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Database: UniProt
Entry: A0A1M6ADU4_9FLAO
LinkDB: A0A1M6ADU4_9FLAO
Original site: A0A1M6ADU4_9FLAO 
ID   A0A1M6ADU4_9FLAO        Unreviewed;       439 AA.
AC   A0A1M6ADU4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Cryptochrome DASH {ECO:0000256|ARBA:ARBA00017881, ECO:0000256|RuleBase:RU367151};
GN   ORFNames=SAMN04488096_101224 {ECO:0000313|EMBL:SHI34716.1};
OS   Mesonia phycicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mesonia.
OX   NCBI_TaxID=579105 {ECO:0000313|EMBL:SHI34716.1, ECO:0000313|Proteomes:UP000184225};
RN   [1] {ECO:0000313|EMBL:SHI34716.1, ECO:0000313|Proteomes:UP000184225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21425 {ECO:0000313|EMBL:SHI34716.1,
RC   ECO:0000313|Proteomes:UP000184225};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQYY01000001; SHI34716.1; -; Genomic_DNA.
DR   RefSeq; WP_073147359.1; NZ_FQYY01000001.1.
DR   AlphaFoldDB; A0A1M6ADU4; -.
DR   STRING; 579105.SAMN04488096_101224; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000184225; 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:SHI34716.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184225}.
FT   DOMAIN          6..139
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         237
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         250..254
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         387..389
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            321
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            374
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            397
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   439 AA;  52736 MW;  0740D9C9C2666E4F CRC64;
     MHEKQTYNVI WFRNDLRVFD NYSIEKARKE NHPTLAVYCF DPRHFEKTKF GFKKIEKYRA
     QFLIETVQNL QKNLKEKLNI SLLIFHDYPE SVFPKLSEKY HFQKIFLQKE WTQEEAEVQK
     NVHYHLPEVE FIETYDQFLF HPEDIPYESF QNIPEVYTQF RKKAEYHVNI RPPANLPQPQ
     PKEYLVEHTT QIPKLKELGL DEFEKDSRTA FPFHGGEEAA DLRIQHYFWD TCQLQHYKKT
     RNGLLGPDYS SKLSAWLANG SISARKIYWE VKKFEKQVVK NNSTYWLIFE LIWRDYFKYI
     SLKHGNKIFQ LGGILNKNLD WNQDKEILQN WINGETDEPF VNANMKEIAA TGFMSNRGRQ
     NVNSFWAKEL KQDWRIGAAY LESMLVDYDV HSNWGNWMYN SGVGNDPRDR KFNIQLQAKR
     YDPEKKYLQT WLGGQKELF
//
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