SORT_HYPJQ
ID SORT_HYPJQ Reviewed; 534 AA.
AC G0R6T1;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Major facilitator-type transporter sor6 {ECO:0000303|PubMed:28010735};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein 6 {ECO:0000303|PubMed:28010735};
GN Name=sor6 {ECO:0000303|PubMed:28010735}; ORFNames=TRIREDRAFT_43701;
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: Major facilitator-type transporter; part of the gene cluster
CC that mediates the biosynthesis of sorbicillinoids, a diverse group of
CC yellow secondary metabolites that restrict growth of competing
CC pathogenic fungi but not of bacteria (PubMed:29104566).
CC {ECO:0000305|PubMed:29104566}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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: Abolishes production of trichodimerol and
CC dihydrotrichotetronin in darkness (PubMed:28809958). Also impacts
CC production of paracelsin in a light dependent manner, with decreased
CC paracelsin levels in light, but likely in an indirect way
CC (PubMed:28809958). {ECO:0000269|PubMed:28809958}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; GL985056; EGR52691.1; -; Genomic_DNA.
DR RefSeq; XP_006961063.1; XM_006961001.1.
DR AlphaFoldDB; G0R6T1; -.
DR EnsemblFungi; EGR52691; EGR52691; TRIREDRAFT_43701.
DR GeneID; 18484938; -.
DR KEGG; tre:TRIREDRAFT_43701; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_43701; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_11_6_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
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 Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..534
FT /note="Major facilitator-type transporter sor6"
FT /id="PRO_0000443848"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 534 AA; 58152 MW; 58A77F8AA5E0DC46 CRC64;
MSKEASQDSR SITPVEAVEP LEVVDAEKNV TTSPYNGSGT VEDPFIVEFQ QDDKSNPMNW
GQFRKWFLTS IVTFSVFAVT FTSSAYSVSA EEIMTEFDIS STLFITGVSV FVLGFAIGPA
VWGPLVTPHD ERSNANRASL QSTRSELYGR QMPWIASHTA MVAFMAGSAG SPNIATLIVL
RFLAGTFGGS PLVNSGGAIA DLFPPAQRGL AMTIYCVAPF LGPILGPIVG GFATEYIGWR
WVQGMCTIFI GVIGIIGVIF VPETYGPVLL QRKANALSKA DGKVYISVLQ KNQGKKQPSE
VFGRALIRPW VLLFREPIVL IASLYMAIIY GTVYMFLGAM PIVYNELRGW SPGFGGLAFL
GMMVGIIIGL GYAIWDNNGR YMKLDPSKRT AESRLPPAIA GAVALPIGMF AFAWTNYPSI
HWAVSIVLSA PFGFGVVLVI LPIVNYLIDS YTVYAASVLA AAAVFRSIMG AVFPLFTSQM
YHNLGIHWAT SIPAFLTLVC MPFPFFMYRY GAVVREKCKY AAEAAQIMKK MQGR
