DBAD_EMENI
ID DBAD_EMENI Reviewed; 444 AA.
AC Q5AUY2; A0A1U8QNZ8; C8V4J8;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=MFS-type transporter dbaD {ECO:0000303|PubMed:23001671};
DE AltName: Full=Derivative of benzaldehyde biosynthesis cluster protein D {ECO:0000303|PubMed:23001671};
GN Name=dbaD {ECO:0000303|PubMed:23001671}; ORFNames=ANIA_07898;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP IDENTIFICATION, INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23001671; DOI=10.1128/aem.01808-12;
RA Gerke J., Bayram O., Feussner K., Landesfeind M., Shelest E., Feussner I.,
RA Braus G.H.;
RT "Breaking the silence: protein stabilization uncovers silenced biosynthetic
RT gene clusters in the fungus Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 78:8234-8244(2012).
RN [4]
RP INDUCTION.
RX PubMed=25701285; DOI=10.1534/genetics.115.174342;
RA Oiartzabal-Arano E., Garzia A., Gorostidi A., Ugalde U., Espeso E.A.,
RA Etxebeste O.;
RT "Beyond asexual development: modifications in the gene expression profile
RT caused by the absence of the Aspergillus nidulans transcription factor
RT FlbB.";
RL Genetics 199:1127-1142(2015).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of the antibiotic 2,4- dihydroxy-3-methyl-6-(2-
CC oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:23001671).
CC Is probably involved in the transport of the metabolites to the
CC environment (Probable). {ECO:0000269|PubMed:23001671,
CC ECO:0000305|PubMed:23001671}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23001671};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Deletion of the conserved eukaryotic csnE deneddylase
CC subunit of the COP9 signalosome leading to defect in protein
CC degradation results in the activation of the silenced dba gene cluster
CC (PubMed:23001671). Expression is positively regulated by the dba
CC cluster specific transcription factor dbaA (PubMed:23001671).
CC Expression is also controlled by the transcription factor flbB
CC (PubMed:25701285). {ECO:0000269|PubMed:23001671,
CC ECO:0000269|PubMed:25701285}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduces the production of yellow
CC pigmentation. {ECO:0000269|PubMed:23001671}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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; AACD01000135; EAA59552.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF73484.1; -; Genomic_DNA.
DR RefSeq; XP_681167.1; XM_676075.1.
DR AlphaFoldDB; Q5AUY2; -.
DR SMR; Q5AUY2; -.
DR EnsemblFungi; CBF73484; CBF73484; ANIA_07898.
DR EnsemblFungi; EAA59552; EAA59552; AN7898.2.
DR GeneID; 2869138; -.
DR KEGG; ani:AN7898.2; -.
DR eggNOG; KOG2504; Eukaryota.
DR HOGENOM; CLU_001265_1_0_1; -.
DR InParanoid; Q5AUY2; -.
DR OMA; CIVFGHM; -.
DR OrthoDB; 916876at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..444
FT /note="MFS-type transporter dbaD"
FT /id="PRO_0000446358"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 444 AA; 47011 MW; F01DA7D2048EC0A9 CRC64;
MTEQPPQNHS VDLNQNEDNN ENDYRSSSAT DAERPCEPKI EESTAKPPTG PPAPPPPPNG
GLVAWLHVIG GFMLFFNTWG IMNAFGVFQT YYESGALFER SSSDISWIGS IQATMLLLVG
FFTGSIYDRG YLRALLVVGS FCIVFGHMML SLCKTYGQVL LAQGFCVGIG AGCLFVPCVS
VLPTYFSSRL GTALGLAVSG SSMGGVIYPI VLNELIGPLG FGWSVRVIGF IALGTLLVPI
AVMKQRVKPP RARALIDWSA FSDIPYMAFT LASLLAFMGL FALLFYISYF GAAKPITDTR
MAFYIVPILN AASCFGRTIP NAMADKIGPF NLIAPCCLAV GVLILCLLAV TTEAGLIVIA
LLSGFFGGAL IGLPPLCFVA LTKDKTKIGT RIGMGFGMVG LGVLAGGPAG GAILSHSHHS
NWTGLWVYGG VTSLVAGFII CIAV
