Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-01305
Entry Name
UniProt Accession
Theoretical PI
9.05
Molecular Weight
37297.67
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Staphylococcal-like nuclease CAN2
Protein Synonyms/Alias
3.1.31.-; Calcium-dependent nuclease 2; AtCAN2; Ca(2+)-dependent nuclease 2;
Gene Name
CAN2
Gene Synonyms/Alias
At2g40410; T3G21.18;
Created Date
03-SEP-2014
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
12
Canonical
LTFLYGKCCKPTTTD
[1]
S-Palmitoylation
13
Canonical
TFLYGKCCKPTTTDD
[1]
S-Palmitoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Predicted from GPS-Lipid
Functional Description
Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. Possesses activity toward the single-stranded DNA, double-stranded DNA and RNA. May be involved in genomic DNA degradation during programmed cell death.
Sequence Annotation
Domain: 140 316 TNase-like.
Active site: 223 223
Active site: 231 231
Active site: 265 265
Metal binding site: 153 153 Calcium.
Metal binding site: 228 228 Calcium.
Protein Length
332 AA.
Protein Sequence
(Canonical)
MGNALTFLYG KCCKPTTTDD SLGPHGVSAA TVGVSALAHD LFNFEITSQV PEGLGRYVQS  60
SRKAQANWYR KILEAWKQAK PPPQTAEEAS RLVTDILKRN QKADVEGLLS FYGLPLSHTL  120
VEVTVEAPVS LPEGILFEFQ TLPVDPKAVA DGDTITVYVS TSEPVVSSSV PREVNLAAVQ  180
RAKAREKRNY PKADELHQKI IDSGYRVLNI ENEEVLARKF RIRLRGIDAP ESQMPFGKEA  240
QEGLLKIVGR KSLKVLVYGE DQYGRCVGDL YCNGIFVQEA MLKKGLAWHY LAYDKRPVLA  300
KWEKEARQKR IGLWASSNPE KPWDWRKNNR RE                                332
FASTA
(Canonical)
>LipidDB-3702-01305|F4IH31
MGNALTFLYGKCCKPTTTDDSLGPHGVSAATVGVSALAHDLFNFEITSQVPEGLGRYVQS
SRKAQANWYRKILEAWKQAKPPPQTAEEASRLVTDILKRNQKADVEGLLSFYGLPLSHTL
VEVTVEAPVSLPEGILFEFQTLPVDPKAVADGDTITVYVSTSEPVVSSSVPREVNLAAVQ
RAKAREKRNYPKADELHQKIIDSGYRVLNIENEEVLARKFRIRLRGIDAPESQMPFGKEA
QEGLLKIVGRKSLKVLVYGEDQYGRCVGDLYCNGIFVQEAMLKKGLAWHYLAYDKRPVLA
KWEKEARQKRIGLWASSNPEKPWDWRKNNRRE
Gene Ontology
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0004520; F:endodeoxyribonuclease activity; IDA:TAIR
GO:0004521; F:endoribonuclease activity; IDA:TAIR
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0003676; F:nucleic acid binding; IEA:InterPro
GO:0006308; P:DNA catabolic process; IDA:TAIR
GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:GOC
GO:0006401; P:RNA catabolic process; IDA:TAIR
GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:GOC
Interpro
InterPro; IPR016071; Staphylococal_nuclease_OB-fold
Pfam
Pfam; PF00565; SNase;
SMART
SMART; SM00318; SNc;
PROSITE
PROSITE; PS50830; TNASE_3;
PRINTS