ID A0A1G9E860_9SPHI Unreviewed; 430 AA.
AC A0A1G9E860;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Cryptochrome DASH {ECO:0000256|ARBA:ARBA00017881, ECO:0000256|RuleBase:RU367151};
GN ORFNames=SAMN04487898_11148 {ECO:0000313|EMBL:SDK72288.1};
OS Pedobacter sp. ok626.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1761882 {ECO:0000313|EMBL:SDK72288.1, ECO:0000313|Proteomes:UP000198594};
RN [1] {ECO:0000313|EMBL:SDK72288.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK626 {ECO:0000313|EMBL:SDK72288.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNEX01000011; SDK72288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9E860; -.
DR STRING; 1761882.SAMN04487898_11148; -.
DR Proteomes; UP000198594; Unassembled WGS sequence.
DR GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
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; 1.
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; 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; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {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:SDK72288.1}.
FT DOMAIN 4..138
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 246..250
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 430 AA; 48901 MW; 79763BBC71D3E237 CRC64;
MRNKKILVWF RNDLRLHDNE MLVEAIAKSD SILPVYFFDP RYFENTRFGT VKTGAYRAGF
LLESVLALRN TFRKMGGDIL LVHGKPEDHI KELVEQFDIA EVYHHREVGP EETLISDDVE
DLLWELKINL KHFIGHTLYN KEDLPFPIKD IPDVFAQFKK KTERDASVKA CFLSPEEITF
VENENWGELP SLTELGFAEN DNDFSATYAV GGEEAGLEHL KMLLADGADI YLKTNGKSSV
DKPGFSSHLS AWLTFGCLSP RKVYWQVKDA EREFGSNANF NQMLLGLLWR DYYRFMFKKH
GIAFFQEKNL ENDIIAATAA IDPALENWKT GHTGNPIVDK YMKDLNDTGF IPHPGRLLVA
TFLIHILGVH WTCGAAYFEE KLIDYAPASN WGNWASVAGV DKDTKSKNGF DLSKQIKILD
IAISDSPSFA
//
