ID A0A656KLQ7_BLUGR Unreviewed; 346 AA.
AC A0A656KLQ7;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=Ribonuclease H {ECO:0000256|ARBA:ARBA00012180, ECO:0000256|PIRNR:PIRNR036852};
DE Short=RNase H {ECO:0000256|PIRNR:PIRNR036852};
DE EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180, ECO:0000256|PIRNR:PIRNR036852};
GN ORFNames=BGT96224_3192 {ECO:0000313|EMBL:EPQ65923.1};
OS Blumeria graminis f. sp. tritici 96224.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=1268274 {ECO:0000313|EMBL:EPQ65923.1, ECO:0000313|Proteomes:UP000053110};
RN [1] {ECO:0000313|Proteomes:UP000053110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX PubMed=23852167; DOI=10.1038/ng.2704;
RA Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT "The wheat powdery mildew genome shows the unique evolution of an obligate
RT biotroph.";
RL Nat. Genet. 45:1092-1096(2013).
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; KE375014; EPQ65923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A656KLQ7; -.
DR OrthoDB; 3280806at2759; -.
DR Proteomes; UP000053110; Unassembled WGS sequence.
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; 2.
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; 2.
DR Pfam; PF00075; RNase_H; 1.
DR PIRSF; PIRSF036852; Ribonuclease_H1_euk; 2.
DR SUPFAM; SSF55658; L9 N-domain-like; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053110}.
FT DOMAIN 193..343
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
SQ SEQUENCE 346 AA; 38439 MW; 1B03F17DD383AD09 CRC64;
MSSNKIPKSS SSSKRKRNDG NNKFYAVKCG IRPGVYNSWK ECQAQITGFS GANYKGFTNF
EDAQSYVAGK TVTNPTKSTN KIRFYGVAVG HCPGVYTDWE EASMQIKDTK KPIFKKFSSF
EEARLFVQSR GKEHDCEKNV LAETPSTYDP EKTVAEENNP SKKVKMNSEI SIKSQGLEPG
ITDTDPRQTE TENSKLVVAY TDGSSRGNGT SNAKAGIGVY FGKNDPRNIS EPLLGKPQTN
QRAELSAIWR AIQICPESKN LRLFTDSNYS IKCLTTWYKG WLKNKWRTAS GSPVLNRDLI
QAVRTLINHR DSCGVTTELQ WVRGHDNDPG NEAADQLAVA GSYASR
//
