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Database: UniProt
Entry: K8EGS0_CARML
LinkDB: K8EGS0_CARML
Original site: K8EGS0_CARML 
ID   K8EGS0_CARML            Unreviewed;       261 AA.
AC   K8EGS0;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 2.
DT   27-MAR-2024, entry version 60.
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   ECO:0000313|EMBL:CCO11038.2};
GN   ORFNames=BN424_1597 {ECO:0000313|EMBL:CCO11038.2};
OS   Carnobacterium maltaromaticum LMA28.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO11038.2, ECO:0000313|Proteomes:UP000000212};
RN   [1] {ECO:0000313|Proteomes:UP000000212}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX   PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA   Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA   Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA   Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT   "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL   Genome Announc. 1:0-0(2013).
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|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}.
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DR   EMBL; HE999757; CCO11038.2; -; Genomic_DNA.
DR   RefSeq; WP_015076299.1; NC_019425.2.
DR   AlphaFoldDB; K8EGS0; -.
DR   STRING; 1234679.BN424_1597; -.
DR   KEGG; cml:BN424_1597; -.
DR   eggNOG; COG0164; Bacteria.
DR   HOGENOM; CLU_036532_2_1_9; -.
DR   OrthoDB; 9803420at2; -.
DR   Proteomes; UP000000212; Chromosome.
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:UP000000212}.
FT   DOMAIN          73..261
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51975"
FT   BINDING         79
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         80
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         171
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   261 AA;  28855 MW;  2042976EF665A240 CRC64;
     MEKKQTIKEI KTILASITDA NDPRLIELKN DERKGTINAI KSWEKAQNKL VALEVKHQEM
     LAYELAVWQD GRNYIAGIDE VGRGPLAGPV VAAAVILPHD FHVLEINDSK QLSESKRDEL
     FDKIKDSALA IGIGIKDEGI IDQVNIYEAT KLAMIEAVEN LTIDPEHLLI DAMALDLPIP
     QSKIIKGDTK SLSIAAASII AKVTRDRMMK EYAKMYPGYG FEKNAGYGTK VHLAGLDAQG
     ITPIHRKSFS PVKELVLETT E
//
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