RNT2_ASPOR
ID RNT2_ASPOR Reviewed; 276 AA.
AC P10281; Q2UQZ3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Ribonuclease T2;
DE Short=RNase T2;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=rntB; ORFNames=AO090005001044;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=1913876; DOI=10.1007/bf00309597;
RA Ozeki K., Kitamoto K., Gomi K., Kumagai C., Tamura G., Hara S.;
RT "Cloning and nucleotide sequence of the genomic ribonuclease T2 gene (rntB)
RT from Aspergillus oryzae.";
RL Curr. Genet. 19:367-373(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [3]
RP PROTEIN SEQUENCE OF 18-256.
RX PubMed=3169020; DOI=10.1111/j.1432-1033.1988.tb14331.x;
RA Kawata Y., Sakiyama F., Tamaoki H.;
RT "Amino-acid sequence of ribonuclease T2 from Aspergillus oryzae.";
RL Eur. J. Biochem. 176:683-697(1988).
RN [4]
RP ACTIVE SITES.
RX PubMed=2298207; DOI=10.1111/j.1432-1033.1990.tb15303.x;
RA Kawata Y., Sakiyama F., Hayashi F., Kyogoku Y.;
RT "Identification of two essential histidine residues of ribonuclease T2 from
RT Aspergillus oryzae.";
RL Eur. J. Biochem. 187:255-262(1990).
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 -!- MISCELLANEOUS: Preference for adenylic acid.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE56022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X61086; CAA43400.1; -; Genomic_DNA.
DR EMBL; AP007151; BAE56022.1; ALT_INIT; Genomic_DNA.
DR PIR; JU0205; JU0205.
DR RefSeq; XP_001818024.1; XM_001817972.2.
DR AlphaFoldDB; P10281; -.
DR SMR; P10281; -.
DR STRING; 510516.P10281; -.
DR EnsemblFungi; BAE56022; BAE56022; AO090005001044.
DR GeneID; 5989969; -.
DR KEGG; aor:AO090005001044; -.
DR Proteomes; UP000006564; Chromosome 1.
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 Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW Hydrolase; Lyase; Nuclease; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:3169020"
FT CHAIN 18..276
FT /note="Ribonuclease T2"
FT /id="PRO_0000030965"
FT ACT_SITE 70
FT /evidence="ECO:0000269|PubMed:2298207"
FT ACT_SITE 128
FT /evidence="ECO:0000250"
FT ACT_SITE 132
FT /evidence="ECO:0000269|PubMed:2298207"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 22..41
FT /evidence="ECO:0000250"
FT DISULFID 30..77
FT /evidence="ECO:0000250"
FT DISULFID 40..143
FT /evidence="ECO:0000250"
FT DISULFID 85..135
FT DISULFID 208..242
SQ SEQUENCE 276 AA; 30742 MW; 88A328A539088EAC CRC64;
MGMLALGAMQ LAAGAVFEFP SCPKDIPFSC QNSTAVADSC CFNSPGGALL QTQFWDTNPP
SGPSDSWTIH GLWPDNCDGS YGQFCDKSRE YSNITAILQE QGRTELLSYM KKYWPNYEGD
DEEFWEHEWN KHGTCINTIE PSCYKDYSPQ KEVGDYLQKT VDLFKGLDSY KALAKAGIVP
DSSKTYKRSE IESALAAIHD GKKPYISCED GALNEIWYFY NIKGNAITGE YQPIDTLTSP
GCSTSGIKYL PKKSENSTAS AWKFRSDKAS QSVRFN
