};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00052}.
CC   -!- SIMILARITY: Belongs to the RNase HII family.
CC       {ECO:0000256|ARBA:ARBA00007383, ECO:0000256|HAMAP-Rule:MF_00052,
CC       ECO:0000256|RuleBase:RU003515}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKC49718.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JZEJ01000001; KKC49718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5R9N3; -.
DR   PATRIC; fig|665792.3.peg.1342; -.
DR   Proteomes; UP000036611; Unassembled WGS sequence.
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:UniProtKB-UniRule.
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   CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   HAMAP; MF_00052_B; RNase_HII_B; 1.
DR   InterPro; IPR022898; RNase_HII.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR   PANTHER; PTHR10954:SF18; RIBONUCLEASE HII; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS51975; RNASE_H_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00052};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00052};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00052};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00052};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00052};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036611}.
FT   DOMAIN          14..203
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51975"
FT   BINDING         20
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00052,
FT                   ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         21
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00052,
FT                   ECO:0000256|PROSITE-ProRule:PRU01319"
FT   BINDING         112
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00052,
FT                   ECO:0000256|PROSITE-ProRule:PRU01319"
SQ   SEQUENCE   204 AA;  22532 MW;  9A9473E585305929 CRC64;
     MLSYERPLWE SGAEHVCGVD EVGRGCLFGD VVAAAVILPR GLVLDGVDDS KKLSEKKREM
     LYDVILDSAV AWAVARIDSE TIDRINIRQA SRLAMKQAVE SLGVRPSHLL VDAETVDMDF
     PQTAIIHGDA VSQSIGAASI LAKVTRDRLC KEIWDLHYPA YGIAVHKGYA TKHHRSMLLQ
     HGPSPLHRRS FLGKILPEDQ LALF
//
DBGET integrated database retrieval system