ID V4ZM07_TOXGV Unreviewed; 548 AA.
AC V4ZM07;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=FAD binding domain of DNA photolyase domain-containing protein {ECO:0000313|EMBL:ESS33267.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:ESS33267.1};
GN ORFNames=TGVEG_206400 {ECO:0000313|EMBL:ESS33267.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS33267.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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:ESS33267.1}.
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DR EMBL; AAYL02000110; ESS33267.1; -; Genomic_DNA.
DR AlphaFoldDB; V4ZM07; -.
DR STRING; 432359.V4ZM07; -.
DR PaxDb; 5811-TGME49_006400; -.
DR EnsemblProtists; ESS33267; ESS33267; TGVEG_206400.
DR VEuPathDB; ToxoDB:TGVEG_206400; -.
DR eggNOG; KOG0133; Eukaryota.
DR OMA; PYLRHER; -.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10211:SF0; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE; 1.
DR PANTHER; PTHR10211; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lyase {ECO:0000313|EMBL:ESS33267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226}.
FT DOMAIN 1..135
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 485..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 61369 MW; AC94EBF714414F61 CRC64;
MRVQDNWALL LAQEAARSLN KPLVVIHLLV PGLAFQPTRR HLSFFMGGAR EVETELKSLN
IGFELPIVSK KDPKGRLDEA NKKIEEVFDA LQPALAVCDF NPLRLPTQVV EALTRVYAEC
LSPLYQVDTH GVVPCWVASD KLETAARTLR PKLMELVKEF ATPFPKVQRM TVPWTHTKLF
PLDEDRILSE LKPDPPEPLD SWKPGTKAAL ELLHSFATPK NLAEYGKSRN DPVAGVQSDL
SPYIHFGHIS VQRCLLEVSK LKSTAADKTL KEGVMSFIDE VVVRSQLSDN FVFFNPHYDD
IKGAPLWAQQ TLNIHAKDKR EPHYGFAALE AGKTYDELWN AAQLQLVRDG KMHGYLRMYW
AKKILEWTKS PQEALKIAIA LNDKYHLDGT DPNGVTGCMW SICGVHDQGF KERPVFGKIR
YMNYPGCERK FDVKAFVRKF PGAAENAVNV AKQGMLPFTG RAKIELKGVA EGGDSDRVAS
ILTKKIEQQK PQNTISGPAT TKETAQTKGS AKKRQRKQSD GDLAPPRNEG VDVEEADINV
EEDVHLSE
//
