ID E9ECH3_METAQ Unreviewed; 702 AA.
AC E9ECH3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Cryptochrome DASH {ECO:0000256|RuleBase:RU367151};
GN ORFNames=MAC_07571 {ECO:0000313|EMBL:EFY86350.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY86350.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY86350.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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}.
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DR EMBL; GL698549; EFY86350.1; -; Genomic_DNA.
DR RefSeq; XP_007813911.1; XM_007815720.1.
DR AlphaFoldDB; E9ECH3; -.
DR STRING; 655827.E9ECH3; -.
DR GeneID; 19251882; -.
DR KEGG; maw:MAC_07571; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_6_1_1; -.
DR InParanoid; E9ECH3; -.
DR OMA; LIFELLW; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000002499; 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 PRINTS; PR00147; DNAPHOTLYASE.
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:UP000002499}.
FT DOMAIN 5..165
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 189..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 299..303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 467..469
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 385
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 454
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 477
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 702 AA; 79613 MW; 2C68E2BBB50A9252 CRC64;
MSRSKLLVYL LRRDLRVADN PILHHLATAS DHGFTHLLPV YVFSAQQVEL SGFLKDGEQS
PYPPAKSQVG KFWRCGPHRA KFTAEAVWNL KRSLEELGSG LVIRCGSVKD VVDHLVKELK
DAVPCVSSVW MTEEPSWEEV QEQESISSLC SQQGIEFELW KDEKYFVDDR DTGLESPADL
PDVFTTYRKS QEPLREKPRK VLPRPAKSSL PAFPEEESIP AQAHPFVSPV SLEDLQKRLV
KPLEHIMDNP PKRPEDATDG HPFTGGETSG WARLRHLGKS SAMTSYKDTR NGLVGVDYSL
KLSAYLSLGC LTARQIHEEL LKLEDGTDEQ YKDAVGYGEG ENDGTKGIRF ELLWRDYMRL
CTAKFGRKLF RLSGFRQDRS YDKKWKTANE EKAASEQEPP PAQISKILER FQNGTTGMGI
IDASQRELFH TGYTSNRARQ NAASFFSKHL EIDWRYGAEW YEMMLVDYDV SSNWANWQYV
AGTGNDPRGD ARTFNPVKQA FDYDKEGTYV RMWVPELQGL EKLENIFQVC TTEAAELERC
GLSENIMVTD PVKKIDFYVD RKPRATRRPY NNKRRGQPRG GRRGGNYNNQ HQNGSGTSSD
APASESAGAS GADAETRDQT RTDRMPNQLQ DSSWRGNHKG GHPVNMQGHH GRGWQCGDHN
RGRGTFGQFR GTWRPYGQRG GFRGRYPYGP QMTYQQFPSG GQ
//