ID A0A432WKJ2_9GAMM Unreviewed; 479 AA.
AC A0A432WKJ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:RUO34268.1};
GN ORFNames=CWE11_05945 {ECO:0000313|EMBL:RUO34268.1};
OS Aliidiomarina sanyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=1249555 {ECO:0000313|EMBL:RUO34268.1, ECO:0000313|Proteomes:UP000288405};
RN [1] {ECO:0000313|EMBL:RUO34268.1, ECO:0000313|Proteomes:UP000288405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GYP-17 {ECO:0000313|EMBL:RUO34268.1,
RC ECO:0000313|Proteomes:UP000288405};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:RUO34268.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PIPM01000004; RUO34268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432WKJ2; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000288405; 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:RUO34268.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288405}.
FT DOMAIN 1..128
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 206
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 256
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 479 AA; 55770 MW; 6E1C698D2DAC6DA8 CRC64;
MINIVWLKRD LRLTDHAPLA AAQAANKPFI ILFVVEDFLR NDPHYSDRHW RFMWQSLTEI
NHQLAGRLTL TQGRLSDTLN NLHRTYRIGT IFSHEEIGIE STYARDRALK KWCIKRGVQW
QEFPCGAVIR GLSDRSGWDQ HWRSVMNQPC PSVELTALSQ LFRADHLPPV SPPREWRQPV
PEQQIGGAQH GWRELKEFMA GRGARYHQDI SKPAASRSSC SRISPYLAWG NLSIREVWQY
ALQHHTQLPT RAWRAFSSRL HWRCHFLQKF ESGMDMEHEH FNPGYRAFPF RADVNVPKDL
KAWEQGQTGI PLVDASMRCL NTTGYINFRM RAMLVSMLSH HLNIDWRLGA PHLARVFLDF
EPGIHYPQLN MQAGVTGIHT IRIYNPVYQG QKQDPNGDFI RHWVPELASL PNGLLHQPWE
MTPMEQTMHG VVLGRDYPEP LVNIAETHRA ARDRLWGFQQ KSEVQLHNPH LLARHTRRA
//