SORR2_HYPJQ
ID SORR2_HYPJQ Reviewed; 664 AA.
AC G0R6T2;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Sorbicillinoid biosynthetic cluster transcription factor sor3 {ECO:0000303|PubMed:29104566};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein 3 {ECO:0000303|PubMed:28010735};
GN Name=sor3 {ECO:0000303|PubMed:28010735};
GN Synonyms=ypr2 {ECO:0000303|PubMed:29104566}; ORFNames=TRIREDRAFT_102497;
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a;
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
RN [2]
RP IDENTIFICATION.
RX PubMed=28010735; DOI=10.1186/s12862-016-0834-6;
RA Druzhinina I.S., Kubicek E.M., Kubicek C.P.;
RT "Several steps of lateral gene transfer followed by events of 'birth-and-
RT death' evolution shaped a fungal sorbicillinoid biosynthetic gene
RT cluster.";
RL BMC Evol. Biol. 16:269-269(2016).
RN [3]
RP FUNCTION.
RX PubMed=29104566; DOI=10.3389/fmicb.2017.02037;
RA Derntl C., Guzman-Chavez F., Mello-de-Sousa T.M., Busse H.J.,
RA Driessen A.J.M., Mach R.L., Mach-Aigner A.R.;
RT "In vivo study of the sorbicillinoid gene cluster in Trichoderma reesei.";
RL Front. Microbiol. 8:2037-2037(2017).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28809958; DOI=10.1371/journal.pone.0182530;
RA Monroy A.A., Stappler E., Schuster A., Sulyok M., Schmoll M.;
RT "A CRE1-regulated cluster is responsible for light dependent production of
RT dihydrotrichotetronin in Trichoderma reesei.";
RL PLoS ONE 12:E0182530-E0182530(2017).
CC -!- FUNCTION: Transcription factor that acts in concert with sor4 which is
CC a transcriptional activator of the gene cluster that mediates the
CC biosynthesis of sorbicillinoids, a diverse group of yellow secondary
CC metabolites that restrict growth of competing pathogenic fungi but not
CC of bacteria (PubMed:29104566, PubMed:28809958). Regulates the cluster
CC genes in a light dependent manner (PubMed:28809958). Also plays a
CC direct or indirect role in regulation of paracelsin biosynthesis and
CC cellulase gene expression (PubMed:28809958).
CC {ECO:0000269|PubMed:28809958, ECO:0000269|PubMed:29104566}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- INDUCTION: The promoter contains putative CRE1 binding motifs 5'-
CC SYGGRG-3' and expression is differentially regulated in light and
CC darkness by CRE1 (PubMed:28809958). Photoreceptors BLR1 and BLR2
CC negatively regulate the expression, while ENV1 exerts positive
CC regulation (PubMed:28809958). {ECO:0000269|PubMed:28809958}.
CC -!- DISRUPTION PHENOTYPE: Decreases the production of trichodimerol in
CC light and darkness (PubMed:28809958). Also impacts production of
CC paracelsin in a light dependent manner, with increased paracelsin
CC levels in light (PubMed:28809958). Results also in increased cbh1
CC transcript levels and correspondingly increased specific cellulase
CC activity (PubMed:28809958). {ECO:0000269|PubMed:28809958}.
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DR EMBL; GL985056; EGR52184.1; -; Genomic_DNA.
DR RefSeq; XP_006961158.1; XM_006961096.1.
DR AlphaFoldDB; G0R6T2; -.
DR SMR; G0R6T2; -.
DR EnsemblFungi; EGR52184; EGR52184; TRIREDRAFT_102497.
DR GeneID; 18480409; -.
DR KEGG; tre:TRIREDRAFT_102497; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_102497; -.
DR eggNOG; ENOG502RJRW; Eukaryota.
DR HOGENOM; CLU_008511_3_1_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..664
FT /note="Sorbicillinoid biosynthetic cluster transcription
FT factor sor3"
FT /id="PRO_0000443841"
FT DNA_BIND 40..67
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 68..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 74747 MW; 6EFDA1C958D871F1 CRC64;
MSARQDEDQR LQAQTQAQAQ VQAQAPLSLY RERLKIANAC QSCRASKVKC DGGRPVCARC
QKRGRACSYS QHDAASPRGR GRQRAKAPTR QPRPIRSRAS VELPVTAPTP VTAQASPLIA
QDYSLQTPSA TQTPSTTGFS GSSDLEHVHE DRDESRAFYA AHGRFAGEVS STIDKMAGLS
PDTTCSLVPF VDAPLFGDVG EPPRNVVLDF ASDLPRAYAD RLLAIYWHHV HPVEPVLDQQ
QFCRTYDAFY SGSGTPLHVD RDIWLSTLNI VFALAVQIQE SIPMQKRDDE ANRYFQRAWA
LLRPEAILWK PGSLELVQCL LLMNRYLHCT NNQQKTSMAA TLAIRIAQNM VCHTSEESPS
SDADKDLRHK VWASCVALER PALLTGHGSD FHAWELELHE IGTHIQLAQV QSKNSMATKL
GLPRLYQQDE YHAIAVQLDG CLNKWEKSLP DDWRLQNMHM IHDRRARAER YLLHFRLLHS
RIYLHRPMLA RLYAIKSHAP TAAAASDPST ISDRLLQECA RMCLEAAQKL TSLIAEIHDP
NEPIGILPWW YRVYYLHIAG IHFLAAMFAS DLFTPSVERA WYQVLAALRA HEHLSLYVQQ
CARTFETLAA RILNARCLSV NGNGIMALDD GAPGLFLDDM FQDVNFDLDE FLFSVDDTGR
RTNY
