ID A0A367J8W7_RHIST Unreviewed; 519 AA.
AC A0A367J8W7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=Cryptochrome DASH {ECO:0000256|RuleBase:RU367151};
DE Flags: Fragment;
GN ORFNames=CU098_002195 {ECO:0000313|EMBL:RCH86356.1};
OS Rhizopus stolonifer (Rhizopus nigricans).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4846 {ECO:0000313|EMBL:RCH86356.1, ECO:0000313|Proteomes:UP000253551};
RN [1] {ECO:0000313|EMBL:RCH86356.1, ECO:0000313|Proteomes:UP000253551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCH86356.1,
RC ECO:0000313|Proteomes:UP000253551};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(2018).
CC -!- FUNCTION: May have a photoreceptor function.
CC {ECO:0000256|RuleBase:RU367151}.
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|RuleBase:RU367151};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC {ECO:0000256|RuleBase:RU367151};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1,
CC ECO:0000256|RuleBase:RU367151};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1,
CC ECO:0000256|RuleBase:RU367151};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862, ECO:0000256|RuleBase:RU367151}.
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:RCH86356.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PJQM01003953; RCH86356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367J8W7; -.
DR STRING; 4846.A0A367J8W7; -.
DR EnsemblFungi; RCH86356; RCH86356; CU098_002195.
DR Proteomes; UP000253551; Unassembled WGS sequence.
DR GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; 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; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR02765; crypto_DASH; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF22; CRYPTOCHROME DASH; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|RuleBase:RU367151};
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:UP000253551}.
FT DOMAIN 4..156
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 260
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 273..277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 324..331
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 446..448
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 380
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 433
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 456
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT NON_TER 519
FT /evidence="ECO:0000313|EMBL:RCH86356.1"
SQ SEQUENCE 519 AA; 61580 MW; AE84231B474B7BE4 CRC64;
MSSSINICFF RNILRVHDNQ SLHAALKGNA HLLPVVCIDP RMIDITLLNN KVHQKFKVPK
TYYFKFDRVS DFRAHFLYET ILALKEELKK RHTDLMILYG KPEEMFPRLK EHLAENNLKL
DKIHTNKEYA YEELLVEKDL SKAMDDDVVY HHDALMVNPE DLDFAGEHTY KVYTHFRKRI
EKMTDPVRPP LEIPDKLPSF PSIAWEFDHA KQGEAFLKEL YEHVPIKKDE RTAFPWKGGE
QSALERLHQY LFKSDGVANY KHTRNGLIGT EYSTKFSAFL ANGCLSPRVI WHEMDRFDKE
ENRKRKRSIK SQSDDDGVYW VKFELLWRDF FRMLTVGYGT RIFMLHGFRN LENPNIAKED
AKKKVDEKPR PKNSYVDKVW RSDDEQFKKW KEGDTGIPFV DASMRELKYT GFMNNRGRQN
VASFLAKDLE IDWRIGAEYF EYMLRDHDVY SNYGNWQYVA GVGCDPREGF RHFNILKQGL
DYDKDGDYIK LWCPELAKLP IKYLHCPWLM SEEEQTKYN
//
