ID A0A267TLD9_9BACT Unreviewed; 492 AA.
AC A0A267TLD9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:PAC33596.1};
GN ORFNames=BWI92_00790 {ECO:0000313|EMBL:PAC33596.1};
OS Flectobacillus sp. BAB-3569.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Flectobacillus.
OX NCBI_TaxID=1509483 {ECO:0000313|EMBL:PAC33596.1, ECO:0000313|Proteomes:UP000215844};
RN [1] {ECO:0000313|EMBL:PAC33596.1, ECO:0000313|Proteomes:UP000215844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-3569 {ECO:0000313|EMBL:PAC33596.1,
RC ECO:0000313|Proteomes:UP000215844};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Flectobacillus sp. BAB-3569 genome sequencing.";
RL Submitted (JUN-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}.
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:PAC33596.1}.
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DR EMBL; NJFZ01000002; PAC33596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267TLD9; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000215844; 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:PAC33596.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215844}.
FT DOMAIN 3..135
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 268
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 492 AA; 58205 MW; 7EDE49069F507FC6 CRC64;
MSSISVVWFK RDLRLLDHQP LQKAIEAGRP LLLLYIFEPS LIQDVHYSPR HWQFVWESLI
DLQKRLSQIH PNAKLWVVRE EALSFFEKHL SSYPIHSLYS YQETGISKTF ERDKNLSKYL
QLQHIPWHEY QSNGVRRGLM HRGDWMKSWY AFMHEAQAMP DWSKAIFSDL DLSAFEINSF
QAICPDYTPT HPMQPGGESF AQKYMQSFWK ERCRFYSKHI SKPLEARKSC SRLSPYIAWG
NLSIKQVYQG CLQQSKKSPS LKRPLENFSS RLRWHCHFIQ KFESEERIEF ENLNRGYDDL
FFSDNHQHFE AWTKGQTGYP LVDACMRCLV STGYLNFRMR AMLVSFLTHN LAYHWKPAAL
FLAQQFLDFE PGIHYPQIQM QAGVTGINTV RIYNPTKQAQ DHDPEGIFIK QWVPELANCP
VALIHEPWKL TPMEQHLYQI EIGKTYPFPL MDIEKEHQKV KERIWGHKAK SEVKQHKKAI
LTKHAIPFQQ KS
//