ID A0A4P9YTL7_9FUNG Unreviewed; 257 AA.
AC A0A4P9YTL7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN ORFNames=SYNPS1DRAFT_18762 {ECO:0000313|EMBL:RKP23333.1};
OS Syncephalis pseudoplumigaleata.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Zoopagomycotina;
OC Zoopagomycetes; Zoopagales; Piptocephalidaceae; Syncephalis.
OX NCBI_TaxID=1712513 {ECO:0000313|EMBL:RKP23333.1, ECO:0000313|Proteomes:UP000278143};
RN [1] {ECO:0000313|Proteomes:UP000278143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Benny S71-1 {ECO:0000313|Proteomes:UP000278143};
RX PubMed=30297742; DOI=10.1038/s41564-018-0261-0;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N.K., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the fungal tree of life.";
RL Nat. Microbiol. 3:1417-1428(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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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. Eukaryotic subfamily.
CC {ECO:0000256|ARBA:ARBA00007058}.
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DR EMBL; KZ991074; RKP23333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P9YTL7; -.
DR Proteomes; UP000278143; 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; IPR004649; RNase_H2_suA.
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 NCBIfam; TIGR00729; ribonuclease HII; 1.
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:UP000278143}.
FT DOMAIN 28..253
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 257 AA; 28359 MW; A25DFCA8C28B4C2C CRC64;
MAATQPGPLT RSYTFHTDVP AACADGQPCL LGVDEAGRGP VLGPMVYSIC YCPLERSNDI
KSLGFADSKT LNEQERERLL QKICEHRDYI GWGVRVLSPQ DISQSMLRRN KYNLNSMAHD
TTIQLLREAL AANVNIKEVY IDTVGPPESY EAKLSQLFPY IKITVAKKAD SLYPIVSAAS
ICAKVTRDTI IQQWSFAEPG ADAVLSRAFG SGYSSDPNTV SWLRNNVDPV FGFPGIVRFS
WATCSRLLDE TASSVVW
//
