ID A0A2V3IEU4_9FLOR Unreviewed; 255 AA.
AC A0A2V3IEU4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN ORFNames=BWQ96_09678 {ECO:0000313|EMBL:PXF40606.1};
OS Gracilariopsis chorda.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Gracilariopsis.
OX NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF40606.1, ECO:0000313|Proteomes:UP000247409};
RN [1] {ECO:0000313|EMBL:PXF40606.1, ECO:0000313|Proteomes:UP000247409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF40606.1,
RC ECO:0000313|Proteomes:UP000247409};
RC TISSUE=Whole body {ECO:0000313|EMBL:PXF40606.1};
RX PubMed=29688518; DOI=10.1093/molbev/msy081;
RA Lee J., Yang E.C., Graf L., Yang J.H., Qiu H., Zel Zion U., Chan C.X.,
RA Stephens T.G., Weber A.P.M., Boo G.H., Boo S.M., Kim K.M., Shin Y.,
RA Jung M., Lee S.J., Yim H.S., Lee J.H., Bhattacharya D., Yoon H.S.;
RT "Analysis of the draft genome of the red seaweed Gracilariopsis chorda
RT provides insights into genome size evolution in Rhodophyta.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|RuleBase:RU003515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|PROSITE-
CC ProRule:PRU01319, ECO:0000256|RuleBase:RU003515};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC the absence of substrate. May bind a second metal ion after substrate
CC binding. {ECO:0000256|PROSITE-ProRule:PRU01319};
CC -!- SIMILARITY: Belongs to the RNase HII family.
CC {ECO:0000256|RuleBase:RU003515}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PXF40606.1}.
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DR EMBL; NBIV01000279; PXF40606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3IEU4; -.
DR STRING; 448386.A0A2V3IEU4; -.
DR Proteomes; UP000247409; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07181; RNase_HII_eukaryota_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 1.10.10.460; Ribonuclease hii. Domain 2; 1.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF7; RIBONUCLEASE H2 SUBUNIT A; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01319}; Reference proteome {ECO:0000313|Proteomes:UP000247409}.
FT DOMAIN 15..251
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 21
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 22
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 128
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 255 AA; 28587 MW; 3CD45317A0EDD801 CRC64;
MSEATDDSMW YPNTPCVLGI DEAGRRPVLG PMVYAAAVCP MSRLTDLRAL GANNSKALRE
EHRDELRRKI QGAAFLRTFE TILTGSFLSE NMLRKEKYNL NLVSHDAAIG LVQKAMDHGI
NVAEIYIDTV GNLQHYAAKF RKRFSAVEKV VVAKKADATY PIVGAASIVA KTTRDRRIRE
WGFPEQRRSA DFRPGDANIA VEFVGSTESS YLSDPITKTC IEQNCDVLFG FPTFVRFSWG
TAKVILEKNA VRFEW
//
