CRYD_RHOBA
ID CRYD_RHOBA Reviewed; 488 AA.
AC Q7UJB1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cryptochrome DASH;
GN Name=cry; Synonyms=phr; OrderedLocusNames=RB12007;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- FUNCTION: May have a photoreceptor function. Binds DNA; probably
CC functions as a transcriptional repressor (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC {ECO:0000250};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD77347.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294154; CAD77347.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_870272.1; NC_005027.1.
DR AlphaFoldDB; Q7UJB1; -.
DR SMR; Q7UJB1; -.
DR STRING; 243090.RB12007; -.
DR EnsemblBacteria; CAD77347; CAD77347; RB12007.
DR KEGG; rba:RB12007; -.
DR PATRIC; fig|243090.15.peg.5804; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_6_2_0; -.
DR InParanoid; Q7UJB1; -.
DR OrthoDB; 184000at2; -.
DR Proteomes; UP000001025; 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 3: Inferred from homology;
KW Chromophore; DNA-binding; FAD; Flavoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..488
FT /note="Cryptochrome DASH"
FT /id="PRO_0000235310"
FT DOMAIN 2..135
FT /note="Photolyase/cryptochrome alpha/beta"
SQ SEQUENCE 488 AA; 56693 MW; AFA221B6CF72C642 CRC64;
MANALVWFRN DLRTIDHEPF LRASTADRCF AVHCIDPRQF ETTELGFQRT GPFRARFLIE
NLTDLRSRLR SLGGELIVRV GRPETVLQHL LPSLAIDAVH FHHEPRTEEA DTAESVQQLC
DQHGIATHVA YGDTLIHPDE LPFEIADTPE LFTDFRKEIE KQCEARSPLE EPIRIHGTLP
EEVNAGDIPT LESLGLSTPP LDDRCLNQFT GGQNAAQQRM EEYIWNEDRL RVYKETRNGM
LHPNDSSKFS PWLAQGCLSP RMIADHVRRY EEERVKNKST YWMIFELLWR DYFRWISRKH
GATLFRAGGL RGVNVDWKSD RELFRRWQDG TTGYPLVDAN MRELRTTGYM SNRGRQNVAS
FLTKNLGIDW RWGARWFESQ LVDYDVASNY GNWNYAAGVG NDARGFRFFN ITKQSRDYDS
QGEYAKHWLP ELRDLDVTEI HEPWKMSPER QQEVGATLGK EYPHPIVDLF DSAKENETIY
MRAKAASH