RNC2_ASPCL
ID RNC2_ASPCL Reviewed; 132 AA.
AC P00652; A1C9F8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Guanyl-specific ribonuclease C2;
DE Short=RNase C-2;
DE EC=4.6.1.24;
DE Flags: Precursor;
GN ORFNames=ACLA_055300;
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 PROTEIN SEQUENCE OF 27-130.
RX DOI=10.1016/0014-5793(83)80458-X;
RA Bezborodova S.I., Khodova O.M., Stepanov V.M.;
RT "The complete amino acid sequence of ribonuclease C-2 from Aspergillus
RT clavatus.";
RL FEBS Lett. 159:256-258(1983).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'-
CC guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA
CC fragment].; EC=4.6.1.24;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW13482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS027048; EAW13482.1; ALT_SEQ; Genomic_DNA.
DR PIR; A00799; NRASTC.
DR RefSeq; XP_001274908.1; XM_001274907.1.
DR AlphaFoldDB; P00652; -.
DR SMR; P00652; -.
DR EnsemblFungi; EAW13482; EAW13482; ACLA_055300.
DR GeneID; 4707141; -.
DR KEGG; act:ACLA_055300; -.
DR eggNOG; ENOG502SA4T; Eukaryota.
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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046589; F:ribonuclease T1 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR InterPro; IPR016191; Ribonuclease/ribotoxin.
DR Pfam; PF00545; Ribonuclease; 1.
DR SUPFAM; SSF53933; SSF53933; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW Nuclease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 27..132
FT /note="Guanyl-specific ribonuclease C2"
FT /id="PRO_0000137369"
FT ACT_SITE 66
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT DISULFID 28..36
FT /evidence="ECO:0000250"
FT DISULFID 32..129
FT /evidence="ECO:0000250"
FT CONFLICT 53
FT /note="Y -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..132
FT /note="SGW -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 132 AA; 14064 MW; 3E2B1FEEFE0DBF84 CRC64;
MLYNKLITIA ALLVPALAAP QGLDVRDCDY TCGSHCYSAS AVSDAQSAGY QLYSAGQSVG
RSRYPHQYRN YEGFNFPVSG NYYEWPILSS GSTYNGGSPG ADRVVFNDND ELAGLITHTG
ASGNGFVACS GW
