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Database: UniProt
Entry: A0A0F8AXY9_9EURY
LinkDB: A0A0F8AXY9_9EURY
Original site: A0A0F8AXY9_9EURY 
ID   A0A0F8AXY9_9EURY        Unreviewed;       471 AA.
AC   A0A0F8AXY9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=FAD-binding protein {ECO:0000313|EMBL:KKF39575.1};
GN   ORFNames=FK85_27495 {ECO:0000313|EMBL:KKF39575.1};
OS   Halorubrum saccharovorum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=2248 {ECO:0000313|EMBL:KKF39575.1, ECO:0000313|Proteomes:UP000053331};
RN   [1] {ECO:0000313|EMBL:KKF39575.1, ECO:0000313|Proteomes:UP000053331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3 {ECO:0000313|EMBL:KKF39575.1,
RC   ECO:0000313|Proteomes:UP000053331};
RA   Rozanov A.S., Kotenko A.V., Bryanskaya A.V., Malup T.K., Peltek S.E.;
RT   "Full genome sequence of Halorubrum H3 strain isolated from Burlinskoye
RT   Salt Lake (Altai Krai, Russia).";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKF39575.1}.
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DR   EMBL; JNFH02000036; KKF39575.1; -; Genomic_DNA.
DR   RefSeq; WP_050025128.1; NZ_JNFH02000036.1.
DR   AlphaFoldDB; A0A0F8AXY9; -.
DR   OrthoDB; 11721at2157; -.
DR   Proteomes; UP000053331; 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:UP000053331}.
FT   DOMAIN          1..128
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         214
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         271
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         371..373
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            305
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            358
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            381
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   471 AA;  53751 MW;  F300095E7769D29C CRC64;
     MQLFWHRRDP RTRDNAGLAA AAERKGEAVV PVFVYDTDLF GATGARKRAF FLRHVKRLKA
     RYRELDSDLI VRAGDPEDVL VELADEYDVE TVFHNEYYRP ARRNRQRAVE EALANAGVAT
     EARTDAVLVD PGRLEERYAN HSRFHSDWEA VPTPEPYPEP DADALADVRD GTAVAEPNAD
     TDVDLGSDID LPEAGYRAAR KRFDDFLAHG IRSYADTRDD LARAVEAPTH AVSRMSPYLA
     VGAIGIREVW AAATDAFEAA TGDERRNADK YRYELSWREQ MYHLLYYNPD LAVANYKSFP
     NRIAWRDNDE DFEAWTRGET GYPLVDAGMR QLNAEGYVHN RPRQVVASFL AKHLLIDWRR
     GARYFAKRLI DHDHASNHGA WQWTASTGTD SVDVRIFDPV AQTAKYDANA TFVKAYVPEL
     RDVPAERIVD WPTLSRGERE DLAPDYHHPI VDRNEGYERA QRVFEEALGK R
//
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