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RNF2_GIBBA
ID   RNF2_GIBBA              Reviewed;         105 AA.
AC   P16412;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Extracellular guanyl-specific ribonuclease Fl2;
DE            Short=RNase Fl2;
DE            EC=4.6.1.24;
OS   Gibberella baccata (Fusarium lateritium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium lateritium species complex.
OX   NCBI_TaxID=5523;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=54228;
RX   PubMed=2806059;
RA   Shlyapnikov S.V., Bezborodova S.I., Chepurnova N.K., Dementiev A.A.;
RT   "A new isoform of intracellular RNAase of Fl2 Fusarium lateritium.
RT   Characteristics and determining the primary structure.";
RL   Dokl. Akad. Nauk SSSR 306:1496-1499(1989).
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   -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
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DR   AlphaFoldDB; P16412; -.
DR   SMR; P16412; -.
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; Pyrrolidone carboxylic acid.
FT   CHAIN           1..105
FT                   /note="Extracellular guanyl-specific ribonuclease Fl2"
FT                   /id="PRO_0000137378"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        58
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        91
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P10282"
FT   DISULFID        6..102
FT                   /evidence="ECO:0000250"
FT   DISULFID        24..83
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   105 AA;  11107 MW;  C467E556628076C4 CRC64;
     QSATTCSSKP YSAQQVRAAA NAACQYYQSN DTAGSTTYPH TYHNYEGFDF AVNGPYQEYP
     IRTSGVYSGG SPGADRVIIN TQCQFAGAIT HTGASGNQFV GCSNT
 
 
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