ID A0A2P6TLL3_CHLSO Unreviewed; 626 AA.
AC A0A2P6TLL3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cryptochrome DASH {ECO:0000256|RuleBase:RU367151};
GN ORFNames=C2E21_6275 {ECO:0000313|EMBL:PRW45174.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW45174.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW45174.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- FUNCTION: May have a photoreceptor function.
CC {ECO:0000256|RuleBase:RU367151}.
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|RuleBase:RU367151};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC {ECO:0000256|RuleBase:RU367151};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1,
CC ECO:0000256|RuleBase:RU367151};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1,
CC ECO:0000256|RuleBase:RU367151};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862, ECO:0000256|RuleBase:RU367151}.
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:PRW45174.1}.
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DR EMBL; LHPG02000012; PRW45174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6TLL3; -.
DR STRING; 3076.A0A2P6TLL3; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000239899; Unassembled WGS sequence.
DR GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 2.
DR Gene3D; 3.40.50.620; HUPs; 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; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR02765; crypto_DASH; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF22; CRYPTOCHROME DASH; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 2.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 2.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|RuleBase:RU367151};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}; Lyase {ECO:0000313|EMBL:PRW45174.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239899}.
FT DOMAIN 56..198
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 562..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 365..372
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 462..464
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 396
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 449
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 472
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 626 AA; 68332 MW; EFF78B4D39A7F2CB CRC64;
MAALAAAGFC TTARIAACRG SLRSSATQRV RARWVVVQVR MSSGGGGSSG GGGGNRAVLW
FRGTDLRVHD NVVVHEAARR VQAGQVSEVL PLYCFDPRFF SASAWGNPKT GAFRAQFLLE
SVLDLKRQLR VLGSDLVIAM GRPEEVLPGL MTERGSGGRT TVIAQSEVTS EETRVERKVK
SAVAAAGGKL ELWWGSTMFH LDDLPFREDL SDLPDVFTPF KQKCEDRSKV RACLPTPKRG
ALPLPGGIPA DLLAFEPQRV EDLNAVVPAG HPQLATTPLD ARGVLDFKGG ESAALARLNY
YLFESHRIAE YFDTRNGMLG GDYSTKFAPW LAHGCLSPRT IYHEIKRYES QTGTANKSTY
WVIFELIWRD FFRFFALKHG NKIFFEGGVT DQAQPWSHDA EAFRRWKEGR TGWPLVDANM
RELAATGFMS NRGRQNVASF LALDLGLDWR WGADWFESLL LDYDVCSNWG NWVAAAGLTG
GRVNKFNITK QSNDYDPQGD YIRSWDYDPQ GDYIRTWVPE LKGVPARRIH EPWLMSREEQ
AAAGVQIGVD YPSPIKSSWK GYGGGGGGGR PSSSGGYRQG GRGGGSGGGW QGGRGGGSGQ
GGRGRGGAGG RSGRGPKPRS AFELYG
//
