ID D4GXR7_HALVD Unreviewed; 484 AA.
AC D4GXR7; L9UIJ1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ADE04937.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:ADE04937.1};
GN Name=phr2 {ECO:0000313|EMBL:ADE04937.1};
GN OrderedLocusNames=HVO_2911 {ECO:0000313|EMBL:ADE04937.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE04937.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE04937.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
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; CP001956; ADE04937.1; -; Genomic_DNA.
DR RefSeq; WP_004044731.1; NZ_AOHU01000104.1.
DR AlphaFoldDB; D4GXR7; -.
DR STRING; 309800.HVO_2911; -.
DR PaxDb; 309800-C498_17745; -.
DR EnsemblBacteria; ADE04937; ADE04937; HVO_2911.
DR GeneID; 8924535; -.
DR KEGG; hvo:HVO_2911; -.
DR PATRIC; fig|309800.29.peg.3445; -.
DR eggNOG; arCOG02840; Archaea.
DR HOGENOM; CLU_010348_2_0_2; -.
DR OrthoDB; 11721at2157; -.
DR Proteomes; UP000008243; Chromosome.
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 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:ADE04937.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008243}.
FT DOMAIN 1..126
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 283
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 286..293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 383..385
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 317
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 370
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 393
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 484 AA; 54489 MW; 91A7539EF483EBF6 CRC64;
MQLHWHRRDL RVADNRGLAT AAEAGPVAPL FVFDRDVLDH AGAPRVRYLL DALAELRGAY
QERGSDLLVA RGDPRTVVPA VAAAFDAERA VWGIDYSGLA RERDADVRLA LDDAGVAREP
VHDAIFHPPG SITTNAGDTY SVYTYFWKKW RDRDKPDPYP EPDADDLVDA ATLESAAEDL
TNGDAEFDIA VGGLPTISDL GFEEPSASVQ PAGTEAARER LSAFCADAIY RYADDRDYPT
RDATSRLSTD LKFGTIGIRE VYAATAAARE GVGGERDESV EEFQSQLAWR EFYAHVLRGH
PNVVTENYKE YEEDIAWRDD DEELAAWKAG ETGYPIVDAG MRQLREEAYM HNRVRMIVAS
FLTKDLLCDW RHGYAHFREH LADHDTANDN GGWQWAASTG TDAQPYFRIF NPMTQGERYD
PDGEYIKRYV PELSDVTANT IHEWHELTDL ERERLAPDYP EPIVDHAERR ERAISMFEAA
RGDD
//
