ID A0A0Q8V469_9MICO Unreviewed; 463 AA.
AC A0A0Q8V469;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KRC50777.1};
GN ORFNames=ASE16_07260 {ECO:0000313|EMBL:KRC50777.1};
OS Leifsonia sp. Root227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC50777.1, ECO:0000313|Proteomes:UP000051819};
RN [1] {ECO:0000313|EMBL:KRC50777.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC50777.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC50777.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC50777.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRC50777.1}.
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DR EMBL; LMIO01000002; KRC50777.1; -; Genomic_DNA.
DR RefSeq; WP_055892938.1; NZ_LMIO01000002.1.
DR AlphaFoldDB; A0A0Q8V469; -.
DR STRING; 1736496.ASE16_07260; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000051819; 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; PS00691; DNA_PHOTOLYASES_1_2; 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:KRC50777.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051819}.
FT DOMAIN 10..139
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 244..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 381..383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 314
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 368
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 391
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 463 AA; 51399 MW; F2D94E80792C5842 CRC64;
MSTHAEQADR PAVVWFRGDL RVADNPALTA AADSGMPVLC VYVLDEESPG VRALGGASRW
WLHHSLVSLS TALDALGGFL TILRGPAERV IGDLLRETDA AAVFWNRRYG LAERTVDEAV
KSAARADGRE ASSFGANLLF EPWTIRTGSG TPFSVFTPFW RACLAAPAPR RPLDAPASIA
GAPPHPGLGV SDLGLLPTHP DWTDGLREAW QPGEDPAHEA LDRFLAEDVA AYTADRDTPG
IDATSRLSPR LRWGELSPHQ VWHATAAARD RSNAEGAATF LSELGWREFA YHTLFQRPAL
ATENIRSEFD AFPWPRLHPA ALRAWQQGST GVPLVDAGMR ELWRTGTMHN RVRMVVASFL
IKNLLIDWRL GEQWFWDTLV DADPASNPFN WQWVAGSGAD AAPYFRVFNP ELQREKFDRH
GDYIRRWVPE WQTEAYQEPI VDLAETRRAA LAAYDAVKGR KTP
//
