ID   RNCL_ASPCL              Reviewed;         177 AA.
AC   P0CL71; A1C5B3; P49074; P78572;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Ribonuclease clavin;
DE            EC=3.1.27.-;
DE   Flags: Precursor;
GN   Name=cla; Synonyms=c-sar; ORFNames=ACLA_002920;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
RN   [2]
RP   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   [3]
RP   FUNCTION.
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, ECO:0000269|PubMed:9080594}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ribonuclease U2 family. {ECO:0000305}.
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DR   EMBL; DS027004; EAW14881.1; -; Genomic_DNA.
DR   RefSeq; XP_001276307.1; XM_001276306.1.
DR   AlphaFoldDB; P0CL71; -.
DR   SMR; P0CL71; -.
DR   STRING; 344612.P0CL71; -.
DR   EnsemblFungi; EAW14881; EAW14881; ACLA_002920.
DR   GeneID; 4708501; -.
DR   KEGG; act:ACLA_002920; -.
DR   VEuPathDB; FungiDB:ACLA_002920; -.
DR   eggNOG; ENOG502SV0S; Eukaryota.
DR   HOGENOM; CLU_1768332_0_0_1; -.
DR   OMA; SSYPHWF; -.
DR   OrthoDB; 2344918at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd00606; fungal_RNase; 1.
DR   Gene3D; 3.10.450.30; Microbial ribonucleases; 1.
DR   InterPro; IPR004025; Fun_ribotoxin.
DR   InterPro; IPR016191; Ribonuclease/ribotoxin.
DR   InterPro; IPR048269; RNase_U2.
DR   PIRSF; PIRSF037430; RNase_U2; 1.
DR   PRINTS; PR01704; FUNRIBOTOXIN.
DR   SUPFAM; SSF53933; Microbial ribonucleases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Nuclease; Protein synthesis inhibitor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..177
FT                   /note="Ribonuclease clavin"
FT                   /id="PRO_0000406983"
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"
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
//