ID   A0A402A3Z4_9CHLR        Unreviewed;       495 AA.
AC   A0A402A3Z4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:GCE13873.1};
GN   ORFNames=KTT_37320 {ECO:0000313|EMBL:GCE13873.1};
OS   Tengunoibacter tsumagoiensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Tengunoibacter.
OX   NCBI_TaxID=2014871 {ECO:0000313|EMBL:GCE13873.1, ECO:0000313|Proteomes:UP000287352};
RN   [1] {ECO:0000313|Proteomes:UP000287352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uno3 {ECO:0000313|Proteomes:UP000287352};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:GCE13873.1}.
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DR   EMBL; BIFR01000001; GCE13873.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402A3Z4; -.
DR   Proteomes; UP000287352; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR10211:SF0; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE; 1.
DR   PANTHER; PTHR10211; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR   SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Lyase {ECO:0000313|EMBL:GCE13873.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287352}.
FT   DOMAIN          49..178
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
SQ   SEQUENCE   495 AA;  57331 MW;  C1FF1E72A0C068ED CRC64;
     MLLLSILERE YVEGVNLIVM LDIESFVRGQ DNQPRIQIWR SGLCAEQGQY VLYWMQRAQR
     GRENHALNTA IALGNQLRLP VITLFVVADY PQANLRHYTF LLEGLAAVAS QLKERKIPFV
     IRRGQPPEEV ARLAEEIGVA AIVSDTCELR VPRQWRTELK ERIQIPFLCV DSDTIVPMNN
     IPQQEYAART IRPKIQRLLP TFLQPIVDNK TEHPLAKAPC ETGEIEQPLR YLESLQIDRS
     VAPPETAHGG YSEGQKAVQR LLQERLYAYT EQRNNPELVG TSELSAFLHF GQISVQQLAW
     DVEQYQPAEA ESKHIDLSGG KAAYLEELIV RRELAINYAY YNPRYDALDG GPQWGQKTLQ
     KHINDPREWV YTRQEFEEGR THDELWNAAQ LEMVNTGRMH GYMRMYWAKK ILEWSQTPQE
     AFDTTVYLND KYELDGRDAN GYVGISWAIC GLHDRPWKER PIFGLIRYMS ADGMKRKFDT
     TAYIYKYGRH PFKKA
//