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Database: UniProt
Entry: A0A4T2C755_9MICO
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ID   A0A4T2C755_9MICO        Unreviewed;       215 AA.
AC   A0A4T2C755;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=D4765_06625 {ECO:0000313|EMBL:TIH38336.1};
OS   Subtercola vilae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Subtercola.
OX   NCBI_TaxID=2056433 {ECO:0000313|EMBL:TIH38336.1, ECO:0000313|Proteomes:UP000306192};
RN   [1] {ECO:0000313|EMBL:TIH38336.1, ECO:0000313|Proteomes:UP000306192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DB165 {ECO:0000313|EMBL:TIH38336.1,
RC   ECO:0000313|Proteomes:UP000306192};
RX   PubMed=31018526;
RA   Villalobos A.S., Wiese J., Imhoff J.F., Dorador C., Keller A.,
RA   Hentschel U.;
RT   "Systematic Affiliation and Genome Analysis of Subtercola vilae DB165(T)
RT   with Particular Emphasis on Cold Adaptation of an Isolate from a High-
RT   Altitude Cold Volcano Lake.";
RL   Microorganisms 7:0-E107(2019).
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:TIH38336.1}.
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DR   EMBL; QYRT01000009; TIH38336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4T2C755; -.
DR   OrthoDB; 9803420at2; -.
DR   Proteomes; UP000306192; 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:UP000306192}.
FT   DOMAIN          7..209
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51975"
FT   BINDING         13
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         14
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         113
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   215 AA;  22232 MW;  5969469200006E74 CRC64;
     MGRAGATMVI GVDEVGRGAL AGPVAVGMCV IDPVRPGRFP VGLRDSKMLS EAKRELLAPL
     AAAWAGASAV GLASADEVDR LGIIACLGLA AKRALGILHA SGVEIMTATV LLDGSHDWLS
     PALGTPLQVT TKVKADRDCA SVAAASVVAK VHRDRLMIDL DGVLPGYGWA SNKGYGSAAH
     FEAIELLGAT EHHRHTWLKS APSVAPIDLA NHGRR
//
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