ID A0A0P7GB23_9EURY Unreviewed; 513 AA.
AC A0A0P7GB23;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KPN30711.1};
GN ORFNames=SY89_01448 {ECO:0000313|EMBL:KPN30711.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN30711.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-2013) 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 -!- 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:KPN30711.1}.
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DR EMBL; LGUC01000001; KPN30711.1; -; Genomic_DNA.
DR RefSeq; WP_054583594.1; NZ_LGUC01000001.1.
DR AlphaFoldDB; A0A0P7GB23; -.
DR STRING; 699431.SY89_01448; -.
DR PATRIC; fig|699431.3.peg.1481; -.
DR OrthoDB; 11721at2157; -.
DR Proteomes; UP000050535; 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 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 4: Predicted;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
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:KPN30711.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535}.
FT DOMAIN 1..127
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 274..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 234
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 246..250
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 312..319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 409..411
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 343
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 396
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 419
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 513 AA; 57019 MW; 1FCBFB5C20B6DE18 CRC64;
MTVFWHRRDL RAADNRGLAA AVDDADDTVP VFVFDDAVLA HASDARLRFM LDSLAELRET
YRERGSDLVV ARGDPAAVLP ALAAAVDAET VHWNADYSGL AQDRDARVAD ALDAAGFDTD
THHDAVLHEP GMIRTNAGDP YSVYTYFWKK WRDREKPDPF ASPAGSDLAD TDAIAPATLD
GGAGDFDLDD ALCPSLPSIE ELGFADPAAD VQSGGTAAAR DRLAAFCDEA IFSYESDREY
PARAGSSRLS PHLKFGTIGL REVYQATEAA MAAAKARDDA ETEGDANAEA DDAEADDELD
PAQESVRTFQ SQLAWREFYA QVLYFNPEIV SQNYKAYEEP IEWRNDADEL AAWKRGETGY
PIVDAGMRQL RAEAWMHNRV RMIVASFLTK DLLIDWRAGY DHFRTHLADH DTANDNGGWQ
WAASTGTDAQ PYFRIFNPAT QGERYDPDAE YIREYVPELR GVDADAIHDW PELSDAERAD
LAPDYPDPIV DHSHRREQAL AMYKRARGED PEE
//
