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ATR5_HYAAE
ID   ATR5_HYAAE              Reviewed;         367 AA.
AC   M4C699; E6YE64;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Avirulence protein ATR5 {ECO:0000303|PubMed:21361788};
DE   AltName: Full=Arabidopsis thaliana recognized protein 5 {ECO:0000303|PubMed:21361788};
DE   Flags: Precursor;
GN   Name=ATR5 {ECO:0000303|PubMed:21361788};
OS   Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS   (Peronospora arabidopsidis).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Hyaloperonospora.
OX   NCBI_TaxID=559515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, AND INDUCTION.
RC   STRAIN=Emoy2;
RX   PubMed=21361788; DOI=10.1094/mpmi-12-10-0278;
RA   Bailey K., Cevik V., Holton N., Byrne-Richardson J., Sohn K.H., Coates M.,
RA   Woods-Toer A., Aksoy H.M., Hughes L., Baxter L., Jones J.D., Beynon J.,
RA   Holub E.B., Toer M.;
RT   "Molecular cloning of ATR5(Emoy2) from Hyaloperonospora arabidopsidis, an
RT   avirulence determinant that triggers RPP5-mediated defense in
RT   Arabidopsis.";
RL   Mol. Plant Microbe Interact. 24:827-838(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Emoy2;
RX   PubMed=21148394; DOI=10.1126/science.1195203;
RA   Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA   Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA   Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA   Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA   Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA   Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA   Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA   Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA   Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA   Tyler B.M.;
RT   "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT   arabidopsidis genome.";
RL   Science 330:1549-1551(2010).
RN   [3]
RP   IDENTIFICATION.
RC   STRAIN=Emoy2;
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Secreted effector that acts as an elicitor of hypersensitive
CC       response (HR) specifically on plants carrying defense protein RPP5.
CC       {ECO:0000269|PubMed:21361788}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21361788}. Host cell
CC       {ECO:0000305|PubMed:21361788}.
CC   -!- INDUCTION: Expressed in spores as well as during host plant infection.
CC       {ECO:0000269|PubMed:21361788}.
CC   -!- DOMAIN: Has the canonical EER motif, but lacks the canonical
CC       translocation motif RxLR, which characterizes most oomycete effectors
CC       identified so far. The EER motif is not required to trigger an RPP5-
CC       dependent immune response. {ECO:0000305|PubMed:21361788}.
CC   -!- MISCELLANEOUS: The ATR5 effector protein is a polymorphic member of the
CC       RXLR class and displays copy-number variation among different isolates
CC       of H.arabidopsidis. {ECO:0000269|PubMed:21361788}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   EMBL; FN598669; CBI63251.1; -; mRNA.
DR   EMBL; JH597955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M4C699; -.
DR   SMR; M4C699; -.
DR   EnsemblProtists; HpaT814631; HpaP814631; HpaG814631.
DR   VEuPathDB; FungiDB:HpaG814631; -.
DR   HOGENOM; CLU_755352_0_0_1; -.
DR   PHI-base; PHI:4735; -.
DR   Proteomes; UP000011713; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..367
FT                   /note="Avirulence protein ATR5"
FT                   /id="PRO_0000447270"
FT   REGION          33..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           61..64
FT                   /note="dEER"
FT                   /evidence="ECO:0000305|PubMed:21361788"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   367 AA;  41475 MW;  8ECF43F88031951E CRC64;
     MRLISPALVV STAIQARHVN SSAPVDSAMT EANPLASAHP PDVGYDGVPA GRVRNPDDPT
     TEERTPGESF MEAINFKIFK LVQEAQGRIL GLPEQPRGDM EWLERYGQDA ILHYLETGDK
     DPSQLEKKYD QLLDELKNAP NLEVEILESI HALFLAYMEE VAKPAVQTTP KLNEQPDKFA
     WAMINKARRN AKPGIRNPYK SLNIPLVENY IKKYNAFIEL RQRELTLLDT FSCAFNHNTV
     KLAKFLAMVD TFSPKRTFVL AMRIELSEIW IEEKRTIAEV ASILGISTIT GYAKNRLSAG
     TFVRFIYQLA KTNEQLGPDI VKDLVKTFGP DRTTELLTRM KTVSPRMFTI LKDHMDVRLK
     ETGVTPN
 
 
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