RNH_BPT4
ID RNH_BPT4 Reviewed; 305 AA.
AC P13319;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Ribonuclease H;
DE Short=RNase H;
DE EC=3.1.26.4;
GN Name=rnh; Synonyms=33.2, das;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BK536;
RX PubMed=2674900; DOI=10.1093/nar/17.16.6729;
RA Hahn S., Rueger W.;
RT "Organization of the bacteriophage T4 genome between map positions 150.745
RT and 145.824.";
RL Nucleic Acids Res. 17:6729-6729(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP FUNCTION, AND PROTEIN SEQUENCE OF 1-9.
RX PubMed=1703156; DOI=10.1016/s0021-9258(18)52376-0;
RA Hollingsworth H.C., Nossal N.G.;
RT "Bacteriophage T4 encodes an RNase H which removes RNA primers made by the
RT T4 DNA replication system in vitro.";
RL J. Biol. Chem. 266:1888-1897(1991).
RN [4]
RP FUNCTION.
RX PubMed=11376000; DOI=10.1074/jbc.m103914200;
RA Bhagwat M., Nossal N.G.;
RT "Bacteriophage T4 RNase H removes both RNA primers and adjacent DNA from
RT the 5' end of lagging strand fragments.";
RL J. Biol. Chem. 276:28516-28524(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
RX PubMed=8674116; DOI=10.1016/s0092-8674(00)81310-0;
RA Mueser T.C., Nossal N.G., Hyde C.C.;
RT "Structure of bacteriophage T4 RNase H, a 5' to 3' RNA-DNA and DNA-DNA
RT exonuclease with sequence similarity to the RAD2 family of eukaryotic
RT proteins.";
RL Cell 85:1101-1112(1996).
CC -!- FUNCTION: Plays essential roles in DNA replication by removing the RNA
CC primers from lagging strand fragments. Exhibits 5'to 3' exonuclease
CC activity on either RNA/DNA or DNA/DNA duplexes and endonuclease
CC activity on either flap or fork DNA structures.
CC {ECO:0000269|PubMed:11376000, ECO:0000269|PubMed:1703156}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
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DR EMBL; X15818; CAA33812.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42554.1; -; Genomic_DNA.
DR PIR; S05556; S05556.
DR RefSeq; NP_049859.1; NC_000866.4.
DR PDB; 1TFR; X-ray; 2.06 A; A=1-305.
DR PDB; 2IHN; X-ray; 3.00 A; A=1-305.
DR PDB; 3H7I; X-ray; 1.50 A; A=1-305.
DR PDB; 3H8J; X-ray; 1.80 A; A=1-305.
DR PDB; 3H8S; X-ray; 2.51 A; A=1-305.
DR PDB; 3H8W; X-ray; 2.80 A; A=1-305.
DR PDBsum; 1TFR; -.
DR PDBsum; 2IHN; -.
DR PDBsum; 3H7I; -.
DR PDBsum; 3H8J; -.
DR PDBsum; 3H8S; -.
DR PDBsum; 3H8W; -.
DR SMR; P13319; -.
DR GeneID; 1258577; -.
DR KEGG; vg:1258577; -.
DR BRENDA; 3.1.13.2; 732.
DR BRENDA; 3.1.99.B1; 732.
DR EvolutionaryTrace; P13319; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:CACAO.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:CACAO.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:InterPro.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:CACAO.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR038969; FEN.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR036276; T4_RNaseH_C.
DR PANTHER; PTHR42646; PTHR42646; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF09293; RNaseH_C; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication; Endonuclease;
KW Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..305
FT /note="Ribonuclease H"
FT /id="PRO_0000164977"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3H7I"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:3H7I"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 40..60
FT /evidence="ECO:0007829|PDB:3H7I"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:3H7I"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3H7I"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:3H7I"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:3H7I"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:3H7I"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:3H7I"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 265..276
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:3H7I"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:3H7I"
SQ SEQUENCE 305 AA; 35558 MW; 7956ECC356C0EDD0 CRC64;
MDLEMMLDED YKEGICLIDF SQIALSTALV NFPDKEKINL SMVRHLILNS IKFNVKKAKT
LGYTKIVLCI DNAKSGYWRR DFAYYYKKNR GKAREESTWD WEGYFESSHK VIDELKAYMP
YIVMDIDKYE ADDHIAVLVK KFSLEGHKIL IISSDGDFTQ LHKYPNVKQW SPMHKKWVKI
KSGSAEIDCM TKILKGDKKD NVASVKVRSD FWFTRVEGER TPSMKTSIVE AIANDREQAK
VLLTESEYNR YKENLVLIDF DYIPDNIASN IVNYYNSYKL PPRGKIYSYF VKAGLSKLTN
SINEF
