ID B3LMC3_YEAS1 Unreviewed; 348 AA.
AC B3LMC3;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=SCRG_02129 {ECO:0000313|EMBL:EDV11726.1};
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV11726.1, ECO:0000313|Proteomes:UP000008335};
RN [1] {ECO:0000313|Proteomes:UP000008335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) 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; CH408047; EDV11726.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LMC3; -.
DR SMR; B3LMC3; -.
DR HOGENOM; CLU_030894_0_0_1; -.
DR Proteomes; UP000008335; 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; 1.
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}.
FT DOMAIN 184..346
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 39431 MW; 02403B2329126B90 CRC64;
MARQGNFYAV RKGRETGIYN TWNECKNQVD GYGGAIYKKF NSYEQAKSFL GQPNTTSNYG
SSTHAGGQVS KPHTTQKRVH RRNRPLHYSS LTSSSACSSL SSANTNTFYS VKSNVPNIES
KIFNNWKDCQ AYVKHKRGIT FKKFEDQLAA ENFISGMSAH DYKLMNISKE SFESKYKLSS
NTMYNKSMNV YCDGSSFGNG TSSSRAGYGA YFEGAPEENI SEPLLSGAQT NNRAEIEAVS
EALKKIWEKL TNEKEKVNYQ IKTDSEYVTK LLNDRYMTYD NKKLEGLPNS DLIVPLVQRF
VKVKKYYELN KECFKNNGKF QIEWVKGHDG DPGNEMADFL AKKGASRR
//
