ID A0A0U3MQY2_9LACT Unreviewed; 311 AA.
AC A0A0U3MQY2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ribonuclease HIII {ECO:0000256|HAMAP-Rule:MF_00053};
DE Short=RNase HIII {ECO:0000256|HAMAP-Rule:MF_00053};
DE EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00053};
GN Name=rnhC {ECO:0000256|HAMAP-Rule:MF_00053};
GN ORFNames=NY10_2310 {ECO:0000313|EMBL:ALV22895.1};
OS Carnobacterium sp. CP1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV22895.1, ECO:0000313|Proteomes:UP000064734};
RN [1] {ECO:0000313|EMBL:ALV22895.1, ECO:0000313|Proteomes:UP000064734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP1 {ECO:0000313|EMBL:ALV22895.1,
RC ECO:0000313|Proteomes:UP000064734};
RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT Amanda bay, East Antarctic.";
RL Submitted (FEB-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_00053}.
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_00053, ECO:0000256|PROSITE-ProRule:PRU01319};
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_00053,
CC ECO:0000256|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00053,
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_00053, ECO:0000256|PROSITE-
CC ProRule:PRU01319};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00053}.
CC -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC {ECO:0000256|ARBA:ARBA00008378, ECO:0000256|HAMAP-Rule:MF_00053}.
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DR EMBL; CP010796; ALV22895.1; -; Genomic_DNA.
DR RefSeq; WP_058920067.1; NZ_CP010796.1.
DR AlphaFoldDB; A0A0U3MQY2; -.
DR STRING; 1564681.NY10_2310; -.
DR KEGG; carc:NY10_2310; -.
DR PATRIC; fig|1564681.3.peg.2319; -.
DR OrthoDB; 9777935at2; -.
DR Proteomes; UP000064734; 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: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; cd06590; RNase_HII_bacteria_HIII_like; 1.
DR CDD; cd14796; RNAse_HIII_N; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 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; IPR024568; RNase_HIII_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR NCBIfam; TIGR00716; rnhC; 1.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF25; RIBONUCLEASE HIII; 1.
DR Pfam; PF11858; DUF3378; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR PIRSF; PIRSF037748; RnhC; 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_00053};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00053};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00053};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00053};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00053};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00053};
KW Reference proteome {ECO:0000313|Proteomes:UP000064734}.
FT DOMAIN 95..311
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 101
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 102
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 205
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00053,
FT ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 311 AA; 33914 MW; AD0D6B565BDEF299 CRC64;
MANEVLTVSP KTLQEMKQYY EDYLKPKTPP GGKFAAKKAT VNITAYNSGK VLFQGQTAQQ
EAALWISKAV QSIPGKAKKN TPSLNTPLPK GFNTWSVIGS DEVGNGSYFG PLTVVAAYVD
KSQLPLLKEL GVRDSKDMKD PEIIRVAKDL VTFLPHSLLN VMPQKYNAIQ PTMTQGKMKA
VLHNQALGHV LMKIQPVVPE AILIDQFELP ATYFKHIQDQ PNQIKESVYF QTKGEGHHLA
VAAASIIARF AFLKGLEDMS AETGLRIPSG AGSNVDLVAA KLLKRGGLSL LGKYAKLHFA
NTQKAQKIAG F
//
