ID S8AF23_DACHA Unreviewed; 658 AA.
AC S8AF23;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=rRNA N-glycosylase {ECO:0000256|ARBA:ARBA00012001};
DE EC=3.2.2.22 {ECO:0000256|ARBA:ARBA00012001};
GN ORFNames=H072_6480 {ECO:0000313|EMBL:EPS39741.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS39741.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS39741.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS39741.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC adenosine on the 28S rRNA.; EC=3.2.2.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000237};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPS39741.1}.
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DR EMBL; AQGS01000454; EPS39741.1; -; Genomic_DNA.
DR RefSeq; XP_011112271.1; XM_011113969.1.
DR AlphaFoldDB; S8AF23; -.
DR eggNOG; ENOG502S2GC; Eukaryota.
DR HOGENOM; CLU_416785_0_0_1; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0017148; P:negative regulation of translation; IEA:InterPro.
DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1.
DR InterPro; IPR036041; Ribosome-inact_prot_sf.
DR InterPro; IPR017989; Ribosome_inactivat_1/2.
DR InterPro; IPR001574; Ribosome_inactivat_prot.
DR InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR PANTHER; PTHR33453; -; 1.
DR PANTHER; PTHR33453:SF48; RRNA N-GLYCOSYLASE; 1.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..658
FT /note="rRNA N-glycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004548440"
SQ SEQUENCE 658 AA; 71719 MW; 8C2C5F2502736E37 CRC64;
MRVRYFVAYV GVAVSLVHAL PGGKKAANGA KGNEPGPSRA LPSTPAFNAE FTFKLDAIDN
GGERYQAEIN RFRTEKGELD NGVLYLPHPK NPPEFFDVVL ETTSSNLDVK LQKDNLYLLA
YRSNDGWREV KGSELICSTK AEFPADYPDL EKVAAFDTSK GLKGRYNTRV GKSSLETAID
TLLSNKASPK EAARAFLVLT QMLPESIRIR EISEHIGTSW GENEIIPFTL VEKENGWKQA
KGETLGIAKR PEPEKPGTAK KIKACKRGKR DICIPELEAS EGQMGNKKQP QSNLNQKNIA
GSKPKLSELK AFGGKVSGGV GVLGAVVITC ALSEPLQEES KKLRKRIDVL AGFLNIPSTV
FNGITGGLSD LFNGGNGDAF MKSVNDGLKA GGDLPGQIGE QFQKAWSKEN WESLVRSADK
GVQAFLDAPG QVGDQITKAW SKENREAFVK STGDLVKAIR ETPALLECGL YDLREAAEDV
VIAFQKAPQQ VASELQKFDR GLDNLGPDGK KAFYAITGSL GVFAPSQFDE IGYMAPGICH
IVNSIGIPKF QKSPVSKCPL VISTRFNRVG EVVRTMFMIH KGATGSNDKK AFWDKLELSV
WGKLAYLEIQ GRSDPSLKSQ SEKAWTAVLD GHTPSDLPEV SDDDKLKLWA VIVRGQLK
//
