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Database: UniProt
Entry: A0A3A6PV22_9EURY
LinkDB: A0A3A6PV22_9EURY
Original site: A0A3A6PV22_9EURY 
ID   A0A3A6PV22_9EURY        Unreviewed;       572 AA.
AC   A0A3A6PV22;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase/cryptochrome family protein {ECO:0000313|EMBL:RJX43260.1};
GN   ORFNames=DM826_06530 {ECO:0000313|EMBL:RJX43260.1};
OS   Halonotius aquaticus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halonotius.
OX   NCBI_TaxID=2216978 {ECO:0000313|EMBL:RJX43260.1, ECO:0000313|Proteomes:UP000276588};
RN   [1] {ECO:0000313|EMBL:RJX43260.1, ECO:0000313|Proteomes:UP000276588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F13-13 {ECO:0000313|EMBL:RJX43260.1,
RC   ECO:0000313|Proteomes:UP000276588};
RA   Duran-Viseras A., Sanchez-Porro C., Ventosa A.;
RT   "Halonotius sp. F13-13 a new haloarchaeeon isolated from a solar saltern
RT   from Isla Cristina, Huelva, Spain.";
RL   Submitted (JUN-2018) 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:RJX43260.1}.
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DR   EMBL; QKNY01000009; RJX43260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A6PV22; -.
DR   Proteomes; UP000276588; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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}; Lyase {ECO:0000313|EMBL:RJX43260.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276588}.
FT   DOMAIN          66..190
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         270
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         284..288
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         318
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         419..421
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   572 AA;  63859 MW;  A10D9166171BCD79 CRC64;
     MGWSNDASER MKQWYGSKAN DIPDCGSSLR VGTRLISICA QRTRVNAPSS AAQLSAVSQQ
     VDGVDDICLV WHCRNLRTDD HPAIEYATEQ HAAILPVFIV DPAFYGADGL ACDARIQFML
     ESLADLTDQY ASLGGGLTML HGEPVELLEE LDAHVAQIVT TADPTGRYGL RRDNAVAEAC
     DITFVDADGL RRDVPDTRDG WSDHVESYLT APIHEVDGEE IPIHDVDTDI DPAWVENYYD
     ISPEKQISRV GGTEHAVQVL NEFIDTLSEY PGNISAPTDA RTGTSQLSPY LRFGCLSVRQ
     VYQAVDDASG SGQATEMFTS RLYWNRHYNQ KLADWAGWMD QAVNPVLEDF HQETHDPDRV
     EAWKTGTTGY PMVDAAMRCL RQTGWLNFRM RAMCASFLCD LLQQPWKIGA DFFYYHLLDA
     DPAINYTQFQ LQAGVDGTNM LRIYNPRKQV RDNDPDGEFI KKWVPELDAL PVEYLDQPEK
     TPLHVQDEVG VRIGETYPYP IVEYEAAREA IIEKIEAVRA AATKALQHPE VNRRASLSQR
     GGATQPTADV AIEAVTDTEE EQNGQSSLDD FT
//
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