ID W7KKG5_9CREN Unreviewed; 425 AA.
AC W7KKG5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:EWG06728.1};
GN ORFNames=ASUL_07919 {ECO:0000313|EMBL:EWG06728.1};
OS Candidatus Aramenus sulfurataquae.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Aramenus.
OX NCBI_TaxID=1326980 {ECO:0000313|EMBL:EWG06728.1, ECO:0000313|Proteomes:UP000054284};
RN [1] {ECO:0000313|EMBL:EWG06728.1, ECO:0000313|Proteomes:UP000054284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1-illumnia {ECO:0000313|EMBL:EWG06728.1};
RX PubMed=24604657;
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Draft Genome Sequence of the Sulfolobales Archaeon AZ1, Obtained through
RT Metagenomic Analysis of a Mexican Hot Spring.";
RL Genome Announc. 2:e00164-14(2014).
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:EWG06728.1}.
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DR EMBL; ASRH01000008; EWG06728.1; -; Genomic_DNA.
DR AlphaFoldDB; W7KKG5; -.
DR PATRIC; fig|1326980.6.peg.1577; -.
DR Proteomes; UP000054284; 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:EWG06728.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054284}.
FT DOMAIN 1..124
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 198
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 239..246
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 336..338
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 270
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 323
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 346
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 425 AA; 50620 MW; B705981F8BF35B36 CRC64;
MFRRDLRLDD NTGLISAMRE CEQVAPIFVI DPRQVENNEY KSEKALTFMF NSLRELDQEI
RDKGGKLFVF KGIAEEVIAK LLDKVEAVYL NEDYTPFSKM RDLAIAEACK RKGKAFRSFE
DYLLTPKAEF KGFSNFTSFY NHVKGLKVRE PVKNDYKNFF TGKLMEEAEL PEPQPAGRFK
GGRKEGLYLV ERAKHIDYSR RDYPAEGNVS YLSPHLKFGT VSPREVYYAL RENLAFTRQL
FWRDFYTLLA YYNERVFQEP FKAKFKDVKW ENDRVLFELW KRGKTGYPIV DAGMRELNNT
GYMHNRVRMI SAFLLTKVFL VDWRWGEKYF AQKLVDYDPS VNNGNWQWVA STGVDYTFRV
FDPWKQQKKF DPEAKYIKTW VEELRDYPSH VIHEAYSREI PGYPRPVVDW RERVEKAREL
YFRET
//
