ID A0A377R164_9NEIS Unreviewed; 434 AA.
AC A0A377R164;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:STR01007.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:STR01007.1};
GN Name=phrB {ECO:0000313|EMBL:STR01007.1};
GN ORFNames=NCTC13336_01234 {ECO:0000313|EMBL:STR01007.1};
OS Kingella potus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=265175 {ECO:0000313|EMBL:STR01007.1, ECO:0000313|Proteomes:UP000254293};
RN [1] {ECO:0000313|EMBL:STR01007.1, ECO:0000313|Proteomes:UP000254293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13336 {ECO:0000313|EMBL:STR01007.1,
RC ECO:0000313|Proteomes:UP000254293};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; UGJJ01000001; STR01007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377R164; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000254293; Unassembled WGS sequence.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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 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 4: Predicted;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
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:STR01007.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254293}.
FT DOMAIN 6..130
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 210
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 222..226
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 362..364
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 434 AA; 47435 MW; 114BF3D5C5897EC2 CRC64;
MSPPPNLLLI HFTRNLRLAA NPLLQAAAQY GLPAAALYFL PEYANPRQQF FLRQTLAELS
DGLSEYGIPL HVFCGNAVRQ LNALMARYPS ALLLTAQHIR LAGTDGAERV RYVQEEPLAL
PVTRYSLENA PPPDFAVYRQ AWLRRVRQDA EEGGQTPDWA AVRRAQHGLP QQWRNAPPLP
AAPAQILSQA GGETAAQAAW QAFAPKLPHY ALMKDFPAQK GTSQLSAALR FGLLPVRQLA
CAGIGGETPE PWLDSVFYGD YCRRLLPFSD GLWTWQNGAL HEICRSAAPP EMPALDSTRA
AAFERWRQGM TGVPIIDAAM RTLAGSGWLH PRLRPLAAAF AVSALKLPAA AGEHYFARTL
TDYDHAPNRT GWQQAASGRL KNPFAESQNA DPGGRFIRSR LPELAHLPDN LIHAPHLAGS
GIALNGYPAP IAFA
//
