ID A0A162DL34_9FLAO Unreviewed; 435 AA.
AC A0A162DL34;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KZS42038.1};
GN ORFNames=AWE51_00940 {ECO:0000313|EMBL:KZS42038.1};
OS Aquimarina aggregata.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS42038.1, ECO:0000313|Proteomes:UP000076715};
RN [1] {ECO:0000313|EMBL:KZS42038.1, ECO:0000313|Proteomes:UP000076715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS42038.1,
RC ECO:0000313|Proteomes:UP000076715};
RA Wang Y.;
RT "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL Submitted (JAN-2016) 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:KZS42038.1}.
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DR EMBL; LQRT01000002; KZS42038.1; -; Genomic_DNA.
DR RefSeq; WP_066309038.1; NZ_LQRT01000002.1.
DR AlphaFoldDB; A0A162DL34; -.
DR STRING; 1642818.AWE51_00940; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000076715; 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; PS00691; DNA_PHOTOLYASES_1_2; 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:KZS42038.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076715}.
FT DOMAIN 4..134
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 215
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 260..267
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 357..359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 291
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 344
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 367
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 435 AA; 51425 MW; B1030218BBDF6A68 CRC64;
MNKKISIFWF RRDLRLNDNV GLLEALKGEY PVLPIFIFDK NILDHLPKDD ARVTFIFESL
NKIDQTLKSK YNSTILQLYA NPKQAFTHLI SQFDIQKIYS NHDYEPYAKN RDTEIEHFLK
THQITFQTFK DQVIFEKSEI VKNDGTPYVV YTPYKNKWKE IFKSDNIISH DTSNYLKNLI
QDVVTPKVSL AEMGFEQSSI KVPNYDASPE VIQNYEKTRD YPAITKGTSL LGPHLRFGTV
SIRAMVRKAI AEENEVFWSE LIWREFFMQI LYHFPHTQNS SFRAKYDRIE WRNNEEEFEK
WKKGETGYPL VDAGMRQLNK TGYMHNRVRM LVASFLCKHL LIDWRWGEAY FAEKLLDYDM
SANVGNWQWA AGSGVDAAPY FRIFNPTTQI TKFDKELKYI STWVTDFNEL TYPQPMVEHK
MARERCLKTY KNAVA
//
