ID A0A1Z5S7L0_SORBI Unreviewed; 507 AA.
AC A0A1Z5S7L0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000256|ARBA:ARBA00014046};
DE EC=4.1.99.3 {ECO:0000256|ARBA:ARBA00013149};
DE AltName: Full=DNA photolyase {ECO:0000256|ARBA:ARBA00031671};
GN ORFNames=SORBI_3001G261545 {ECO:0000313|EMBL:OQU91920.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:OQU91920.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:OQU91920.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC DNA).; EC=4.1.99.3; Evidence={ECO:0000256|ARBA:ARBA00033999};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-2 family.
CC {ECO:0000256|ARBA:ARBA00006409}.
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DR EMBL; CM000760; OQU91920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5S7L0; -.
DR STRING; 4558.A0A1Z5S7L0; -.
DR EnsemblPlants; OQU91920; OQU91920; SORBI_3001G261545.
DR Gramene; OQU91920; OQU91920; SORBI_3001G261545.
DR eggNOG; KOG0133; Eukaryota.
DR InParanoid; A0A1Z5S7L0; -.
DR Proteomes; UP000000768; Chromosome 1.
DR ExpressionAtlas; A0A1Z5S7L0; baseline and differential.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:EnsemblPlants.
DR GO; GO:0000719; P:photoreactive repair; IBA:GO_Central.
DR GO; GO:0009650; P:UV protection; IEA:EnsemblPlants.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR008148; DNA_photolyase_2.
DR InterPro; IPR032673; DNA_photolyase_2_CS.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00591; phr2; 1.
DR PANTHER; PTHR10211:SF0; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE; 1.
DR PANTHER; PTHR10211; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS01083; DNA_PHOTOLYASES_2_1; 1.
DR PROSITE; PS01084; DNA_PHOTOLYASES_2_2; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT DOMAIN 26..164
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 483..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 57407 MW; EC9B5F725A3C96A4 CRC64;
MPPASPNLVH PSRVRILHPG GGHMPGPVVY WMLRDQRLAD NWALLHAAEL AAASAPAAPL
AIAFTLFPRP FLLGAHLRQL GFLLRGLRRL AADAHARGLP FFLLEGGPAE VPALVRRLGA
SALVTDFSPL RPVREAFDAV VHELLRDAAD MAVHQVDAHN VVPVWVATGK LEYSAKTFRS
KVSKVMDEYL VEYPELPGWT PWCMEQPKDV DWDALINSIF SEAENVPEID WCEPGEAAAM
EVLLGNNDGF LTKRIKSYDT GRNDPTKPHA LSCLSPYLHF GHISAQRCAM EAKKRRHLSP
KSVDAFLEEL IIRRELADNF CYYQPNYDSL AGAWEWARKT LMDHAGDKRE HIYTREQLEN
AKTSDPLWNA SQLEMVHHGK MHGFMRMYWA KKILEWTSGP EEALSIAIYL NDKYHIDGRD
PNGYVGCMWS ICGLHDQGWK ERPVFGKIRY MNYAGCKRKF DVDAYISYVK SLVARAKKRK
TEEYLNPRSK NPKSELGQQL NMSKALI
//
