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Database: UniProt
Entry: C1FDS1_MICCC
LinkDB: C1FDS1_MICCC
Original site: C1FDS1_MICCC 
ID   C1FDS1_MICCC            Unreviewed;       579 AA.
AC   C1FDS1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000256|ARBA:ARBA00014046};
DE            EC=4.1.99.3 {ECO:0000256|ARBA:ARBA00013149};
DE   AltName: Full=DNA photolyase {ECO:0000256|ARBA:ARBA00031671};
GN   ORFNames=MICPUN_55168 {ECO:0000313|EMBL:ACO68441.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO68441.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO68441.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC         DNA).; EC=4.1.99.3; Evidence={ECO:0000256|ARBA:ARBA00033999};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00649}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-2 family.
CC       {ECO:0000256|ARBA:ARBA00006409}.
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DR   EMBL; CP001574; ACO68441.1; -; Genomic_DNA.
DR   RefSeq; XP_002507183.1; XM_002507137.1.
DR   AlphaFoldDB; C1FDS1; -.
DR   STRING; 296587.C1FDS1; -.
DR   GeneID; 8250497; -.
DR   KEGG; mis:MICPUN_55168; -.
DR   eggNOG; KOG0133; Eukaryota.
DR   InParanoid; C1FDS1; -.
DR   OMA; IHNYLRM; -.
DR   OrthoDB; 1341644at2759; -.
DR   Proteomes; UP000002009; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd00293; USP_Like; 1.
DR   Gene3D; 1.25.40.80; -; 1.
DR   Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 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; IPR008148; DNA_photolyase_2.
DR   InterPro; IPR032673; DNA_photolyase_2_CS.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   NCBIfam; TIGR00591; phr2; 1.
DR   PANTHER; PTHR10211:SF0; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE; 1.
DR   PANTHER; PTHR10211; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF08711; Med26; 1.
DR   SMART; SM00509; TFS2N; 1.
DR   SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR   SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR   PROSITE; PS01083; DNA_PHOTOLYASES_2_1; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
DR   PROSITE; PS51319; TFIIS_N; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00649}; Reference proteome {ECO:0000313|Proteomes:UP000002009}.
FT   DOMAIN          21..151
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   DOMAIN          504..579
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51319"
SQ   SEQUENCE   579 AA;  65214 MW;  5D4CCFD7E2EDBDEC CRC64;
     MNRLVNEKRV RVLKEGKVGT GPVIYWCSRD QRVRDNWALI YACETANETG APVVVVFSLV
     TRFLGAGARQ FCFMLKGLRE MEQALLAKNI KFVLLEGDPS LTVPRFAKEC GASLIVADQS
     PLRLGRTWRV AIASSVDCPL HEVDAHNVVP VWEASQKLEV GARTLRGKLA KLYPEFLVEF
     PETPVVKETW PCAAAAALPT IGIDWEALIV RARNDGAAVP EVTWAVPGEF AAHATLEHFL
     TRRLKYYEHR NDPAKPQALS GLSPYLHFGQ ISAQRCALEA RRYAKSSNKA VDVFLEELIV
     RRELADNFCW YSPKYDTIEG QKYEWAKETV REHSKDKRAY LYSLQQFENG ETHDDLWNAA
     QLEMVHGGKM HGFMRMYWAK KIMEWTESPD QALEFAIHLN DKYQLDGRDP SGYVGCMWSI
     VGVHDQGWSE RPIFGKIRYM AYSGCVKKFK VQDYIKRVDE LVTAVKAGEK DTAVVNPGRF
     HIEVSRSLDC DSLAVTGSRV CSEDELQRFV RVASANARSD TTRSLEALRA LKSVDITAET
     LIKTGVGKEL KKLSKQRENP SVSSAAAAIV QAWQKLLLP
//
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