SNM1_ARATH
ID SNM1_ARATH Reviewed; 484 AA.
AC Q38961; Q96280;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DNA cross-link repair protein SNM1;
DE Short=AtSNM1;
GN Name=SNM1; OrderedLocusNames=At3g26680; ORFNames=MLJ15.8;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=8932388; DOI=10.1093/nar/24.21.4313;
RA Quigley F., Dao P., Cottet A., Mache R.;
RT "Sequence analysis of an 81 kb contig from Arabidopsis thaliana chromosome
RT III.";
RL Nucleic Acids Res. 24:4313-4318(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=15448639; DOI=10.1038/sj.embor.7400256;
RA Molinier J., Stamm M.-E., Hohn B.;
RT "SNM-dependent recombinational repair of oxidatively induced DNA damage in
RT Arabidopsis thaliana.";
RL EMBO Rep. 5:994-999(2004).
CC -!- FUNCTION: May be required for repair of DNA lesions formed after
CC exposure to oxidative stress. {ECO:0000269|PubMed:15448639}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- INDUCTION: Induced by bleomycin, methyl methane sulphonate and hydrogen
CC peroxide, which are known to induce oxidative lesions in DNA. Also
CC induced by bacterial flagellin, which is known to elicit plant defense
CC responses and a rapid oxidative burst, and by xylanase.
CC {ECO:0000269|PubMed:15448639}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
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DR EMBL; X97827; CAA66406.1; -; mRNA.
DR EMBL; X98130; CAA66817.1; -; Genomic_DNA.
DR EMBL; AB026648; BAB01732.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77196.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77197.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77198.1; -; Genomic_DNA.
DR EMBL; AK117422; BAC42087.1; -; mRNA.
DR EMBL; BT005000; AAO50533.1; -; mRNA.
DR RefSeq; NP_001319649.1; NM_001338816.1.
DR RefSeq; NP_001319650.1; NM_001338817.1.
DR RefSeq; NP_850635.1; NM_180304.2.
DR AlphaFoldDB; Q38961; -.
DR SMR; Q38961; -.
DR STRING; 3702.AT3G26680.2; -.
DR PaxDb; Q38961; -.
DR PRIDE; Q38961; -.
DR ProteomicsDB; 234476; -.
DR EnsemblPlants; AT3G26680.1; AT3G26680.1; AT3G26680.
DR EnsemblPlants; AT3G26680.2; AT3G26680.2; AT3G26680.
DR EnsemblPlants; AT3G26680.3; AT3G26680.3; AT3G26680.
DR GeneID; 822280; -.
DR Gramene; AT3G26680.1; AT3G26680.1; AT3G26680.
DR Gramene; AT3G26680.2; AT3G26680.2; AT3G26680.
DR Gramene; AT3G26680.3; AT3G26680.3; AT3G26680.
DR KEGG; ath:AT3G26680; -.
DR Araport; AT3G26680; -.
DR TAIR; locus:2090832; AT3G26680.
DR eggNOG; KOG1361; Eukaryota.
DR HOGENOM; CLU_005260_2_2_1; -.
DR InParanoid; Q38961; -.
DR OMA; KSGPIYC; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q38961; -.
DR PRO; PR:Q38961; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38961; baseline and differential.
DR Genevisible; Q38961; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Nucleus; Reference proteome.
FT CHAIN 1..484
FT /note="DNA cross-link repair protein SNM1"
FT /id="PRO_0000209128"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 484
FT /note="R -> P (in Ref. 1; CAA66406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 55161 MW; B429A279811EA414 CRC64;
MDFSDEDDDE NCFGSRFNDG VNEEEEDEEG FVFNDDVEEN EEEEGFASDF YKAGSDWSCL
VEDEETVSSS VKKMKQSNLF QIWGLQENSP DTTKKMKQTD LFQSWGLQKP SPFTSPASNS
AKKTTSALGK RRRDSSFSND SPRPCPFYKK LPGTPFTVDA FRYGCVQGCS AYFLTHFHAD
HYIGLTKAWS HGPIYCSSLT SRLLRLSLSV NPSSIHPLEL DVEYTINGIK VTLIEANHCP
GAALIHFRLL DGTCYLHTGD FRASKQMQTH PLLFNQRVHV LYLDTTYCNP RYKFPSKEDV
LSYVVRITKD FLRKQPKTLI VVGSYSIGKE CVYLAIAKAL GVKIFANASR RRILQSFGWD
DISKNLSTDG KATCLHVLPM SSLKVERLDE HLKIYREQYG AVLAFRPTGW TYSEKIGEHL
DLIKPTSRGK ITIYGVPYSE HSSFTELREF VQFLRPDKII PTVNNGNAGT REKMQSCFRE
WLRR
