ID A4EK19_9RHOB Unreviewed; 505 AA.
AC A4EK19;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:EBA11566.1};
GN ORFNames=RCCS2_16596 {ECO:0000313|EMBL:EBA11566.1};
OS Roseobacter sp. CCS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA11566.1, ECO:0000313|Proteomes:UP000003535};
RN [1] {ECO:0000313|EMBL:EBA11566.1, ECO:0000313|Proteomes:UP000003535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS2 {ECO:0000313|EMBL:EBA11566.1,
RC ECO:0000313|Proteomes:UP000003535};
RA Mary Ann M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) 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:EBA11566.1}.
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DR EMBL; AAYB01000003; EBA11566.1; -; Genomic_DNA.
DR RefSeq; WP_008234393.1; NZ_AAYB01000003.1.
DR AlphaFoldDB; A4EK19; -.
DR eggNOG; COG0415; Bacteria.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000003535; 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:EBA11566.1}.
FT DOMAIN 10..139
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 484..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 505 AA; 56767 MW; 3C9CA972313606E9 CRC64;
MPAENSPPRP LTVVWFKRDL RLHDHAPLSQ AAQAGTVLPL YVIEPEYWAL PDVSYRQWRF
WAGAIADLQQ QIATLGGQLC LRSGAVVDVL SQLRADYGPF DLVAHQETGN AWTFARDNAV
RDWCHRNGAD FTEHQQHGIW RGAALDRNRW AKRWDAMMAA PLTPIPSDID WARVTSDALP
DAAALGLTDD GIVAMQSPGL AAARATLDSF LHDRGAPYQK AMSSPVSGET ACSRLSPHLM
AGSISMREVY QATLARQSAV AALPKADRGT WPSAMKSFVG RLHWHCHFMQ KLEAEPEIEW
LPMARIYEGL RPTPTDSSLL SAFEEGRTGY PFVDACMRYL RATGWINFRM RAMLMSFASY
NLWLPWQQSG TVLARLFTDY EPGIHWPQSQ MQSGETGINA VRIYSPVKQG YDQDPTGVFT
RQWVPELAHL TGKALQDPWT LDALPKGYPA RIVDHQQTAR EAKQRIYGLR RTAEARSQSA
AIFEKHGSRK PRDLRTRRKV AHTDD
//
