ID A0A3L6Q8T7_PANMI Unreviewed; 714 AA.
AC A0A3L6Q8T7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cryptochrome-1-like isoform X2 {ECO:0000313|EMBL:RLM73607.1};
GN ORFNames=C2845_PM15G10220 {ECO:0000313|EMBL:RLM73607.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLM73607.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLM73607.1}.
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DR EMBL; PQIB02000013; RLM73607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6Q8T7; -.
DR STRING; 4540.A0A3L6Q8T7; -.
DR Proteomes; UP000275267; Chromosome 15.
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 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000275267}.
FT DOMAIN 16..147
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 253..257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 396..398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 330
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 383
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 406
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 714 AA; 80507 MW; 80664314DDCFE6D5 CRC64;
MSVSSSSMCG GGETGMRIVV WFRRDLRVED NPALAAAARA GGEVVPAYVW SPEEDGPYHP
GRVSRWWISQ SLQHLDASLR RLGAGKLVTR RSADAVVALL HLVRDTGATH VYFNHLYDPI
SLVRDHRLKE MLTAEGIVVQ SFNADLLYEP WEVVDDEGQP FTMFAPFWNR CLSMPYDPPA
PLLPPKKINS GNLSMCPSDD LIFEDESERG SNALLARAWT PGWQNADKAL TAFLNGPLAD
YSVNRKKADS ASTSLLSPHL HFGELSVRKV FHLVRMKQLV WSNEGNHAAE ESCTLFLRSI
GLREYSRYLS FNHPSSHERP LLAHLRFFPW VVNECYFKIW RQGRTGYPLV DAGMRELWAT
GWLHDRIRVV VSSFFVKVLQ LPWRWGMKYF WDTLLDADLE SDALGWQYIT GSLPDGRELD
RIDNPQFEGY KFDPHGEYVR RWIPELARLP TEWIHHPWDA PVSVLQAAGI ELGSNYPLPI
VELDAAKVRL QEALSEMWQL EAASRATMSN GMEEGLGDSS EVPPIEFPQE LQMEVDRQPA
QAAANVPMTA RRRQDQMVPT MTSSLNRAET EVSADLGNSE DTRAQVPFHA HFEPRVERED
AIQNAEGPAP RINGVHQHNI FQQPQLRRRE AVAPSVSEAS SSWTGREGAV VPVWSPPAAS
GHSETFAADE ADVSSRSYLD RHPQSHRLMN WSQLSQSLTT GWEVENSVQP NLIG
//
