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Database: UniProt
Entry: A0A346PQZ3_9EURY
LinkDB: A0A346PQZ3_9EURY
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ID   A0A346PQZ3_9EURY        Unreviewed;       467 AA.
AC   A0A346PQZ3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:AXR81938.1};
DE            EC=4.1.99.3 {ECO:0000313|EMBL:AXR81938.1};
GN   ORFNames=AArcMg_1931 {ECO:0000313|EMBL:AXR81938.1};
OS   Natrarchaeobaculum sulfurireducens.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrarchaeobaculum.
OX   NCBI_TaxID=2044521 {ECO:0000313|EMBL:AXR81938.1, ECO:0000313|Proteomes:UP000258613};
RN   [1] {ECO:0000313|Proteomes:UP000258613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AArc-Mg {ECO:0000313|Proteomes:UP000258613};
RA   Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA   Golyshin P.N., Rojo D., Ciordia S., Mena M.D.C., Ferrer M., Messina E.,
RA   Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT   "Phenotypic and genomic properties of facultatively anaerobic sulfur-
RT   reducing natronoarchaea from hypersaline soda lakes.";
RL   Submitted (FEB-2018) 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; CP027033; AXR81938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A346PQZ3; -.
DR   KEGG; nag:AArcMg_1931; -.
DR   OrthoDB; 11721at2157; -.
DR   Proteomes; UP000258613; Chromosome.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901363; F:heterocyclic compound binding; IEA:UniProt.
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:SF9; (6-4)-PHOTOLYASE, ISOFORM A; 1.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 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:AXR81938.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000258613}.
FT   DOMAIN          1..127
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         214
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         226..230
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         266
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         269..276
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            300
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            353
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            376
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   467 AA;  53033 MW;  7267F05B9457B06D CRC64;
     MVLFWHRRDL RVRDNCGLEQ AASFDEPLVS LFVLDPTVLE HASPVRVACL LDGLSALREQ
     YRERDSDLLV RRGEASEVVP QVASEVEAST VVWNEDYSGL ASERDRAVTA ALEDDGVRLE
     SVHDAICHEP GSITPNQGEH YSVFSYFWKK WRDREKQSPV DAPTAADLGE VRGDPLPSLE
     ELGFEEPEVS FPSVTPTAAR ERVASFCSGP IYRYAETRDV PSAGMTSRLS PHLKWGTVGV
     RELYAATERA ADRAEDGDAR ASVREFQRQL AWREFYAHVL AFNPETVSEN FSGYQNGIEW
     HNDPEELEAW QAGRTGYPIV DAGMRQLLEE AWMHNRVRML VASFLTKDLL IDWREGYDWF
     RRHLADHETA NDVGGWQWAA STGTDAQPYF RVFNPMKQGR EYDPDAEYIR QYVPELADAS
     SDEIHGWHEL EPSEREAVAP DYPAPLVDHG ERRTMAIETF ERARGDG
//
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