ID   RNF1_ARTBC              Reviewed;         129 AA.
AC   D4AVI0;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Extracellular guanyl-specific ribonuclease ARB_00194 {ECO:0000305};
DE            Short=RNase ARB_00194 {ECO:0000305};
DE            EC=4.6.1.24 {ECO:0000250|UniProtKB:P10282};
DE   Flags: Precursor;
GN   ORFNames=ARB_00194;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
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; Evidence={ECO:0000250|UniProtKB:P10282};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABSU01000013; EFE32736.1; -; Genomic_DNA.
DR   RefSeq; XP_003013376.1; XM_003013330.1.
DR   AlphaFoldDB; D4AVI0; -.
DR   SMR; D4AVI0; -.
DR   EnsemblFungi; EFE32736; EFE32736; ARB_00194.
DR   GeneID; 9519416; -.
DR   KEGG; abe:ARB_00194; -.
DR   eggNOG; ENOG502SA4T; Eukaryota.
DR   HOGENOM; CLU_111658_2_0_1; -.
DR   OMA; STYPHRY; -.
DR   Proteomes; UP000008866; 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   PIRSF; PIRSF037430; RNase_U2; 1.
DR   SUPFAM; SSF53933; SSF53933; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endonuclease; Hydrolase; Lyase; Nuclease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..129
FT                   /note="Extracellular guanyl-specific ribonuclease
FT                   ARB_00194"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434677"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000250|UniProtKB:P10282"
FT   ACT_SITE        81
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10282"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P10282"
FT   DISULFID        28..125
FT                   /evidence="ECO:0000250|UniProtKB:P10282"
FT   DISULFID        46..106
FT                   /evidence="ECO:0000250|UniProtKB:P10282"
SQ   SEQUENCE   129 AA;  13016 MW;  64F373FEFB8C7799 CRC64;
     MKFLALLSLV AAATAAPAAL EARGATTCGS TSYSASQVTA ASNAACNYVQ SGTTAGGSTY
     PHQYRNYEGF YFQGLSGPFY EFPLRTSGVY NGGSPGADRV IITGNCDEAG QITHTGASGS
     GFVACSGTS