SCPR_EMENI
ID SCPR_EMENI Reviewed; 277 AA.
AC Q5B7I8; A0A1U8QIT7; C8V549;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=C2H2-type zinc-finger transcription factor {ECO:0000303|PubMed:20952652};
DE AltName: Full=Fellutamide B biosynthesis cluster protein F {ECO:0000305};
DE AltName: Full=Inp $cluster regulator scpR {ECO:0000305};
DE AltName: Full=Secondary metabolism cross-pathway regulator {ECO:0000303|PubMed:20952652};
GN Name=scpR {ECO:0000303|PubMed:20952652}; ORFNames=AN3492;
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 FUNCTION.
RX PubMed=20952652; DOI=10.1128/aem.00683-10;
RA Bergmann S., Funk A.N., Scherlach K., Schroeckh V., Shelest E., Horn U.,
RA Hertweck C., Brakhage A.A.;
RT "Activation of a silent fungal polyketide biosynthesis pathway through
RT regulatory cross talk with a cryptic nonribosomal peptide synthetase gene
RT cluster.";
RL Appl. Environ. Microbiol. 76:8143-8149(2010).
RN [4]
RP FUNCTION.
RX PubMed=27294372; DOI=10.1021/acschembio.6b00213;
RA Yeh H.H., Ahuja M., Chiang Y.M., Oakley C.E., Moore S., Yoon O.,
RA Hajovsky H., Bok J.W., Keller N.P., Wang C.C., Oakley B.R.;
RT "Resistance gene-guided genome mining: serial promoter exchanges in
RT Aspergillus nidulans reveal the biosynthetic pathway for fellutamide B, a
RT proteasome inhibitor.";
RL ACS Chem. Biol. 11:2275-2284(2016).
CC -!- FUNCTION: C2H2-type zinc-finger transcription factor that controls the
CC expression of the nonribosomal peptide synthases inpA and inpB, as well
CC as of the other inp cluster-associated genes (PubMed:20952652,
CC PubMed:27294372). Mediates also the expression of the asperfuranone
CC biosynthesis gene cluster by binding to the afoA promoter
CC (PubMed:20952652). Probably recognizes the 5'-CT/C/AAAAGGAT/AT/GG/CA-3'
CC motif in the promoters of teget genes (PubMed:20952652).
CC {ECO:0000269|PubMed:20952652, ECO:0000269|PubMed:27294372}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; BN001302; CBF76044.1; -; Genomic_DNA.
DR EMBL; AACD01000059; EAA59053.1; -; Genomic_DNA.
DR RefSeq; XP_661096.1; XM_656004.1.
DR AlphaFoldDB; Q5B7I8; -.
DR SMR; Q5B7I8; -.
DR EnsemblFungi; CBF76044; CBF76044; ANIA_03492.
DR EnsemblFungi; EAA59053; EAA59053; AN3492.2.
DR GeneID; 2872910; -.
DR KEGG; ani:AN3492.2; -.
DR HOGENOM; CLU_1004825_0_0_1; -.
DR InParanoid; Q5B7I8; -.
DR OMA; PDSTIRC; -.
DR OrthoDB; 1327693at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Metal-binding; Nucleus; Reference proteome; Translation regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..277
FT /note="C2H2-type zinc-finger transcription factor"
FT /id="PRO_0000444107"
FT ZN_FING 185..208
FT /note="C2H2-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 23..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 30569 MW; F095A780CE9A7C2E CRC64;
MNTMNNMHLY ADSLGIHPAD HYPTMNEIET TDNTYPRYTS PPHPSILHHP QAPEPAPPRA
QTAHPPAWAL TSQSGYQMNE PSLSLTPEHR PAAGPPNGPN LNHDSDPRRP ARRQQPCGVG
TTRPLPGCPG QGQEPSRRRT TFTDSISNPD STIRCWDHGC EGRKFSSVGN YRRHLREKNG
QAKMHPCPDC GRVFTRSTAR NFHRQSGTCG LIPSQLMLQM GMGMQLQVQM QPVSQHSLAS
GHPPAFNLAP PVLLEPLADW SEPSQMDLYA ASGVVFD
