ID A0A559KIV3_9MOLU Unreviewed; 315 AA.
AC A0A559KIV3;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN Name=rnhC {ECO:0000313|EMBL:TVY12070.1};
GN ORFNames=MDPP_00389 {ECO:0000313|EMBL:TVY12070.1};
OS Candidatus Phytoplasma pini.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma.
OX NCBI_TaxID=267362 {ECO:0000313|EMBL:TVY12070.1, ECO:0000313|Proteomes:UP000320078};
RN [1] {ECO:0000313|EMBL:TVY12070.1, ECO:0000313|Proteomes:UP000320078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDPP {ECO:0000313|EMBL:TVY12070.1,
RC ECO:0000313|Proteomes:UP000320078};
RA Cai W., Costanzo S., Shao J., Zhao Y., Davis R.;
RT "Draft Genome Sequence of Candidatus Phytoplasma pini-Related Strain MDPP:
RT A Resource for Comparative Genomics of Gymnosperm-infecting Phytoplasmas.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|ARBA:ARBA00004065,
CC 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|PROSITE-
CC ProRule:PRU01319, 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|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={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|PROSITE-ProRule:PRU01319};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.
CC {ECO:0000256|ARBA:ARBA00008378}.
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:TVY12070.1}.
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DR EMBL; VIAE01000016; TVY12070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A559KIV3; -.
DR OrthoDB; 9777935at2; -.
DR Proteomes; UP000320078; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 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};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01319}; Reference proteome {ECO:0000313|Proteomes:UP000320078}.
FT DOMAIN 105..315
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 111
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 112
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 214
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 315 AA; 36817 MW; F68DA824C4B1BEFC CRC64;
MSNEYYTFYL NLSQFTIIKK KYQNFLIIKK NPNILFIIYK DEVRITCFYN GTCLVQGANI
QKEINYIKKI LSLSNNEKEN QTQFLNHKNS FQDPIKNNDI QNNNVGIIGT DESGSGDVFG
PLVVCAAFVM PKDIPFLKKI GVRDSKKLSE QQIKKIFILT SKKIDYCIKI VDNEKEYNFL
IKSANLNKIK ALCHNFVILK LLDKINQKAI IIMDQFTTIK SYFNYLQNEP KIYHSIRFET
KAESKYLSVA LASIIARYFF LKEINKLSHQ IEIPLLLGAS RKVDEQINHI YQKYNSNIFY
KIAKCNFKNI KTYLK
//