ID D0E0T0_CAPBU Unreviewed; 674 AA.
AC D0E0T0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Cryptochrome 1 {ECO:0000313|EMBL:ACX49997.1};
DE Flags: Fragment;
GN Name=CRY1 {ECO:0000313|EMBL:ACX49997.1};
OS Capsella bursa-pastoris (Shepherd's purse) (Thlaspi bursa-pastoris).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=3719 {ECO:0000313|EMBL:ACX49997.1};
RN [1] {ECO:0000313|EMBL:ACX49997.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=US740 {ECO:0000313|EMBL:ACX49997.1};
RX PubMed=19581451; DOI=10.1534/genetics.109.103705;
RA Slotte T., Huang H.R., Holm K., Ceplitis A., Onge K.S., Chen J.,
RA Lagercrantz U., Lascoux M.;
RT "Splicing variation at a FLOWERING LOCUS C homeolog is associated with
RT flowering time variation in the tetraploid Capsella bursa-pastoris.";
RL Genetics 183:337-345(2009).
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 class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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DR EMBL; GQ251564; ACX49997.1; -; mRNA.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR GO; GO:0097159; F:organic cyclic compound binding; 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; IPR020978; Cryptochrome_C.
DR InterPro; IPR014134; Cryptochrome_pln.
DR InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR02766; crypt_chrom_pln; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF50; CRYPTOCHROME-1; 1.
DR Pfam; PF12546; Cryptochrome_C; 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 2: Evidence at transcript level;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}.
FT DOMAIN 15..144
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 502..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 250..254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 393..395
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 327
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 380
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 403
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT NON_TER 674
FT /evidence="ECO:0000313|EMBL:ACX49997.1"
SQ SEQUENCE 674 AA; 75677 MW; 64C83ED2B26362A3 CRC64;
MSGSVSGCGG GGSGGCSIVW FRRDLRVEDN PALAAAVRAG PVIAVFVWAP EEEGHYHPGR
VSRWWLKNSL AQLDSSLRSL GTCLITKRST DSVTSLLEVV KSTGASQIFF NHLYDPLSLV
RDHRAKXVLT AQGIAVRSFN ADLLYEPWEV TDELGRPFSM FGAFWERCLS MPYDPESPLL
PPKKIISGDV SKCVSDPLVF EDDSEKGSNA LLARAWSPGW SNADKALTTF INGPLIEYSK
NRRKADSATT SFLSPHLHFG EVSVRKVFHL VRIKQVAWAN EGNEAGEESV NLFLKSIGLR
EYSRYISFNH PYSHERPLLG HLKFFPWAVD ENYFKAWRQG RTGYPLVDAG MRELWATGWL
HDRIRVVVSS FFVKVLQLPW RWGMKYFWDT LLDADLESDA LGWQYITGTL PDSREFDRID
NPQFEGYKFD PNGEYVRRWL PELSRLPTDW IHHPWNAPES VLQAAGIELG SNYPRPIVGL
DEAKARLHEA LSQMWQLEAA SRAAIENGSE EGLGDSAEVE EAPIDFPRDI TMEETEPARL
NPIRRYEDQM VPSITSSLLR PEEDEESSLN LRNSVGDSRA EVPRNLVNTN QAQQPRAEPA
SNQVTAMIPE FNIRLVAEST EDSTAESSSS GRRERDGGIV PEWSPGYSEQ FPSEENGMGA
GSTTSSYLQN HHEI
//
