PYIT_MAGGR
ID PYIT_MAGGR Reviewed; 602 AA.
AC A0A4P8W7F5;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=MFS-type efflux transporter pyiT {ECO:0000303|PubMed:31099577};
DE AltName: Full=Pyrichalasin H biosynthesis cluster protein T {ECO:0000303|PubMed:31099577};
GN Name=pyiT {ECO:0000303|PubMed:31099577};
OS Magnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=148305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=NI980;
RX PubMed=31099577; DOI=10.1021/acs.orglett.9b01344;
RA Wang C., Hantke V., Cox R.J., Skellam E.;
RT "Targeted gene inactivations expose silent cytochalasans in Magnaporthe
RT grisea NI980.";
RL Org. Lett. 21:4163-4167(2019).
RN [2]
RP FUNCTION.
RX PubMed=31644300; DOI=10.1021/acs.orglett.9b03372;
RA Wang C., Becker K., Pfuetze S., Kuhnert E., Stadler M., Cox R.J.,
RA Skellam E.;
RT "Investigating the function of cryptic cytochalasan cytochrome P450
RT monooxygenases using combinatorial biosynthesis.";
RL Org. Lett. 21:8756-8760(2019).
CC -!- FUNCTION: MFS-type efflux transporter; part of the gene cluster that
CC mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-
CC derived cytochalasan that inhibits the growth of rice seedlings, but
CC also inhibits lymphocyte capping and actin polymerization and alters
CC cell morphology (PubMed:31099577) (Probable). Pyrichalasin H is
CC indicated as the responsible agent for the genus-specific pathogenicity
CC of M.grisea toward crabgrass (PubMed:31099577). PyiT might be involved
CC in the excretion of pyrichalasin H (Probable).
CC {ECO:0000269|PubMed:31099577, ECO:0000305|PubMed:31099577,
CC ECO:0000305|PubMed:31644300}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; MK801691; QCS37513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P8W7F5; -.
DR SMR; A0A4P8W7F5; -.
DR Proteomes; UP000515153; Genome assembly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..602
FT /note="MFS-type efflux transporter pyiT"
FT /id="PRO_0000449448"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 602 AA; 65822 MW; 82B36DF32FBE6035 CRC64;
MEKAKDSLPT TGDPVPSQGT INPVDETGGS ASDEKKAKKG CDFWFTFSSL VLTAFLSALE
GSVVSTALPT IARALEASEN YVWVVNVYYL SKYETWLTYL LRFSSAAFQP IYGQLADLWG
RRWLTIGAVV IFTVGSGICG GATSIDMLIG GRAIQGLGSA GINMLVELIL CDLLPLRERG
QFFGIIFMFV ILGSVIGPFL GGILVDRVSW RWVFYINIPF SGVCVVLLFF FLHIKNAGTG
NFIDKVKRID FFGNFLLAAS VGSCLFALTY GDTRYPFSDT RIIVSLVLGL LGHVAFMFFE
ASPWCKEPVM PMVLFKNRTS AGAYIATFLQ TLVSFWVLYF LPLYFQSTQL VSATRSGVML
LPFSVVYALS SLAGGALTTK LGRFRNIHFA SFALMTIGMG TLTILNRSTS LAVIVVLEMI
VALAIGVPTA NLLTAIQAAL PDELNALSTG TFAFLRSVGT IWGVSIPAAI FNNRFDQLLP
ELSDPTAVRA LQRGGAYQQA TSEFVDSFPS DVRDVIISIY ERSLERVWQI GIVFAGVGFL
VIFLERDLKL GTQKKTEDIE INDIPQTAAD NSASRPNTIN DTASQAPILK QRRSTNQERE
TV
