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Database: UniProt
Entry: A0A2K8SGD9_9NOSO
LinkDB: A0A2K8SGD9_9NOSO
Original site: A0A2K8SGD9_9NOSO 
ID   A0A2K8SGD9_9NOSO        Unreviewed;       488 AA.
AC   A0A2K8SGD9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=PhrB, deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:AUB34522.1};
GN   ORFNames=COO91_00345 {ECO:0000313|EMBL:AUB34522.1};
OS   Nostoc flagelliforme CCNUN1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB34522.1, ECO:0000313|Proteomes:UP000232003};
RN   [1] {ECO:0000313|EMBL:AUB34522.1, ECO:0000313|Proteomes:UP000232003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB34522.1,
RC   ECO:0000313|Proteomes:UP000232003};
RA   Shang J.;
RT   "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT   its photosynthetic adaptation to extreme terrestrial habitat.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP024785; AUB34522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8SGD9; -.
DR   KEGG; nfl:COO91_00345; -.
DR   Proteomes; UP000232003; Chromosome.
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; IPR019947; Photolyase_8HDF.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR03556; photolyase_8HDF; 1.
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:AUB34522.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232003}.
FT   DOMAIN          10..139
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         236
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         248..252
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         288
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         291..298
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         388..390
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   488 AA;  55848 MW;  7D9BE7F027DE1A8A CRC64;
     MNYIQQGMSD LILFWHRRDL RISDNTGLAA AKQQSPKVVG VFCLDPNLLE RDDVAPVKVT
     YMIGCLQKLQ ERYAQVGSQL LILHANPVQA IPALAEAINA KAVFWNWDVE PYSQERDRTV
     INALKEKGIQ FLNQNWDQIL NSPEQLRTGS NQPYTVYTPF WKNWITKPKA NPVETLQNVE
     GLTEAEQEIA KLAGALTLPS AKDLGFIWDG ELIISPGEVA AQERLEEFTA KAITEYQEQR
     NFPAVDGTSQ LSAALKFGVI GIRTVWQATI EALENSRSEE TAVNIRTWQQ ELAWREFYQH
     AMYNFPELAD GAFRDTFKNF PWQTNDEHFQ AWCEGRTGYP IVDAAMRQMN ESGWMHNRCR
     MIVASFLTKD LLINPQLGEK YFMQHLIDGD LSANNGGWQW SASSGMDPKP VRIFNPASQT
     QKFDPEGEYI RQWVSELRSV DTEYLVTGKI PSLERHAVGY PEPIVDHRIQ QQQFKLRYQQ
     QKTVSNAE
//
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