ID A0A0L8IBQ0_OCTBM Unreviewed; 343 AA.
AC A0A0L8IBQ0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
GN ORFNames=OCBIM_22021664mg {ECO:0000313|EMBL:KOF98933.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF98933.1};
RN [1] {ECO:0000313|EMBL:KOF98933.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF98933.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF98933.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KQ416049; KOF98933.1; -; Genomic_DNA.
DR RefSeq; XP_014778914.1; XM_014923428.1.
DR AlphaFoldDB; A0A0L8IBQ0; -.
DR STRING; 37653.A0A0L8IBQ0; -.
DR EnsemblMetazoa; Ocbimv22021664m; Ocbimv22021664m.p; Ocbimv22021664m.g.
DR EnsemblMetazoa; XM_014923428.1; XP_014778914.1; LOC106875333.
DR GeneID; 106875333; -.
DR KEGG; obi:106875333; -.
DR OMA; IRSMTEW; -.
DR OrthoDB; 3280806at2759; -.
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 GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
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; 1.
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 193..338
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 160..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 37693 MW; 56E3266C923D3294 CRC64;
MTSVAASLLR RPTSTLNTLK FACCLDNFIV MPFYAVKKGR VPGVYETWTE CQEQINGFYG
AKFKKFNTEE EALAFADISP SDKTLSSVAK SIQPIVKKLM SRVKEVSPLC QTLVSMLADL
DDSEDSKEFS TLACNVENDL AKLTASVKLT IDSKLLTGTT KRKASDSSEN TPEPPEKKKC
VEEGGFSGKK FADDDGVVVY TDGCCFHNGK HGASAGLGIY WGEGEKNTSE RLDGRQTNNR
AEIHAAIRAV EQAKAKNISN LIVKTDSQFL INCITKWLEG WKKKNWMKSS GEEVINKEDL
QELDEKLEGI NVKWVHVDAH CGVAGNEAAD KLANKGAKLP LPK
//
