ID A0A2J6LSL4_LACSA Unreviewed; 215 AA.
AC A0A2J6LSL4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN ORFNames=LSAT_2X119841 {ECO:0000313|EMBL:PLY90327.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY90327.1};
RN [1] {ECO:0000313|EMBL:PLY90327.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLY90327.1}.
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DR EMBL; NBSK01002402; PLY90327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6LSL4; -.
DR STRING; 4236.A0A2J6LSL4; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_2X119841_mrna; cds-PLY90327.1; gene-LSAT_2X119841.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_2X119841_mrna; cds-PLY90327.1; gene-LSAT_2X119841.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:UniProt.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd14702; bZIP_plant_GBF1; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR045314; bZIP_plant_GBF1.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR PANTHER; PTHR45764:SF85; BZIP TRANSCRIPTION FACTOR 11; 1.
DR PANTHER; PTHR45764; BZIP TRANSCRIPTION FACTOR 44; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 81..144
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 54..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 215 AA; 24439 MW; 9867DB85FD202865 CRC64;
MQLHHQKHHR TYITNYNKAI EQLDDAITKG DASTVVKFQS TIKFNGEGIL MASSSGTTTS
SGGSYPIQNS GSDEDLQQLM DQRRKKRMIS NRESARRSRK RKQKHLDDLK SQLNQLRNEN
NQIISSVSIT TQHYISVEAE NSVLRAQVAE LSHRLQSLNE MIAFMYQPVD TGCRFEDEQY
GSGGGTEFVD EFMNNSLSYL YANQPIMASA DMIQY
//
