ID A0A371CN05_9APHY Unreviewed; 445 AA.
AC A0A371CN05;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
GN ORFNames=OH76DRAFT_1392968 {ECO:0000313|EMBL:RDX41627.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX41627.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX41627.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX41627.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
CC -!- SIMILARITY: Belongs to the RNase H family.
CC {ECO:0000256|ARBA:ARBA00005300}.
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DR EMBL; KZ857506; RDX41627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371CN05; -.
DR STRING; 139420.A0A371CN05; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT DOMAIN 146..296
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 101..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 47645 MW; 6D69853D7F32B158 CRC64;
MAKVGCYAVA RGRKPGIYLE WKDCSAQVLN FNGAKYKKFL DAAEAELWIN ANASGPLAGR
QSTTTAVRTE ATTAPAEGRV TADEAKSIAR QSEAVAVTYA HASNRSSAPR METAASVPAQ
RAVPPPPQEI RTTVSSFASG TSGSASSGPI VVYTDGSCRG NGKPGSTAGV GVWWGVDDPR
NVSERCPGDQ TNNRAELLSI IRVLERAPTD RPLEIRSDSQ YSISCMTAWV FDWKRRGWRK
SDGKPVLNLA LIQYADLLLE ERRRVLKQSV EFKKVLAHSG VEGNEAADRL ANEGAALPAV
PELDWDSMIR AVRARMDAAC STAENTVSVP RAATSPAKQA ASPSSPQPPA FVSRPTRRQP
SPPVKSSTTA SALLSPKSPS ASGPSGATVP SSRIILRTTD ELASSDVVHG RPDLRIAERE
LEIYAECLLD DDELMREAEL EGVYA
//
