ID M4RT58_9BIFI Unreviewed; 407 AA.
AC M4RT58;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
GN ORFNames=D805_1410 {ECO:0000313|EMBL:AGH41677.1};
OS Bifidobacterium thermophilum RBL67.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH41677.1, ECO:0000313|Proteomes:UP000011835};
RN [1] {ECO:0000313|EMBL:AGH41677.1, ECO:0000313|Proteomes:UP000011835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RBL67 {ECO:0000313|EMBL:AGH41677.1,
RC ECO:0000313|Proteomes:UP000011835};
RX PubMed=23640377;
RA Jans C., Lacroix C., Follador R., Stevens M.J.;
RT "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT Strain RBL67.";
RL Genome Announc. 1:E00191-13(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the RNase H family.
CC {ECO:0000256|ARBA:ARBA00005300}.
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DR EMBL; CP004346; AGH41677.1; -; Genomic_DNA.
DR RefSeq; WP_015450934.1; NC_020546.1.
DR AlphaFoldDB; M4RT58; -.
DR KEGG; btp:D805_1410; -.
DR PATRIC; fig|1254439.12.peg.1402; -.
DR HOGENOM; CLU_049854_0_0_11; -.
DR Proteomes; UP000011835; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR CDD; cd09278; RNase_HI_prokaryote_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR022892; RNaseHI.
DR PANTHER; PTHR10642; RIBONUCLEASE H1; 1.
DR PANTHER; PTHR10642:SF26; RIBONUCLEASE H1; 1.
DR Pfam; PF00075; RNase_H; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722}.
FT DOMAIN 1..152
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 41900 MW; 9701D401989C052F CRC64;
MTITVSTDGS ALGNPNGPMG WAWADHTPHA GGTPGHEHEG DCDAGGASNG TNQIGELCAV
LEALRAHPGA EPLTIESDSQ YAINCSTTWV RGWKKHDWKT SQGKPVKNRE LIAAIDHEIS
QRPGPVKFVW VKGHNNNPGN DKVDHLAHGY AGDCRIGVKP GYLPLEGWQS LLASEYAKGT
VVPEDAHMLM EGKISAAEYH LGRAEDTGGV PGADGIQRTD SSQAAGGGPV SRTTSGTRHT
HSLADRLAEP EGVPDDLPDY HATAGSVDAI DAADSATTAI AANKDNTASD TPSVSDVAPA
AIDSATTATA EAAESGNSEI ATSPAAGQAA PTHNTAAASV TPTSSGANRL RTVPGLTLSG
TLRFSPPPSS SPTYSGEPRH IHGLVEIDGY VQGDGSIELN GARFMLG
//