RNCL_ASPCL
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 25-MAY-2022, entry version 45.
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; 5057.CADACLAP00000058; -.
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; 1464399at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
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 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
