ID A0A136MMA1_9BACT Unreviewed; 402 AA.
AC A0A136MMA1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00048, ECO:0000256|HAMAP-Rule:MF_00052};
DE Includes:
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};
DE Includes:
DE RecName: Full=UPF0102 protein UZ16_OP3001001889 {ECO:0000256|HAMAP-Rule:MF_00048};
GN Name=rnhB {ECO:0000256|HAMAP-Rule:MF_00052,
GN ECO:0000313|EMBL:KXK35040.1};
GN ORFNames=UZ16_OP3001001889 {ECO:0000313|EMBL:KXK35040.1};
OS Candidatus Hinthialibacteria bacterium OLB16.
OC Bacteria; Candidatus Hinthialibacterota.
OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK35040.1, ECO:0000313|Proteomes:UP000070296};
RN [1] {ECO:0000313|EMBL:KXK35040.1, ECO:0000313|Proteomes:UP000070296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK35040.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-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_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}.
CC -!- SIMILARITY: Belongs to the UPF0102 family.
CC {ECO:0000256|ARBA:ARBA00006738, ECO:0000256|HAMAP-Rule:MF_00048}.
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:KXK35040.1}.
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DR EMBL; LMZT01000096; KXK35040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MMA1; -.
DR STRING; 1617433.UZ16_OP3001001889; -.
DR PATRIC; fig|1617433.3.peg.2040; -.
DR Proteomes; UP000070296; 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; cd20736; PoNe_Nuclease; 1.
DR CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR Gene3D; 3.40.1350.10; -; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_00052_B; RNase_HII_B; 1.
DR HAMAP; MF_00048; UPF0102; 1.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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 InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR003509; UPF0102_YraN-like.
DR NCBIfam; TIGR00252; YraN family protein; 1.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF18; RIBONUCLEASE HII; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR Pfam; PF02021; UPF0102; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 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}.
FT DOMAIN 30..222
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 36
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 37
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 131
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 402 AA; 44583 MW; C1C5FE6FA1643AF2 CRC64;
MTPKASPPLR SALERVAGMV SFDRSHCPDG VLAGIDEAGR GPWAGPVVAA GVVLDVSVDP
ALLYELNDSK KLTPRQRERL ARKIAEIAQG IGVGTASVDE IDRLGILKAT FLAMRRALDD
LAILPDHILV DGNRDPDLGF PTTCLVQGDS RSASVAAASI MAKTHRDRLM DLLAGDEDPY
GFRCHKGYGT ELHSHALSVF GLSGHHRRSF KPVAHYLIHP GPSPGFLKAW KLLLSVRPGS
DCSHLFDQVE SELPYLTESE SWLLQHRLMS LRSMIPKVPE GSLAQRHKGD FFEGLVGKYL
KDKGFILLEQ NYQTREGEID WIVQDGETLV FIEVKMRRSA EYGGAAEAVD RRKRQRIILA
ALSYLDRYPR EMDCRFDVVA LEGDRKGGTR LEYFPNAFTL DP
//
