PHMH_PHANO
ID PHMH_PHANO Reviewed; 568 AA.
AC Q0V6Q0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=MFS-type efflux transporter phmH {ECO:0000303|PubMed:31815421};
DE AltName: Full=Phomacin biosynthesis cluster protein H {ECO:0000303|PubMed:31815421};
GN Name=phmH {ECO:0000303|PubMed:31815421}; ORFNames=SNOG_00314;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=31815421; DOI=10.1021/acschembio.9b00791;
RA Li H., Wei H., Hu J., Lacey E., Sobolev A.N., Stubbs K.A., Solomon P.S.,
RA Chooi Y.H.;
RT "Genomics-driven discovery of phytotoxic cytochalasans involved in the
RT virulence of the wheat pathogen Parastagonospora nodorum.";
RL ACS Chem. Biol. 15:226-233(2020).
CC -!- FUNCTION: MFS-type efflux transporter; part of the gene cluster that
CC mediates the biosynthesis of thethe mycotoxins phomacins, leucine-
CC derived cytochalasans with potent actin polymerization-inhibitory
CC activities and monocot-specific antigerminative activities
CC (PubMed:31815421). PhmH might be involved in the excretion of phomacins
CC (Probable). {ECO:0000269|PubMed:31815421, ECO:0000305|PubMed:31815421}.
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; CH445325; EAT91809.2; -; Genomic_DNA.
DR RefSeq; XP_001791004.1; XM_001790952.1.
DR AlphaFoldDB; Q0V6Q0; -.
DR STRING; 13684.SNOT_00314; -.
DR EnsemblFungi; SNOT_00314; SNOT_00314; SNOG_00314.
DR GeneID; 5967798; -.
DR KEGG; pno:SNOG_00314; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_0_1; -.
DR InParanoid; Q0V6Q0; -.
DR OrthoDB; 672661at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; Virulence.
FT CHAIN 1..568
FT /note="MFS-type efflux transporter phmH"
FT /id="PRO_0000449447"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 568 AA; 62250 MW; 3C0F5A8FF9239C7C CRC64;
MVSGTDTTEV GATTKAPPSE GTEGILDDHS SNSQPQAEKP AKTHYPLSFW LAFLGLCCTG
LVSALDGSIV ATALPSIIES LDGGDDYPLY GQLADLWGRR YVMIGATIIF ILGSGLCGGS
SSMNMLIWSR AVQGIGAGGI NMLIDMIICD LVPMRERGNF IGLLFLFVSL GATIGPFVGG
ILTDRASWRW LWLLILLQIF YINLPFGGVA LLLLILFLHV KWKNDLSTME RLRRVDVIGN
SILIGATFAI LYALTYGGTR YTWSDPHIAA PLTIGLVGLV AAFFWEMSPW CKYPVMPPLH
FQNRTSAAAF FISFMCMLLA FWINFFYPVY FQAVLIASPT RAGVYTLPRA IAFPLFAAVG
GAIVSKTGRY RTVHLVSTGI MPLVMGLSSI LDQGSSKAEW VIWQLLFGVS GGMMISTTLQ
AVQAALPESE VATSVGTWSF VRSLGTIWGL SIPAAIFNNR FDQLSTQFDP SIRALFTRGQ
AYEHGTAKFI QSFDPETRQI VIQAYIEALK RVWQIGIVFG GVTFLSVFFE KEIHLRTELK
TDFGLDEKKK GEVAKEENDV ENNGTTVQ
