RNRH_RHINI
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 25-MAY-2022, entry version 112.
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}.
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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 CDD; cd01061; RNase_T2_euk; 1.
DR Gene3D; 3.90.730.10; -; 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; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 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
