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Database: UniProt
Entry: M4RT58_9BIFI
LinkDB: M4RT58_9BIFI
Original site: M4RT58_9BIFI 
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
//
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