CRYD_SYNY3
ID CRYD_SYNY3 Reviewed; 489 AA.
AC P77967;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cryptochrome DASH;
GN Name=cry; Synonyms=phr, phrB; OrderedLocusNames=sll1629;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP EXPRESSION IN E.COLI, AND COFACTOR.
RX PubMed=10871367; DOI=10.1093/nar/28.12.2353;
RA Hitomi K., Okamoto K., Daiyasu H., Miyashita H., Iwai S., Toh H.,
RA Ishiura M., Todo T.;
RT "Bacterial cryptochrome and photolyase: characterization of two photolyase-
RT like genes of Synechocystis sp. PCC6803.";
RL Nucleic Acids Res. 28:2353-2362(2000).
RN [3]
RP DISCUSSION OF SEQUENCE AND COFACTOR.
RX PubMed=12878596; DOI=10.1074/jbc.m305792200;
RA Worthington E.N., Kavakli I.H., Berrocal-Tito G., Bondo B.E., Sancar A.;
RT "Purification and characterization of three members of the
RT photolyase/cryptochrome family blue-light photoreceptors from Vibrio
RT cholerae.";
RL J. Biol. Chem. 278:39143-39154(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-453, AND CHARACTERIZATION.
RX PubMed=12535521; DOI=10.1016/s1097-2765(03)00008-x;
RA Brudler R., Hitomi K., Daiyasu H., Toh H., Kucho K., Ishiura M.,
RA Kanehisa M., Roberts V.A., Todo T., Tainer J.A., Getzoff E.D.;
RT "Identification of a new cryptochrome class. Structure, function, and
RT evolution.";
RL Mol. Cell 11:59-67(2003).
CC -!- FUNCTION: May have a photoreceptor function. Binds DNA; represses
CC transcription of at least 8 genes, including slr0364 and slr1866. Does
CC not encode a DNA photolyase function. Its disruption does not affect
CC circadian rhythm.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10871367};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10871367};
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250|UniProtKB:Q84KJ5};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC {ECO:0000250|UniProtKB:Q84KJ5};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA17766.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000022; BAA17766.1; ALT_INIT; Genomic_DNA.
DR PIR; S74805; S74805.
DR PDB; 1NP7; X-ray; 1.90 A; A/B=1-489.
DR PDBsum; 1NP7; -.
DR AlphaFoldDB; P77967; -.
DR SMR; P77967; -.
DR IntAct; P77967; 3.
DR STRING; 1148.1652848; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR PaxDb; P77967; -.
DR EnsemblBacteria; BAA17766; BAA17766; BAA17766.
DR KEGG; syn:sll1629; -.
DR eggNOG; COG0415; Bacteria.
DR InParanoid; P77967; -.
DR OMA; NWNYTAG; -.
DR PhylomeDB; P77967; -.
DR EvolutionaryTrace; P77967; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0000719; P:photoreactive repair; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR014133; Cry_DASH.
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; PTHR11455; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; SSF48173; 1.
DR SUPFAM; SSF52425; SSF52425; 1.
DR TIGRFAMs; TIGR02765; crypto_DASH; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromophore; DNA-binding; FAD; Flavoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..489
FT /note="Cryptochrome DASH"
FT /id="PRO_0000235311"
FT DOMAIN 6..140
FT /note="Photolyase/cryptochrome alpha/beta"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:1NP7"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 57..76
FT /evidence="ECO:0007829|PDB:1NP7"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:1NP7"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:1NP7"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1NP7"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1NP7"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:1NP7"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1NP7"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 281..303
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:1NP7"
FT TURN 310..315
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 355..367
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 451..456
FT /evidence="ECO:0007829|PDB:1NP7"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:1NP7"
FT HELIX 472..480
FT /evidence="ECO:0007829|PDB:1NP7"
SQ SEQUENCE 489 AA; 57040 MW; 11CA917E34F0BAD0 CRC64;
MKHVPPTVLV WFRNDLRLHD HEPLHRALKS GLAITAVYCY DPRQFAQTHQ GFAKTGPWRS
NFLQQSVQNL AESLQKVGNK LLVTTGLPEQ VIPQIAKQIN AKTIYYHREV TQEELDVERN
LVKQLTILGI EAKGYWGSTL CHPEDLPFSI QDLPDLFTKF RKDIEKKKIS IRPCFFAPSQ
LLPSPNIKLE LTAPPPEFFP QINFDHRSVL AFQGGETAGL ARLQDYFWHG DRLKDYKETR
NGMVGADYSS KFSPWLALGC LSPRFIYQEV KRYEQERVSN DSTHWLIFEL LWRDFFRFVA
QKYGNKLFNR GGLLNKNFPW QEDQVRFELW RSGQTGYPLV DANMRELNLT GFMSNRGRQN
VASFLCKNLG IDWRWGAEWF ESCLIDYDVC SNWGNWNYTA GIGNDARDFR YFNIPKQSQQ
YDPQGTYLRH WLPELKNLPG DKIHQPWLLS ATEQKQWGVQ LGVDYPRPCV NFHQSVEARR
KIEQMGVIA
