RNS11_NICAL
ID RNS11_NICAL Reviewed; 196 AA.
AC Q7SID5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Ribonuclease S-F11;
DE EC=4.6.1.19 {ECO:0000250|UniProtKB:P04007};
DE AltName: Full=SF11-RNase;
DE AltName: Full=Stylar glycoprotein F11;
OS Nicotiana alata (Winged tobacco) (Persian tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4087;
RN [1] {ECO:0000305, ECO:0000312|PDB:1IOO}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), SUBUNIT, ACTIVE SITE, GLYCOSYLATION
RP AT ASN-28, AND DISULFIDE BONDS.
RX PubMed=11724536; DOI=10.1006/jmbi.2001.5127;
RA Ida K., Norioka S., Yamamoto M., Kumasaka T., Yamashita E., Newbigin E.,
RA Clarke A.E., Sakiyama F., Sato M.;
RT "The 1.55 A resolution structure of Nicotiana alata S(F11)-RNase associated
RT with gametophytic self-incompatibility.";
RL J. Mol. Biol. 314:103-112(2001).
CC -!- FUNCTION: Self-incompatibility (SI) is the inherited ability of a
CC flowering plant to prevent self-fertilization by discriminating between
CC self and non-self pollen during pollination. In many species of the
CC Solanaceae, self-incompatibility is controlled by the single,
CC multiallelic locus S (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173118; EC=4.6.1.19;
CC Evidence={ECO:0000250|UniProtKB:P04007, ECO:0000255|PROSITE-
CC ProRule:PRU10045};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11724536}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNase T2 family.
CC {ECO:0000269|PubMed:11724536}.
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DR PDB; 1IOO; X-ray; 1.55 A; A/B=1-196.
DR PDBsum; 1IOO; -.
DR AlphaFoldDB; Q7SID5; -.
DR SMR; Q7SID5; -.
DR iPTMnet; Q7SID5; -.
DR EvolutionaryTrace; Q7SID5; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR CDD; cd01061; RNase_T2_euk; 1.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR InterPro; IPR001568; RNase_T2-like.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR018188; RNase_T2_His_AS_1.
DR PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00530; RNASE_T2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase;
KW Nuclease; Secreted.
FT CHAIN 1..196
FT /note="Ribonuclease S-F11"
FT /id="PRO_0000235824"
FT ACT_SITE 32
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045,
FT ECO:0000269|PubMed:11724536"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045,
FT ECO:0000269|PubMed:11724536"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11724536"
FT DISULFID 16..21
FT /evidence="ECO:0000269|PubMed:11724536"
FT DISULFID 46..94
FT /evidence="ECO:0000269|PubMed:11724536"
FT DISULFID 153..186
FT /evidence="ECO:0000269|PubMed:11724536"
FT DISULFID 169..180
FT /evidence="ECO:0000269|PubMed:11724536"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1IOO"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:1IOO"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1IOO"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1IOO"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:1IOO"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:1IOO"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:1IOO"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1IOO"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1IOO"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:1IOO"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:1IOO"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1IOO"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:1IOO"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1IOO"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:1IOO"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1IOO"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1IOO"
SQ SEQUENCE 196 AA; 23093 MW; 12B30F3E5440E1BD CRC64;
DFEYLQLVLT WPASFCYANH CERIAPNNFT IHGLWPDNVK TRLHNCKPKP TYSYFTGKML
NDLDKHWMQL KFEQDYGRTE QPSWKYQYIK HGSCCQKRYN QNTYFGLALR LKDKFDLLRT
LQTHRIIPGS SYTFQDIFDA IKTVSQENPD IKCAEVTKGT PELYEIGICF TPNADSMFRC
PQSDTCDKTA KVLFRR
