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Database: UniProt
Entry: A0A0N1B091_9SPHN
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Original site: A0A0N1B091_9SPHN 
ID   A0A0N1B091_9SPHN        Unreviewed;       463 AA.
AC   A0A0N1B091;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KPF65321.1};
GN   ORFNames=IP79_03980 {ECO:0000313|EMBL:KPF65321.1};
OS   Porphyrobacter sp. AAP60.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX   NCBI_TaxID=1523423 {ECO:0000313|EMBL:KPF65321.1, ECO:0000313|Proteomes:UP000037996};
RN   [1] {ECO:0000313|EMBL:KPF65321.1, ECO:0000313|Proteomes:UP000037996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP60 {ECO:0000313|EMBL:KPF65321.1,
RC   ECO:0000313|Proteomes:UP000037996};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF65321.1}.
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DR   EMBL; LJHV01000002; KPF65321.1; -; Genomic_DNA.
DR   RefSeq; WP_054117899.1; NZ_LJHV01000002.1.
DR   AlphaFoldDB; A0A0N1B091; -.
DR   STRING; 1523423.IP79_03980; -.
DR   PATRIC; fig|1523423.3.peg.1407; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000037996; Unassembled WGS sequence.
DR   GO; GO:1901363; F:heterocyclic compound binding; IEA:UniProt.
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:SF9; (6-4)-PHOTOLYASE, ISOFORM A; 1.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 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:KPF65321.1}.
FT   DOMAIN          3..126
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          153..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         263
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            297
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   463 AA;  53401 MW;  B83241F561F6F10D CRC64;
     MSNTQIVWLR RDLRLADNPA LYHAAKSGPV VCVYVLDDES AKHHAYGGAS RWWLHHSLES
     LSNSLAQRHA KLILRRGDAV EELTKLAEEV GASTIHTNRH YEPWWRKAQK KLADRLDLQL
     HDGNFLMPPG SITTGTGGQY KIYTPFSRAM RTEFPPRDEL PAPETLSSPS QWPASDELAS
     WDLLPTKPDW AAGIAEFWQV GEVAAQDRMT WWLDHVDDYD DKRNFPSVDK VSRLSPHLHF
     GEISPIQIWH AFKHKRSDGW RTFEGELIWR DYAQNAICQF PDYATSNYRE DFDRFAWRDP
     ATDEAAAKDL QAWQQGRTGY PIVDAGMRQL WQTGWMHNRV RMITASFLIK HLLIDWREGE
     KWFWDCLCDA DYASNATNWQ WTAGTGVDSN MFSRIMAPLT QSEKFDAARY IREYVPELAK
     LEAPHIHDPD EFGRRPSGYP RKIIGHKAAR ERALSALKAM KDG
//
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