ID A3J0E7_9FLAO Unreviewed; 440 AA.
AC A3J0E7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Cryptochrome DASH {ECO:0000256|ARBA:ARBA00017881, ECO:0000256|RuleBase:RU367151};
GN ORFNames=FBBAL38_03455 {ECO:0000313|EMBL:EAZ96444.1};
OS Flavobacteria bacterium BAL38.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391598 {ECO:0000313|EMBL:EAZ96444.1, ECO:0000313|Proteomes:UP000003784};
RN [1] {ECO:0000313|EMBL:EAZ96444.1, ECO:0000313|Proteomes:UP000003784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL38 {ECO:0000313|EMBL:EAZ96444.1,
RC ECO:0000313|Proteomes:UP000003784};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) 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}.
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:EAZ96444.1}.
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DR EMBL; AAXX01000001; EAZ96444.1; -; Genomic_DNA.
DR AlphaFoldDB; A3J0E7; -.
DR eggNOG; COG0415; Bacteria.
DR Proteomes; UP000003784; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000003784}.
FT DOMAIN 7..139
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 253..257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 390..392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 324
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 377
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 400
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 440 AA; 52570 MW; B66A39D035B79E3D CRC64;
MFKNKIMNGL VWFRNDLRTI DNHSLYNACR ENDTVIGIYC LDPRHFEITP FGFKKTEKFR
SQFLLETVTE LQKNLLEKNI RLLVYYGYPE ILIPEIIAKY QIHSIYSQHE WTSEENEIEQ
EIRNLISAVN WKNHYDQFLF HPADLPFEDW KKIPEVFTDF RKQIEKKIRV RPTVAISPKP
LTNLIEETTP IPTLKDLGFD SEASDFKQPE KTAFPFKGGE NHAKKRIKDY FWDTKKLAVY
KKTRNGLIGK NYSSKLSAWL ANGSVSARTI YWEVQKFEKK VIKNEDTYWL IFELIWRDYF
KYISLKHGNK IFQLNGILQK EYHWNQNKKA FNQWANGTTP EHFVNANMIE LQKTGWMSNR
GRQNVASYWA KEWEQDWRIG AAYFESMLID YDVHSNYGNW MYNAGVGNDP RDRKFNIKRQ
AEMYDADGKF QKMWLIPELF
//
