PHYB_PHYPO
ID PHYB_PHYPO Reviewed; 180 AA.
AC P81477;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Ribonuclease Phyb;
DE Short=RNase Phyb;
DE EC=3.1.26.1;
DE AltName: Full=Physarum polycephalum ribonuclease;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=8514732; DOI=10.1093/oxfordjournals.jbchem.a124062;
RA Inokuchi N., Koyama T., Sawada F., Irie M.;
RT "Purification, some properties, and primary structure of base non-specific
RT ribonucleases from Physarum polycephalum.";
RL J. Biochem. 113:425-432(1993).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10052134; DOI=10.1271/bbb.63.141;
RA Inokuchi N., Saitoh S., Kobayashi H., Itagaki T., Koyama T., Uchiyama S.,
RA Irie M.;
RT "Comparison of base specificity and other enzymatic properties of two
RT protozoan ribonucleases from Physarum polycephalum and Dictyostelium
RT discoideum.";
RL Biosci. Biotechnol. Biochem. 63:141-145(1999).
RN [3]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
CC -!- FUNCTION: Releases mononucleotides from RNA in the order of 3'-GMP, 3'-
CC AMP, and 3'-pyrimidine nucleotides. The base specificities of 2 base
CC recognition sites, the B1 site (for the base at 5'-side of scissile
CC phosphodiester bond) and the B2 site (for the base at 3'-side of the
CC scissile bond) are A, G, U > C and A = G > C > U, respectively.
CC {ECO:0000269|PubMed:10052134, ECO:0000269|PubMed:8514732}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.1;
CC Evidence={ECO:0000269|PubMed:10052134};
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 PIR; JX0262; JX0262.
DR AlphaFoldDB; P81477; -.
DR SMR; P81477; -.
DR iPTMnet; P81477; -.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
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; Nuclease.
FT CHAIN 1..180
FT /note="Ribonuclease Phyb"
FT /id="PRO_0000206506"
FT ACT_SITE 26
FT /evidence="ECO:0000250"
FT ACT_SITE 75
FT /evidence="ECO:0000250"
FT ACT_SITE 79
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8514732"
FT DISULFID 41..82
FT /evidence="ECO:0000250"
SQ SEQUENCE 180 AA; 19724 MW; 1F71BBC5E11FE2B6 CRC64;
KSTSFDFFIF VTEWNASIST EYFTIHGLWP ENSDGSYPSG CSSGKFSTST ISDLIDTMQV
WPSFTGDNAS FWSHEWSKHG TCSGYAEHDF FATVLSLYDQ YDVKSALDNG GIEPGSSSVS
SDSLISVITD NIGGVPVLNC EGSTFASVGL CITKNLELRD CPDNMGSFWD CPAKVYYRNN
