PALH_MAGO7
ID PALH_MAGO7 Reviewed; 829 AA.
AC Q52E66; A4R8L3; G4N799;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=pH-response regulator protein palH/RIM21;
GN Name=RIM21; ORFNames=MGG_06440;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC factor RIM101 in response to alkaline ambient pH. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the palH/RIM21 family. {ECO:0000305}.
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DR EMBL; CM001234; EHA50809.1; -; Genomic_DNA.
DR RefSeq; XP_003717128.1; XM_003717080.1.
DR AlphaFoldDB; Q52E66; -.
DR STRING; 318829.MGG_06440T0; -.
DR EnsemblFungi; MGG_06440T0; MGG_06440T0; MGG_06440.
DR GeneID; 2684595; -.
DR KEGG; mgr:MGG_06440; -.
DR VEuPathDB; FungiDB:MGG_06440; -.
DR eggNOG; ENOG502QWMT; Eukaryota.
DR HOGENOM; CLU_014594_1_0_1; -.
DR InParanoid; Q52E66; -.
DR OMA; VYAVRYQ; -.
DR OrthoDB; 588615at2759; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR014844; PalH.
DR PANTHER; PTHR35779; PTHR35779; 1.
DR Pfam; PF08733; PalH; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..829
FT /note="pH-response regulator protein palH/RIM21"
FT /id="PRO_0000058202"
FT TOPO_DOM 1..34
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..159
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..272
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..338
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 89887 MW; F01B116EC83CF954 CRC64;
MDPLEARQLI PAAPGSDDEG RTSRARLCQA VNLPANGALV MPNGEVITLT APAAFKPACA
PNTTPAIIAG PGGTTGAGVD DAAHVGPQFS DLSDPFYAST FPQCYALAAT TVIAYTLVIM
LVITPRSFLD GGIVVLGRRG FTSGGSGHGI IGGRPWLQKV AALTVAISLT IATADTFKVA
EQQYAFGLQN ARELQDKVLN GTELKIIRII SDTFLWLAQA QTLIRLFPRQ REKVIIKWTA
FALITFDLIF DSLNSFQFPG PGNSRPGSFT DAIPALSYLF QLALGVLYAA WVIYYSLMKK
KYAYYHPQMK NICFVAGLSL LSILVPVVFF ILDISKPEFT GWGDYVRWVG AAAASVIVWE
WVERIEALER EEKRNGILGR EVFDGDEMLE TDSDATWPQR SRATKGPHGD GDDDDDDGEG
GRRIAVGDGT GRRRARRANG SHDSLAADSG RGRNHTQLWT SIASRYRSRP NNGADVSETE
KDNTRQTSKN VRPAAARFLQ PPLWPARPPP AATPVSRTDT ASADSTVYAI RYHPLTDVHS
RTTTRPTPPP QLSTERQSAV VDVSGTPTAV EDVRSHDQPS GSQSASPSPP RDQQSPGPPN
LVRLSREETR RERRQSLATT SRTGTRVGPD SDDPSASSQQ GGESSRGSES TAAKGWRTLA
QTLPFRGGTA RSAEDSSDSQ STTSKSRSKL QVSREGKSDR WDLRNRMEDF AVTQAERIRE
RIRPTPDTDS LPVTVIPAPA RRGAALAQLL EEDESRQGSG RPRPQDDERP ILGSPTLPSS
GQRQNSMGPE PLSSNDDLSD SHIPPPAVVR AASRANTSRS TTRDRPPEP
