ID A0A2P8F6D2_9RHOB Unreviewed; 469 AA.
AC A0A2P8F6D2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase type I {ECO:0000313|EMBL:PSL17252.1};
GN ORFNames=CLV88_11922 {ECO:0000313|EMBL:PSL17252.1};
OS Shimia abyssi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1662395 {ECO:0000313|EMBL:PSL17252.1, ECO:0000313|Proteomes:UP000240418};
RN [1] {ECO:0000313|EMBL:PSL17252.1, ECO:0000313|Proteomes:UP000240418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100673 {ECO:0000313|EMBL:PSL17252.1,
RC ECO:0000313|Proteomes:UP000240418};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
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:PSL17252.1}.
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DR EMBL; PYGJ01000019; PSL17252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8F6D2; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000240418; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {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:PSL17252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000240418}.
FT DOMAIN 2..127
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 231..235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 266
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 300
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 469 AA; 52823 MW; 720EE3F3DCF6DF3F CRC64;
MKQTIVLFRR DLRLSDHPAL TAAADRGAVI PVVLLDDAVT SLGGAAKMRL GLSLACFSAD
LEKRGMRVIL RRGEAASLVH ELIRESGADA VYWSRRYDPD GVATDTALKA GLSEIGVEAR
SYAGTLLFEP WTVETGAGGP FRVYSPFWKA VRGRVLPNVL PIPKLIAPDA WPASDALDDW
HLSRDMQRGA EVVARHVSAG EAASVTRLDD FVVERIDAYK DARDFMDRDA TSGLSDALSV
GEISPLQCWA AGQRAMEEGK RGAEHFLKEV VWREFAWHLM WHFPTLDREN WRAGWDRFEW
IEDEAHPHYL AWCQGRTGVA LVDAAMRELY VTGKMHNRAR MITASYLTKH LRSHWRLGLK
WFQDCLVDWD AASNAMGWQW VAGSGPDAAP FFRIFNPDRQ ADQFDARQIY RRRWLADRYG
AQDDHTDQFH AATPKSWHET MQQPVLKPIV GLKQGRDAAL AAYGDVKSQ
//
