CSEP4_BLUG1
ID CSEP4_BLUG1 Reviewed; 118 AA.
AC N1JJ94;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Secreted effector CSEP0064 {ECO:0000303|PubMed:30856238};
DE Flags: Precursor;
GN Name=CSEP0064 {ECO:0000303|PubMed:30856238};
GN Synonyms=BEC1054 {ECO:0000303|PubMed:23441578}; ORFNames=BGHDH14_bgh02874;
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14;
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23441578; DOI=10.1094/mpmi-01-13-0005-r;
RA Pliego C., Nowara D., Bonciani G., Gheorghe D.M., Xu R., Surana P.,
RA Whigham E., Nettleton D., Bogdanove A.J., Wise R.P., Schweizer P.,
RA Bindschedler L.V., Spanu P.D.;
RT "Host-induced gene silencing in barley powdery mildew reveals a class of
RT ribonuclease-like effectors.";
RL Mol. Plant Microbe Interact. 26:633-642(2013).
RN [3] {ECO:0007744|PDB:6FMB}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-118, DISULFIDE BONDS,
RP FUNCTION, INTERACTION WITH PR10, AND RNA-BINDING.
RX PubMed=30856238; DOI=10.1371/journal.ppat.1007620;
RA Pennington H.G., Jones R., Kwon S., Bonciani G., Thieron H., Chandler T.,
RA Luong P., Morgan S.N., Przydacz M., Bozkurt T., Bowden S., Craze M.,
RA Wallington E.J., Garnett J., Kwaaitaal M., Panstruga R., Cota E.,
RA Spanu P.D.;
RT "The fungal ribonuclease-like effector protein CSEP0064/BEC1054 represses
RT plant immunity and interferes with degradation of host ribosomal RNA.";
RL PLoS Pathog. 15:E1007620-E1007620(2019).
CC -!- FUNCTION: Secreted effector that increases susceptibility to infection
CC in both monocotyledonous and dicotyledonous plants (PubMed:23441578,
CC PubMed:30856238). Non-catalytic homolog of fungal RNases that binds
CC host RNA and inhibits the degradation of host ribosomal RNA induced by
CC ribosome-inactivating proteins (RIPs), preventing host cell death, an
CC inviable interaction and demise of the fungus (PubMed:30856238).
CC {ECO:0000269|PubMed:23441578, ECO:0000269|PubMed:30856238}.
CC -!- SUBUNIT: Interacts in planta with the pathogenesis-related protein
CC PR10. {ECO:0000269|PubMed:30856238}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23441578}. Host cell
CC {ECO:0000269|PubMed:23441578}.
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DR EMBL; CAUH01008659; CCU83233.1; -; Genomic_DNA.
DR PDB; 6FMB; X-ray; 1.30 A; A=21-118.
DR PDBsum; 6FMB; -.
DR AlphaFoldDB; N1JJ94; -.
DR SMR; N1JJ94; -.
DR EnsemblFungi; BLGH_06959-mRNA-1; BLGH_06959-mRNA-1; BLGH_06959.
DR HOGENOM; CLU_167694_0_0_1; -.
DR OrthoDB; 1857719at2759; -.
DR PHI-base; PHI:2903; -.
DR PHI-base; PHI:8918; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Reference proteome; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..118
FT /note="Secreted effector CSEP0064"
FT /evidence="ECO:0000255"
FT /id="PRO_5004107267"
FT DISULFID 27..113
FT /evidence="ECO:0000269|PubMed:30856238,
FT ECO:0007744|PDB:6FMB"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:6FMB"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6FMB"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:6FMB"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6FMB"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6FMB"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6FMB"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6FMB"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6FMB"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:6FMB"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:6FMB"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6FMB"
SQ SEQUENCE 118 AA; 13030 MW; 6AA9AEBBD278863E CRC64;
MRPFQLLSAL AIFINLEAVE AAAYWDCDGT EIPERNVRAA VVLAFNYRKE SFHGYPATFI
IGSTFSGVGE VRQFPVEDSD ANWQGGAVKY YILTNKRGSY LEVFSSVGSG NKCTFVEG
