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Database: UniProt
Entry: W4F8M3_9BACL
LinkDB: W4F8M3_9BACL
Original site: W4F8M3_9BACL 
ID   W4F8M3_9BACL            Unreviewed;       472 AA.
AC   W4F8M3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN   ORFNames=C176_01085 {ECO:0000313|EMBL:ETT88609.1};
OS   Viridibacillus arenosi FSL R5-213.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX   NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT88609.1, ECO:0000313|Proteomes:UP000019062};
RN   [1] {ECO:0000313|EMBL:ETT88609.1, ECO:0000313|Proteomes:UP000019062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT88609.1,
RC   ECO:0000313|Proteomes:UP000019062};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602081-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1};
CC   -!- SIMILARITY: Belongs to the DNA photolyase family.
CC       {ECO:0000256|RuleBase:RU004182}.
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:ETT88609.1}.
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DR   EMBL; ASQA01000002; ETT88609.1; -; Genomic_DNA.
DR   RefSeq; WP_038178948.1; NZ_ASQA01000002.1.
DR   AlphaFoldDB; W4F8M3; -.
DR   PATRIC; fig|1227360.4.peg.220; -.
DR   eggNOG; COG0415; Bacteria.
DR   Proteomes; UP000019062; Unassembled WGS sequence.
DR   GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
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; 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   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 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; 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:RU004182};
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:UP000019062}.
FT   DOMAIN          2..130
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         234..238
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         268
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         368..370
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            302
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            355
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            378
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   472 AA;  55140 MW;  DB7B68851A96D6DC CRC64;
     MKKIIVWFRK DLRIHDHGAL FEAAQQGYII PVFIWPSEQE FEYTDSIAAK WSLHQSLISL
     KQDLATKGIP LIIRKGNIQK ELLQLIKETS ADAVFYNRCY EPFMVQSLFE IEIQLSKSKI
     EVQSFPGNLL YQQCTILNKS HEPYKVFTSY WKRTMQEHVP TPYAIPKMTS TLETLPESLE
     IHELQLLSPN SIEPRLDLHW KIGEQAAISH WTEFLEYGLN KYERYKDFPS TQATSLLSPY
     LVWGNISVKS IWHSIQSHEI QDPSTEMFLR QLVWRDFAYD QLIHFPTMPI KPLREAFNTF
     SWEGTSSDFN KWKLGQTGYP LVDAGMRELQ ATGYMHNRVR MVVASFLVKH LLVPWTEGSK
     WFAQKLIDFD VANNAMGWQW TTGCGIDSAP YFRIFNPVAQ GQRFDPNGDY IRQWIPELKH
     LSKKFIHKPW EASQEILALA QVELGNDYPY PIVEHDFARK RALQAYNLIK KA
//
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