BBD2_ARATH
ID BBD2_ARATH Reviewed; 329 AA.
AC Q93VH2; Q8LA58; Q9FWS0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Bifunctional nuclease 2;
DE Short=AtBBD2;
DE EC=3.1.-.-;
GN Name=BBD2; OrderedLocusNames=At1g19660; ORFNames=F14P1.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION.
RX PubMed=20018603; DOI=10.1104/pp.109.147645;
RA You M.K., Shin H.Y., Kim Y.J., Ok S.H., Cho S.K., Jeung J.U., Yoo S.D.,
RA Kim J.K., Shin J.S.;
RT "Novel bifunctional nucleases, OmBBD and AtBBD1, are involved in abscisic
RT acid-mediated callose deposition in Arabidopsis.";
RL Plant Physiol. 152:1015-1029(2010).
CC -!- FUNCTION: Bifunctional nuclease with both RNase and DNase activities.
CC Involved in basal defense response. Participates in abscisic acid-
CC derived callose deposition following infection by a necrotrophic
CC pathogen (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bifunctional nuclease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC024609; AAF98407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29879.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29880.1; -; Genomic_DNA.
DR EMBL; AY035016; AAK59521.1; -; mRNA.
DR EMBL; AY059082; AAL15188.1; -; mRNA.
DR EMBL; AK317508; BAH20173.1; -; mRNA.
DR EMBL; AY088015; AAM65561.1; -; mRNA.
DR PIR; D86329; D86329.
DR RefSeq; NP_001031068.1; NM_001035991.1.
DR RefSeq; NP_001322963.1; NM_001332402.1.
DR RefSeq; NP_564093.1; NM_101822.4.
DR AlphaFoldDB; Q93VH2; -.
DR SMR; Q93VH2; -.
DR STRING; 3702.AT1G19660.2; -.
DR PaxDb; Q93VH2; -.
DR PRIDE; Q93VH2; -.
DR ProteomicsDB; 240820; -.
DR EnsemblPlants; AT1G19660.1; AT1G19660.1; AT1G19660.
DR EnsemblPlants; AT1G19660.2; AT1G19660.2; AT1G19660.
DR GeneID; 838553; -.
DR Gramene; AT1G19660.1; AT1G19660.1; AT1G19660.
DR Gramene; AT1G19660.2; AT1G19660.2; AT1G19660.
DR KEGG; ath:AT1G19660; -.
DR Araport; AT1G19660; -.
DR TAIR; locus:2013164; AT1G19660.
DR eggNOG; ENOG502QQ9S; Eukaryota.
DR HOGENOM; CLU_050306_1_0_1; -.
DR InParanoid; Q93VH2; -.
DR OMA; LQAQIVC; -.
DR OrthoDB; 966528at2759; -.
DR PhylomeDB; Q93VH2; -.
DR PRO; PR:Q93VH2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93VH2; baseline and differential.
DR Genevisible; Q93VH2; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030891; C:VCB complex; IBA:GO_Central.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.10.690.10; -; 1.
DR InterPro; IPR036104; BFN_sf.
DR InterPro; IPR003729; Bi_nuclease_dom.
DR InterPro; IPR001943; UVR_dom.
DR Pfam; PF02577; DUF151; 1.
DR Pfam; PF02151; UVR; 1.
DR SUPFAM; SSF103256; SSF103256; 1.
DR PROSITE; PS51658; BFN; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..329
FT /note="Bifunctional nuclease 2"
FT /id="PRO_0000419549"
FT DOMAIN 121..256
FT /note="BFN"
FT DOMAIN 287..322
FT /note="UVR"
FT CONFLICT 37
FT /note="K -> N (in Ref. 5; AAM65561)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> G (in Ref. 5; AAM65561)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="I -> T (in Ref. 5; AAM65561)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="G -> V (in Ref. 5; AAM65561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 37052 MW; BB4A7752CFCBE36E CRC64;
MRSLQAPVVC PSVRPRQLGV SALLVNCSVS KTRSLRKQFW GNQTKNDKSQ AATVNLRLHL
RRYKSIKCLF SSHSDGTGST AENFNENDED YVKSSVLEAV EVKSGPDGFM VKMKDGRQLR
CVHNNPQGGN LPNYAPHSAI VLKMEDGTGL LLPIIVLEMP SVLLMAAMTN VQIARPTMYQ
VVKDMVDKMG YEVRLVRVTT RVHEAYFAEL YLSKVGDKSD CVSFDLRPSD AINIAVRCKV
PIQVNKYLAY SDGMRVIDSG KLSKQTPASD GLLFTELDRP NGQPCFDTKE FDLVRNMMQA
VDEERYDEAA EWRDKLGKFQ AKRKLRKYT
