ID S6U8U1_PSESF Unreviewed; 482 AA.
AC S6U8U1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:EPN34771.1};
GN ORFNames=A244_34018 {ECO:0000313|EMBL:EPN34771.1};
OS Pseudomonas syringae pv. actinidiae ICMP 18807.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=1194404 {ECO:0000313|EMBL:EPN34771.1, ECO:0000313|Proteomes:UP000015729};
RN [1] {ECO:0000313|EMBL:EPN34771.1, ECO:0000313|Proteomes:UP000015729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 18807 {ECO:0000313|EMBL:EPN34771.1,
RC ECO:0000313|Proteomes:UP000015729};
RX PubMed=23935484; DOI=10.1371/journal.ppat.1003503;
RA McCann H.C., Rikkerink E.H., Bertels F., Fiers M., Lu A., Rees-George J.,
RA Andersen M.T., Gleave A.P., Haubold B., Wohlers M.W., Guttman D.S.,
RA Wang P.W., Straub C., Vanneste J.L., Rainey P.B., Templeton M.D.;
RT "Genomic analysis of the Kiwifruit pathogen Pseudomonas syringae pv.
RT actinidiae provides insight into the origins of an emergent plant
RT disease.";
RL PLoS Pathog. 9:E1003503-E1003503(2013).
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 class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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:EPN34771.1}.
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DR EMBL; AOKG01002350; EPN34771.1; -; Genomic_DNA.
DR RefSeq; WP_017703078.1; NZ_ANJL01000011.1.
DR AlphaFoldDB; S6U8U1; -.
DR PATRIC; fig|1194404.4.peg.6986; -.
DR Proteomes; UP000015729; 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:EPN34771.1}.
FT DOMAIN 1..132
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 236..240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 278..285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 376..378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 310
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 363
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 386
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 482 AA; 54696 MW; 0E8799C91C42BC8F CRC64;
MQLIWLRSDL RVHDNTALTA ALQRGPTLAV YLLSPTQWRN HDDADCKVDF WLRNLVELEK
ALGKLNVPLL IREADTWDQA PEVLSSLCKQ FKVEGLHLNE EYGINETRRD QAVQQSMQAD
GVHFTSHLDQ LLFKPGSILT KTGNYFQVFT QFKKVCYTRL HEAMPRTVHT PEAQQPLSIK
SDAIPDQVKG FSTPSKSLRD LWPAGEVEAS RRIEAFADEQ ISYYKDERDF PAKPGTSQLS
AYLAAGVISP RQCLHAALAS NQGEFETGDV GTVTWINELL WREFYKHTLV GYPRVSRHRA
FRPETEALKW RDAPEELLAW QEARTGLPII DAAMRQLLET GWMHNRLRMV VAMFLTKNLL
IDWREGERFF MRHLIDGDLA ANNGGWQWSS STGTDSAPYF RIFNPLSQSE RFDPEGVFIK
RWLPELADLN KKQIHDPASI GGLFGIADYP KPIVDLSKSR ARALAAFKAL PARQPAAGAD
NG
//
