TRAF_PENCR
ID TRAF_PENCR Reviewed; 482 AA.
AC A0A481WQD3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=MFS-type transporter traF {ECO:0000303|PubMed:30811183};
DE AltName: Full=Terrestric acid biosynthesis cluster protein F {ECO:0000303|PubMed:30811183};
GN Name=traF {ECO:0000303|PubMed:30811183};
OS Penicillium crustosum (Blue mold fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PRB-2;
RX PubMed=30811183; DOI=10.1021/jacs.9b00110;
RA Fan J., Liao G., Kindinger F., Ludwig-Radtke L., Yin W.B., Li S.M.;
RT "Peniphenone and penilactone formation in Penicillium crustosum via 1,4-
RT Michael additions of ortho-quinone methide from hydroxyclavatol to gamma-
RT butyrolactones from Crustosic Acid.";
RL J. Am. Chem. Soc. 141:4225-4229(2019).
CC -!- FUNCTION: MFS-type transporter; part of the tra gene cluster that
CC produces terrestric acid (PubMed:30811183). The clavatol biosynthesis
CC cluster cla and the terrestric acid cluster tra are both involved in
CC the production of peniphenones and penilactones (PubMed:30811183).
CC {ECO:0000269|PubMed:30811183}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not result in significant changes in
CC sencondary metabolites production. {ECO:0000269|PubMed:30811183}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC {ECO:0000255}.
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DR EMBL; MK360919; QBK15054.1; -; Genomic_DNA.
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 3: Inferred from homology;
KW Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..482
FT /note="MFS-type transporter traF"
FT /id="PRO_0000455058"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 482 AA; 52532 MW; A9FD9760B4797C5E CRC64;
MTSGTEQATL NTEENGSDSD HLSKEPIAMP ALDWDGPTDS NNPRNFSTPK KVFITACLAS
LVCISTFGSS VMSPASGQLI HEFGISKELS ILATALYVLG FAVGPLLFGP ASEVLGRKYP
LSVGVFLFAI FSIPIAVAKN VATIFVCRFL CGTFAAAPLA IAGGGLADLW EPLSRGIAVA
GFASATFLGP VLGPLVGGFV TKSHLGWRWT QWLSIIFSLV FLAIYFVFCP ETYSPIVLAR
LAKKRGQMPP GGKVDFKQLA KVYMLRPFIM LVQEPILALL TLYMGFIYGF LYLCFEAFPI
AFEEHRGWDI GIGSLPFLSI TVGVLIGVVI IIVHTMTRMR RKLETVGDAP EERLVPMMIG
SILMPAGIFW FAWTSNTSLP WAPQVVSGVF IGCGILLIFL QGMNYIIDVY KVMANSAISI
NAMFRGLLGA GFPLFASYMF DNLGVPWAMS LLGFLCVALV PVPFLFFIYG ERIRKWSKFT
AH