ID U2RSV6_LEIAQ Unreviewed; 320 AA.
AC U2RSV6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=FAD binding domain of DNA photolyase {ECO:0000313|EMBL:ERK71634.1};
DE Flags: Fragment;
GN ORFNames=N136_02016 {ECO:0000313|EMBL:ERK71634.1};
OS Leifsonia aquatica ATCC 14665.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1358026 {ECO:0000313|EMBL:ERK71634.1, ECO:0000313|Proteomes:UP000016605};
RN [1] {ECO:0000313|EMBL:ERK71634.1, ECO:0000313|Proteomes:UP000016605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14665 {ECO:0000313|EMBL:ERK71634.1,
RC ECO:0000313|Proteomes:UP000016605};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERK71634.1}.
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DR EMBL; AWVQ01000249; ERK71634.1; -; Genomic_DNA.
DR RefSeq; WP_021762015.1; NZ_KI272120.1.
DR AlphaFoldDB; U2RSV6; -.
DR PATRIC; fig|1358026.3.peg.1719; -.
DR HOGENOM; CLU_867448_0_0_11; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000016605; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 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; PS00691; DNA_PHOTOLYASES_1_2; 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:ERK71634.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016605}.
FT DOMAIN 139..292
FT /note="Cryptochrome/DNA photolyase FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03441"
FT BINDING 91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 103..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 240..242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 173
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 227
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 250
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ERK71634.1"
SQ SEQUENCE 320 AA; 36318 MW; 6BA463BF4A05C2DB CRC64;
PWTIRTGAGT PFSVYTPFWR ACLAAPPPRK PLPAPQELTA ADPVDGESID DLALLPTDPD
WAGGLREAWE PGERSARRRL AAFLDEDVAR YRDDRDAPGI DATSRLSPHL RWGELSPHQV
WHATAEARDR ANAEGASTFV SELGWREFAY HTLFAHPELA TVNIHREYDS FPWPRLHPAA
LRAWHQGRTG IPLVDAGMRE LWTTGTMHNR VRMVVASFLI KNLLIDWRRG EQWFWDTLVD
ADPASNPFNW QWVAGSGADA APYFRVFNPE LQRTKFDPHG DYVRRWVPEW DTAGYPEPIV
DLAETRRAAL AAFDAVKKAR
//
