ID U1JT29_9GAMM Unreviewed; 462 AA.
AC U1JT29;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:ERG20147.1};
GN ORFNames=PCIT_02884 {ECO:0000313|EMBL:ERG20147.1};
OS Pseudoalteromonas citrea DSM 8771.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG20147.1, ECO:0000313|Proteomes:UP000016487};
RN [1] {ECO:0000313|EMBL:ERG20147.1, ECO:0000313|Proteomes:UP000016487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487};
RX PubMed=22535931; DOI=10.1128/JB.00265-12;
RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA He H.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of type strains of seven species of the marine bacterium
RT Pseudoalteromonas.";
RL J. Bacteriol. 194:2746-2747(2012).
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:ERG20147.1}.
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DR EMBL; AHBZ02000036; ERG20147.1; -; Genomic_DNA.
DR AlphaFoldDB; U1JT29; -.
DR STRING; 1117314.PCIT_02884; -.
DR eggNOG; COG0415; Bacteria.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000016487; 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:ERG20147.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016487}.
FT DOMAIN 1..130
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 229..233
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 268
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 271..278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 369..371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 303
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 356
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 379
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 462 AA; 53372 MW; B86A2FB7876A4465 CRC64;
MKSIFWFRRD LRYFGNEALI EATKNGANMA LFFVCEKQWR VEHGVAPIQI DLIKRRIDYL
GQKLAQVGIE LRIISVDMYA DIPAKLDAFC KSYQVDYVYA NTEYEINEVA RDTACMSLGV
KLRLFDGDVI AKPGSVLTKS QEMFKVFTPF KKAWLKLFEQ TQFIVPSWPL DQQGKLTTVW
CKPDSLIGDD SSCKWPVDDE SLARIASRFV IEKCAKYHAE RDIPGIKGTS GLSPYLAIGA
ISVKQLIAEV QCHFPDILQT PSKDEFTWIN ELIWREFYRH LIVAYPNLCK YRNFNSKYDT
VVWNDNEELF SAWCRGDTGY PIVDAAMRQL NQTGWMHNRL RMIVASFLTK HLLIDWRKGE
RYFMEKLIDG DFASNSGGWQ WAASTGCDAQ PYFRIFNPVT QSKKFDPEGN FIRTYVPELA
DIPSKYIHFP HDYIASFSSS NYSPAIVEHK EARQRALDAF KV
//
