ID A0A292II94_9MOLU Unreviewed; 319 AA.
AC A0A292II94;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN ORFNames=MAMA39_01930 {ECO:0000313|EMBL:CDN40316.1};
OS Mycoplasma amphoriforme A39.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=572419 {ECO:0000313|EMBL:CDN40316.1, ECO:0000313|Proteomes:UP000261764};
RN [1] {ECO:0000313|EMBL:CDN40316.1, ECO:0000313|Proteomes:UP000261764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A39 {ECO:0000313|EMBL:CDN40316.1,
RC ECO:0000313|Proteomes:UP000261764};
RX PubMed=25344534; DOI=10.1093/cid/ciu820;
RA Gillespie S.H., Ling C.L., Oravcova K., Pinheiro M., Wells L., Bryant J.M.,
RA McHugh T.D., Bebear C., Webster D., Harris S.R., Seth-Smith H.M.,
RA Thomson N.R.;
RT "Genomic Investigations unmask Mycoplasma amphoriforme, a new respiratory
RT pathogen.";
RL Clin. Infect. Dis. 60:381-388(2015).
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}.
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DR EMBL; HG937516; CDN40316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292II94; -.
DR KEGG; mamp:MAMA39_01930; -.
DR Proteomes; UP000261764; Chromosome.
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:UP000261764}.
FT DOMAIN 99..319
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 105
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 106
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 319 AA; 36815 MW; 0877DE8EF8F35842 CRC64;
MKTYTQKLSK DEIVQIKKEF AVFQVRTNNP NLYFCFKYEN VTISIYRTGS ILFQGNYVDK
VVKFVLAKHD ESKRIPEVNA KSNTPFKKKN YEPLFSMEVN EIGCDEVGVG DYFGGMVMCV
AYVNENQKKD LQKIGVQDSK KLNDQQISTI AIKLIDQLQI TYAVSNYIAL EYNNLYDKYQ
NSHILKTLGH NQALTKLLNA NSNIKLTNTR IIMDQYVSKQ HYYNYLAKIN VTNPVRINTF
ETKADSKYLS VAAASIIARY VWLNEIDKMS KKYQIPIFLG ASNPKILTIA KKIYQDYGIN
ELKKCVKLHF SFTDKITVN
//
