CRYD_SOLLC
ID CRYD_SOLLC Reviewed; 577 AA.
AC Q38JU2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Cryptochrome DASH, chloroplastic/mitochondrial {ECO:0000303|PubMed:16876787};
DE AltName: Full=Cryptochrome-3 {ECO:0000303|PubMed:16876787};
DE AltName: Full=Protein CRY-DASH {ECO:0000303|PubMed:16876787};
DE Flags: Precursor;
GN Name=CRYD {ECO:0000303|PubMed:16876787};
GN Synonyms=CRY3 {ECO:0000303|PubMed:16876787};
GN OrderedLocusNames=Solyc08g074270 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP LIGHT.
RC STRAIN=cv. Moneymaker;
RX PubMed=16876787; DOI=10.1016/j.febslet.2006.07.044;
RA Facella P., Lopez L., Chiappetta A., Bitonti M.B., Giuliano G.,
RA Perrotta G.;
RT "CRY-DASH gene expression is under the control of the circadian clock
RT machinery in tomato.";
RL FEBS Lett. 580:4618-4624(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: May have a photoreceptor function and might bind ss- and ds-
CC DNA in a sequence non-specific manner. Lacks photolyase activity. Has a
CC potential role in detecting the dawn and dusk transitions and,
CC consequently, in circadian input pathways.
CC {ECO:0000305|PubMed:16876787}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q84KJ5};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q84KJ5};
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250|UniProtKB:Q84KJ5};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC {ECO:0000250|UniProtKB:Q84KJ5};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q84KJ5}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q84KJ5}.
CC -!- TISSUE SPECIFICITY: Expressed in the endosperm and embryo 96 hours
CC after seed imbibition. In the embryo, detected in the root meristem,
CC the root cap, the shoot apical meristem and the epidermis of
CC cotyledons. In adult plants, detcted in roots, the whole leaf lamina,
CC the stem and in glandular trichomes. {ECO:0000269|PubMed:16876787}.
CC -!- INDUCTION: Circadian-regulation showing peaks at dawn and at dusk.
CC {ECO:0000269|PubMed:16876787}.
CC -!- MISCELLANEOUS: 5,10-methenyltetrahydrofolate (MTHF) acts as a
CC functional antenna for the photoreduction of FAD.
CC {ECO:0000250|UniProtKB:Q84KJ5}.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
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DR EMBL; DQ222242; ABB01166.2; -; Genomic_DNA.
DR RefSeq; NP_001296304.1; NM_001309375.1.
DR AlphaFoldDB; Q38JU2; -.
DR SMR; Q38JU2; -.
DR STRING; 4081.Solyc08g074270.2.1; -.
DR PaxDb; Q38JU2; -.
DR PRIDE; Q38JU2; -.
DR GeneID; 101248230; -.
DR KEGG; sly:101248230; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_6_2_1; -.
DR InParanoid; Q38JU2; -.
DR OrthoDB; 378952at2759; -.
DR PhylomeDB; Q38JU2; -.
DR Proteomes; UP000004994; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0000719; P:photoreactive repair; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR014133; Cry_DASH.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; PTHR11455; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; SSF48173; 1.
DR SUPFAM; SSF52425; SSF52425; 1.
DR TIGRFAMs; TIGR02765; crypto_DASH; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Chromophore; DNA-binding; FAD; Flavoprotein; Mitochondrion;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 54..577
FT /note="Cryptochrome DASH, chloroplastic/mitochondrial"
FT /id="PRO_0000235319"
FT DOMAIN 78..219
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000255"
FT REGION 550..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 66011 MW; BB875FE48064211D CRC64;
MIKQPFLLTK FTPFSSKSKH TLFTFHCNFS IKMASLTART TPTVQNVPGL TPEEMERVCE
QTFQRYESGG LGKRKGKGVA IVWFRNDLRV LDNEALLRAW VSSEAILPVY CVDPRLFGTT
HYFGMPKTGA LRAQFIIECL NDLKRNLVKR GLDLLIQHGK PEDIVPSLAK AYKAHTVYAH
KETCSEEVKV EKMVTRNLQK LVSPSSGGIG NDPGSGNTTK LELVWGSTMY HIDDLPFDCE
SLPDVYTQFR KSVEYKSKVR NCTKLPTSFG PPPEVGDWGH VPQVSELGLQ QEKVSKGMNF
VGGESAALGR VHDYFWKKDL LKVYKETRNG MLGADYSTKF SPWLASGSLS PRFIYEEVKR
YEKERLSNDS TYWVLFELIW RDYFRFLSIK LANLLFQAGG PQKVNINWSQ DQTMFDAWRR
GQTGYPLIDA NMKELAATGY MSNRGRQIVC SFLVRDMGID WRMGAEWFET CLLDYDPCSN
YGNWTYGAGV GNDPREDRYF SIPKQAQNYD PEGEFVAYWL PELRALPREK RHSPGMMYLN
PIVALKHGYT KKTGDSKTAF SSRRGRPEDN RRKRHGY
