ID   RNCL_ASPCV              Reviewed;         177 AA.
AC   P0CL70; A1C5B3; P49074; P78572;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Ribonuclease clavin;
DE            EC=3.1.27.-;
DE   Flags: Precursor;
GN   Name=cla; Synonyms=c-sar;
OS   Aspergillus clavatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=5057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=NBRC 8605;
RX   PubMed=8706730; DOI=10.1111/j.1432-1033.1996.0272u.x;
RA   Parente D., Raucci G., Celano B., Pacilli A., Zanoni L., Canevari S.,
RA   Adobati E., Colnaghi M.I., Dosio F., Arpicco S., Cattel L., Mele A.,
RA   de Santis R.;
RT   "Clavin, a type-1 ribosome-inactivating protein from Aspergillus clavatus
RT   IFO 8605. cDNA isolation, heterologous expression, biochemical and
RT   biological characterization of the recombinant protein.";
RL   Eur. J. Biochem. 239:272-280(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BCRC 32114;
RX   PubMed=9080594; DOI=10.1016/s0041-0101(96)00170-5;
RA   Huang K.-C., Hwang Y.-Y., Hwu L., Lin A.;
RT   "Characterization of a new ribotoxin gene (c-sar) from Aspergillus
RT   clavatus.";
RL   Toxicon 35:383-392(1997).
CC   -!- FUNCTION: Clavin has the same substrate specificity as alpha-sarcin. It
CC       is specific for purines in both single- and double-stranded RNA. Its
CC       toxic action on eukaryotic cells is the result of cleavage of a single
CC       phosphodiester bond in the 60S subunit of ribosomes.
CC       {ECO:0000269|PubMed:8706730}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ribonuclease U2 family. {ECO:0000305}.
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DR   EMBL; U19383; AAC49407.1; -; mRNA.
DR   EMBL; U48731; AAB42201.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CL70; -.
DR   SMR; P0CL70; -.
DR   EnsemblFungi; EAW14881; EAW14881; ACLA_002920.
DR   VEuPathDB; FungiDB:ACLA_002920; -.
DR   OMA; SSYPHWF; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR   GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProtKB.
DR   GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
DR   InterPro; IPR004025; Fun_ribotoxin.
DR   InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR   InterPro; IPR016191; Ribonuclease/ribotoxin.
DR   PIRSF; PIRSF037430; RNase_U2; 1.
DR   PRINTS; PR01704; FUNRIBOTOXIN.
DR   SUPFAM; SSF53933; SSF53933; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Nuclease; Protein synthesis inhibitor; Secreted;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..177
FT                   /note="Ribonuclease clavin"
FT                   /id="PRO_0000030835"
FT   REGION          98..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        123
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        164
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        33..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        103..159
FT                   /evidence="ECO:0000250"
FT   CONFLICT        13
FT                   /note="T -> M (in Ref. 2; AAB42201)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="W -> L (in Ref. 2; AAB42201)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="G -> V (in Ref. 2; AAB42201)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   177 AA;  19855 MW;  EA602B8555D7022D CRC64;
     MVAIKNLVLV ALTAVTALAM PSPLEERAAT WTCMNEQKNP KTNKYENKRL LYNQNNAESN
     AHHAPLSDGK TGSSYPHWFT NGYDGDGKIL KGRTPIKWGN SDCDRPPKHS KNGDGKNDHY
     LLEFPTFPDG HQYNFDSKKP KEDPGPARVI YTYPNKVFCG IVAHTRENQG DLKLCSH