ID A0A1H9K8M2_9FLAO Unreviewed; 493 AA.
AC A0A1H9K8M2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase family protein (Cryptochrome) {ECO:0000313|EMBL:SEQ95510.1};
GN ORFNames=SAMN05421824_2658 {ECO:0000313|EMBL:SEQ95510.1};
OS Hyunsoonleella jejuensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=419940 {ECO:0000313|EMBL:SEQ95510.1, ECO:0000313|Proteomes:UP000198999};
RN [1] {ECO:0000313|EMBL:SEQ95510.1, ECO:0000313|Proteomes:UP000198999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21035 {ECO:0000313|EMBL:SEQ95510.1,
RC ECO:0000313|Proteomes:UP000198999};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOFN01000004; SEQ95510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9K8M2; -.
DR STRING; 419940.SAMN05421824_2658; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000198999; 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:SEQ95510.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198999}.
FT DOMAIN 6..136
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 217
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 493 AA; 58284 MW; 2127DB3CFDBA42E7 CRC64;
MTTKPPITVV WLKRDLRLHD NEAIYNALKA NKPTLLLYCF EPLLMNDPHY SERHWNFIKE
SIVDLNKELE AYNSKILTVQ CDIIAAINQL QTLYSISEIY SHQETGILVT FERDKNFKRY
CKNNLITWHE NINNGVQRGL KNRDNWNELV DAFYAVEPLK FTPKNNQLLT IEAIKDLETL
FKIPNLNAQQ FTPFQKGGRT TGKRYLSTFF EERHRDYMLH ISKPELARTS CSRISPYIAW
GNLSVREVYH QAYHLKETSK HKKALEAFMS RLRWQTHFIQ KFEMEHTMEE ASLNKGFHKL
KKSISKDYQQ AWKTGQTGYP MVDACMRCLN ETGYLNFRMR ALVVSFFTHN LWQPWQEATT
HLSQMFLDFE PGIHFPQLQM QAGETGINML RIYNPVKNSL EHDPNATFIK KWVPELEKLD
TPFAHQPYLM TEMEQQFYGF NLGKDYPKPI VDLETTRKKA GDTLWTLRKD KTVLEESKRI
LRKHTRNKRL SKS
//