ID A0A0K3CTF0_RHOTO Unreviewed; 636 AA.
AC A0A0K3CTF0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=BY PROTMAP: gi|647402450|emb|CDR48705.1| RHTO0S19e02850g1_1 [Rhodosporidium toruloides] {ECO:0000313|EMBL:CTR10506.1};
GN Name=FGENESH: predicted gene_13.197 {ECO:0000313|EMBL:CTR10506.1};
GN ORFNames=BN2166_0063670 {ECO:0000313|EMBL:CTR10506.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR10506.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR10506.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR10506.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CWKI01000013; CTR10506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3CTF0; -.
DR STRING; 5286.A0A0K3CTF0; -.
DR OMA; TPYKNAW; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; 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; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000199069}.
FT DOMAIN 110..248
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 213..240
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 400..404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 441
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 444..451
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 545..547
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 477
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 532
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 555
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 636 AA; 71986 MW; 595D9A20DDC8C2C9 CRC64;
MAAPKRVRSA SSSASPVAEN GGSAKKRARR SPTKEDEDVK PNIKEEAEDD DGSDPRFRSV
STTAALERDR EHTSFPHEME QTPLARLYDA MRELSEVKAA KDEKPSKDGV VVYWMRNKDL
RLEDNTALSY ASAVAQEHSL PLIALHIFSL GDYKSHDRSP RRIDFQLRQL AYLRAELDKL
HIPLFTFTQS SERKAIPRIL CEKLAEWNAF GLYANIEYEV DELRRDIEVL ERTRDAREQG
EGWKGQVEFF KDFCIVAPGE LLTKQGKPYS VYSPWQRAWA AHINSNLSSF ISPQNGPVIA
NPSSARTHPI LEPMFSHEVP TSLPGFELAE QEKKDMERLW PVGEGVTEGI MGRFLKTKMR
EAKFFEPPLE GDGNEVENPK KDSKIAKYTE GRNRVDWDGT SHISAYLAAG LISPRECVRA
VYKVVGGKEV PAGRDTGFGM WIQEVAWRDF YQHVLAAWPR VCMSKPFNLK YDGTIEWATD
DDESKFEAWK EGKTGFPIVD AAMRSLKAQG YMHNRCRMIV ASFLCKDLLL DWRKGEKYFM
QMLVDGDLGS NNGGWQWSVI RIFNPASQSE KVDPNGTYIR HWVPELKSVK GKAIHNPSAA
LSKAEILKLG YVPPIVDHAE ARKKAIEAYK EAAAQG
//
