DEVR_ASPFC
ID DEVR_ASPFC Reviewed; 525 AA.
AC B0XU60;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Basic helix-loop-helix transcription factor devR {ECO:0000303|PubMed:27393422};
GN Name=devR {ECO:0000303|PubMed:30914505}; ORFNames=AFUB_030440;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=27393422; DOI=10.1111/mmi.13462;
RA Valiante V., Baldin C., Hortschansky P., Jain R., Thywissen A.,
RA Strassburger M., Shelest E., Heinekamp T., Brakhage A.A.;
RT "The Aspergillus fumigatus conidial melanin production is regulated by the
RT bifunctional bHLH DevR and MADS-box RlmA transcription factors.";
RL Mol. Microbiol. 102:321-335(2016).
RN [3]
RP INDUCTION.
RX PubMed=30914505; DOI=10.1128/mbio.00215-19;
RA Manfiolli A.O., Siqueira F.S., Dos Reis T.F., Van Dijck P., Schrevens S.,
RA Hoefgen S., Foege M., Strassburger M., de Assis L.J., Heinekamp T.,
RA Rocha M.C., Janevska S., Brakhage A.A., Malavazi I., Goldman G.H.,
RA Valiante V.;
RT "Mitogen-activated protein kinase cross-talk interaction modulates the
RT production of melanins in Aspergillus fumigatus.";
RL MBio 10:0-0(2019).
CC -!- FUNCTION: Fungal-specific basic helix-loop-helix (bHLH) transcription
CC factor involved in the activation of the dihydroxynaphthalene (DHN)-
CC melanin pathway (PubMed:27393422). Specifically recognizes DNA binding
CC sites (E-boxes) identified in the promoter sequence of the gene coding
CC for the polyketide synthase pksP (PubMed:27393422).
CC {ECO:0000269|PubMed:27393422}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27393422}.
CC Note=Localization to the nucleus is increased by external KCl.
CC {ECO:0000269|PubMed:27393422}.
CC -!- INDUCTION: Expression is inceased 10 to 15 fold when the MAPK mpkB is
CC deleted. {ECO:0000269|PubMed:30914505}.
CC -!- DISRUPTION PHENOTYPE: Affects sporulation and reduces the expression of
CC the DHN-melanin gene cluster. {ECO:0000269|PubMed:27393422}.
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR EMBL; DS499595; EDP54983.1; -; Genomic_DNA.
DR EnsemblFungi; EDP54983; EDP54983; AFUB_030440.
DR HOGENOM; CLU_017046_1_0_1; -.
DR PhylomeDB; B0XU60; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0071339; C:MLL1 complex; IEA:InterPro.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR037933; MAX-like.
DR PANTHER; PTHR10328; PTHR10328; 2.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..525
FT /note="Basic helix-loop-helix transcription factor devR"
FT /id="PRO_0000454891"
FT DOMAIN 371..422
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..384
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 385..422
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 443..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 56987 MW; EBD7B9023F42DEBC CRC64;
METTLTHRPW EPTTTGPQNA PTSSAQTLPS ISTLTASMAS NIPLPAEKSP GNASLNTVER
DSGNWSMPQS TSMISCSTSA MPGTDSLPGS STYSTATNGT GNYPSLSFLT SSQPSPNRGS
VSERSPYPND HSSTNTPSSA GAHPSPNFGS QTNPTLPSLN QNFDAPSQRG SIAEPPESRR
SSVDSRMNQG ISSLAINPAS PYHSTNASQT SIVSGLQRER GISMDVNMNN SYRGPRYSGT
QPLSPLGPRA GEHRSFAAGR TAPAISSNPR SEIYAAETPT AGLAYAFPDP DVARSNSMSS
TNDKSQHPFS RKGSTAESLA SSIYSDARLP RGQHELPQNV HHHTLQHKQV RDLIGDPEPP
TSSTPYSRTP ELRVTHKLAE RKRRSEMKDC FEALRMRLPQ SQNNKSSKWE TLTRAIEYIG
QLEKMLSNAR RENDVLRSEV EEMRAQLNQQ QQQQAHQHSR PPSIFEHHPM NGPQANGQSH
GPGPAFSNYG PNSSTMMQEQ PRTLPPLVNG PVAPMQGVQY TDDRR