GenomeNet

Database: UniProt
Entry: A0A0M3HRL8_ASCLU
LinkDB: A0A0M3HRL8_ASCLU
Original site: A0A0M3HRL8_ASCLU 
ID   A0A0M3HRL8_ASCLU        Unreviewed;       270 AA.
AC   A0A0M3HRL8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-NOV-2023, entry version 21.
DE   RecName: Full=Ribonuclease H1 {ECO:0000256|PIRNR:PIRNR036852};
DE            Short=RNase H1 {ECO:0000256|PIRNR:PIRNR036852};
DE            EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR036852};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000496901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0000496901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000256|PIRNR:PIRNR036852}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036852};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR036852};
CC   -!- SIMILARITY: Belongs to the RNase H family.
CC       {ECO:0000256|ARBA:ARBA00005300, ECO:0000256|PIRNR:PIRNR036852}.
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DR   AlphaFoldDB; A0A0M3HRL8; -.
DR   WBParaSite; ALUE_0000496901-mRNA-1; ALUE_0000496901-mRNA-1; ALUE_0000496901.
DR   Proteomes; UP000036681; Unplaced.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR   CDD; cd09280; RNase_HI_eukaryote_like; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 1.
DR   InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR   InterPro; IPR017067; RNase_H1_euk.
DR   InterPro; IPR011320; RNase_H1_N.
DR   InterPro; IPR037056; RNase_H1_N_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10642; RIBONUCLEASE H1; 1.
DR   PANTHER; PTHR10642:SF26; RIBONUCLEASE H1; 1.
DR   Pfam; PF01693; Cauli_VI; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   PIRSF; PIRSF036852; Ribonuclease_H1_euk; 2.
DR   SUPFAM; SSF55658; L9 N-domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|PIRNR:PIRNR036852};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR036852};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR036852};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR036852};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR036852}.
FT   DOMAIN          99..266
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
SQ   SEQUENCE   270 AA;  29467 MW;  CE67DA7F7B091B7D CRC64;
     MKVAYYAVAR GTKPGVYRTW AECEKQVKGF AGARYKKFLN EHEALDFIAA NGGKISFRSV
     GASSTAAAGF VHKKQTLHEV SSTMKDLKRI GSDIAKWQSE GVPVVFTDGA CSSNGHHGAK
     AGIGVFWGDD HPDNVSEPLI SGPPTNNRAE LSAVITALRT VRLLCDLSSM SLNCHHLGKA
     ACERNFSRLI ICTDSNLLIK SMDSWIKTWR KNGWKTANGG DVKNKDLIVE LDKLLEKVKV
     HFKHVAGHAG IYGNEKADEL ARNGALRYIA
//
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