ID A0A1E5UR27_9POAL Unreviewed; 598 AA.
AC A0A1E5UR27;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Ribosome-inactivating protein {ECO:0000256|RuleBase:RU004915};
DE Contains:
DE RecName: Full=Ribosome-inactivating protein chain A {ECO:0000256|RuleBase:RU004915};
DE AltName: Full=rRNA N-glycosidase {ECO:0000256|RuleBase:RU004915};
DE EC=3.2.2.22 {ECO:0000256|RuleBase:RU004915};
DE Contains:
DE RecName: Full=Ribosome-inactivating protein chain B {ECO:0000256|RuleBase:RU004915};
GN ORFNames=BAE44_0023713 {ECO:0000313|EMBL:OEL15268.1};
OS Dichanthelium oligosanthes.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Dichantheliinae; Dichanthelium.
OX NCBI_TaxID=888268 {ECO:0000313|EMBL:OEL15268.1, ECO:0000313|Proteomes:UP000095767};
RN [1] {ECO:0000313|EMBL:OEL15268.1, ECO:0000313|Proteomes:UP000095767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Kellogg 1175 {ECO:0000313|Proteomes:UP000095767};
RC TISSUE=Leaf {ECO:0000313|EMBL:OEL15268.1};
RA Studer A.J., Schnable J.C., Brutnell T.P.;
RT "The draft genome of Dichanthelium oligosanthes: A C3 panicoid grass
RT species.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The A chain is responsible for inhibiting protein synthesis
CC through the catalytic inactivation of 60S ribosomal subunits by
CC removing adenine from position 4,324 of 28S rRNA. The B chain binds to
CC cell receptors and probably facilitates the entry into the cell of the
CC A chain; B chains are also responsible for cell agglutination (lectin
CC activity). {ECO:0000256|RuleBase:RU004915}.
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 ECO:0000256|RuleBase:RU004915};
CC -!- SUBUNIT: Might form dimers or tetramers of disulfide-linked A and B
CC chains. {ECO:0000256|RuleBase:RU004915}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
CC {ECO:0000256|RuleBase:RU004915}.
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:OEL15268.1}.
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DR EMBL; LWDX02067398; OEL15268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5UR27; -.
DR STRING; 888268.A0A1E5UR27; -.
DR OrthoDB; 1039802at2759; -.
DR Proteomes; UP000095767; Unassembled WGS sequence.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1.
DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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 InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR33453; -; 1.
DR PANTHER; PTHR33453:SF48; RRNA N-GLYCOSYLASE; 1.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU004915};
KW Plant defense {ECO:0000256|RuleBase:RU004915};
KW Protein synthesis inhibitor {ECO:0000256|RuleBase:RU004915};
KW Reference proteome {ECO:0000313|Proteomes:UP000095767};
KW Signal {ECO:0000256|SAM:SignalP}; Toxin {ECO:0000256|RuleBase:RU004915}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..598
FT /note="Ribosome-inactivating protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009187268"
FT DOMAIN 334..465
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 469..597
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 63627 MW; 81CD614E9FF80602 CRC64;
MKGGTLKFNL MLSLVLSWLC LASSALASET ANNAAVLKDY PLVTYSTAAA TPERYNSFIF
SVRAALVSKS KGKSNGIPVL LSENDPLAIE TYLNITLTNK AGYSVSLKMD VTGAYFTAYV
AGKYSCLLKR SGGKFSSATC YSDPWGSSVD TSSSRDSGGG YPAGDVDDLE AAASTWRAKD
LDEAVSTLFL YPTSKCTDAE LSRAVAACDM MIASAATFPY IQRRMSAGMW DGNGVSDDPS
LHGLQARWPT LSTAVQESFQ GAFAAPVTVQ RSNGKVGIRV DNVRAAMPLV SFLEHDNCKE
KAKLPMVIRS VVDEAADDMM GGAAAAPEAC SKAEPTMRII GPEGRCVDVP NNWYYEGKQL
QLWSCKSYDD VNQLWTFKRD GTIRSKGTWC LTASSATAAD SRVVISSCPP RGAAANDRAV
WDVRADGTIA LRCSGLVLSV PNSALFAGLT VRRDDRGTGQ SWTPTNNTTP LAAPIVGYGD
LCLQVDSAGT VSLAACGGDG KGMSWSLYPD GSVRPPAWLF FQWRCLAADA SGRVSVNYCD
GSGSACERWV FRSDGTILNT GTGNVLDARP SATKSGCYDV VVSPARKGRA TQQWAVML
//
