ID RNRH_RHINI Reviewed; 238 AA. AC P08056; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Ribonuclease Rh; DE Short=RNase Rh; DE EC=4.6.1.19; DE Flags: Precursor; OS Rhizopus niveus. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina; OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus. OX NCBI_TaxID=4844; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 17-238. RC STRAIN=NBRC 4810 / AS 3.4817; RX PubMed=3391995; DOI=10.1093/oxfordjournals.jbchem.a122284; RA Horiuchi H., Yanai K., Takagi M., Yano K., Wakabayashi E., Sanda A., RA Mine S., Ohgi K., Irie M.; RT "Primary structure of a base non-specific ribonuclease from Rhizopus RT niveus."; RL J. Biochem. 103:408-418(1988). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 4810 / AS 3.4817; RX PubMed=1655721; DOI=10.1093/oxfordjournals.jbchem.a123456; RA Ohgi K., Horiuchi H., Watanabe H., Takagi M., Yano K., Irie M.; RT "Expression of RNase Rh from Rhizopus niveus in yeast and characterization RT of the secreted proteins."; RL J. Biochem. 109:776-785(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=1633875; DOI=10.1016/0014-5793(92)80997-u; RA Kurihara H., Mitsui Y., Ohgi K., Irie M., Mizuno H., Nakamura K.T.; RT "Crystal and molecular structure of RNase Rh, a new class of microbial RT ribonuclease from Rhizopus niveus."; RL FEBS Lett. 306:189-192(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND, AND ACTIVE SITE. RX PubMed=8551522; DOI=10.1006/jmbi.1996.0025; RA Kurihara H., Nonaka T., Mitsui Y., Ohgi K., Irie M., Nakamura K.T.; RT "The crystal structure of ribonuclease Rh from Rhizopus niveus at 2.0-A RT resolution."; RL J. Mol. Biol. 255:310-320(1996). CC -!- FUNCTION: This is a base non-specific ribonuclease. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'- CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA- CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284, CC ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10045, ECO:0000255|PROSITE-ProRule:PRU10046}; CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D00238; BAA00167.1; -; Genomic_DNA. DR EMBL; D12476; BAA02042.1; -; mRNA. DR PIR; JH0367; JH0367. DR PDB; 1BOL; X-ray; 2.00 A; A=17-238. DR PDBsum; 1BOL; -. DR AlphaFoldDB; P08056; -. DR SMR; P08056; -. DR EvolutionaryTrace; P08056; -. DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProt. DR CDD; cd01061; RNase_T2_euk; 1. DR Gene3D; 3.90.730.10; Ribonuclease T2-like; 1. DR InterPro; IPR033697; Ribonuclease_T2_eukaryotic. DR InterPro; IPR001568; RNase_T2-like. DR InterPro; IPR036430; RNase_T2-like_sf. DR InterPro; IPR018188; RNase_T2_His_AS_1. DR InterPro; IPR033130; RNase_T2_His_AS_2. DR PANTHER; PTHR11240; RIBONUCLEASE T2; 1. DR PANTHER; PTHR11240:SF22; RIBONUCLEASE X25; 1. DR Pfam; PF00445; Ribonuclease_T2; 1. DR SUPFAM; SSF55895; Ribonuclease Rh-like; 1. DR PROSITE; PS00530; RNASE_T2_1; 1. DR PROSITE; PS00531; RNASE_T2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease; KW Hydrolase; Lyase; Nuclease; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000269|PubMed:3391995" FT CHAIN 17..238 FT /note="Ribonuclease Rh" FT /id="PRO_0000030964" FT ACT_SITE 62 FT /evidence="ECO:0000269|PubMed:8551522" FT ACT_SITE 121 FT /evidence="ECO:0000269|PubMed:8551522" FT ACT_SITE 125 FT /evidence="ECO:0000269|PubMed:8551522" FT DISULFID 19..36 FT /evidence="ECO:0000269|PubMed:8551522" FT DISULFID 26..69 FT /evidence="ECO:0000269|PubMed:8551522" FT DISULFID 35..136 FT /evidence="ECO:0000269|PubMed:8551522" FT DISULFID 79..128 FT /evidence="ECO:0000269|PubMed:8551522" FT DISULFID 198..229 FT /evidence="ECO:0000269|PubMed:8551522" FT CONFLICT 82..84 FT /note="NRA -> SLY (in Ref. 1; BAA00167)" FT /evidence="ECO:0000305" FT STRAND 24..27 FT /evidence="ECO:0007829|PDB:1BOL" FT TURN 34..36 FT /evidence="ECO:0007829|PDB:1BOL" FT STRAND 42..48 FT /evidence="ECO:0007829|PDB:1BOL" FT STRAND 60..67 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 88..95 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 97..106 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 114..124 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 144..159 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 162..167 FT /evidence="ECO:0007829|PDB:1BOL" FT TURN 168..170 FT /evidence="ECO:0007829|PDB:1BOL" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:1BOL" FT HELIX 179..190 FT /evidence="ECO:0007829|PDB:1BOL" FT STRAND 195..199 FT /evidence="ECO:0007829|PDB:1BOL" FT STRAND 202..213 FT /evidence="ECO:0007829|PDB:1BOL" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:1BOL" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:1BOL" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:1BOL" SQ SEQUENCE 238 AA; 25635 MW; A3BAB811D24334B3 CRC64; MKAVLALATL IGSTLASSCS STALSCSNSA NSDTCCSPEY GLVVLNMQWA PGYGPDNAFT LHGLWPDKCS GAYAPSGGCD SNRASSSIAS VIKSKDSSLY NSMLTYWPSN QGNNNVFWSH EWSKHGTCVS TYDPDCYDNY EEGEDIVDYF QKAMDLRSQY NVYKAFSSNG ITPGGTYTAT EMQSAIESYF GAKAKIDCSS GTLSDVALYF YVRGRDTYVI TDALSTGSCS GDVEYPTK //