ID   AVR4_PASFU              Reviewed;         135 AA.
AC   Q00363;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Race-specific elicitor A4;
DE   Flags: Precursor;
GN   Name=AVR4;
OS   Passalora fulva (Tomato leaf mold) (Cladosporium fulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX   NCBI_TaxID=5499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Race 5;
RX   PubMed=8114941; DOI=10.1038/367384a0;
RA   Joosten M.H.A.J., Cozijnsen T.J., de Wit P.J.G.M.;
RT   "Host resistance to a fungal tomato pathogen lost by a single base-pair
RT   change in an avirulence gene.";
RL   Nature 367:384-386(1994).
CC   -!- FUNCTION: This necrosis-inducing peptide induces a hypersensitive
CC       response on Cf-4 tomato genotypes. Race-specific elicitors are
CC       compounds which only induce defense responses in genotypes of host
CC       plants which are resistant to the pathogenic race that produces the
CC       elicitor, but not in susceptible genotypes.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X78829; CAA55403.1; -; mRNA.
DR   EMBL; Y08356; CAA69643.1; -; Genomic_DNA.
DR   PIR; S41047; S41047.
DR   PDB; 6BN0; X-ray; 1.95 A; A/B/C/D=35-113.
DR   PDBsum; 6BN0; -.
DR   AlphaFoldDB; Q00363; -.
DR   SMR; Q00363; -.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   KEGG; ag:CAA55403; -.
DR   OMA; KGLQWND; -.
DR   PHI-base; PHI:18; -.
DR   PHI-base; PHI:5476; -.
DR   PHI-base; PHI:5487; -.
DR   PHI-base; PHI:5546; -.
DR   PHI-base; PHI:5556; -.
DR   PHI-base; PHI:5561; -.
DR   PHI-base; PHI:5567; -.
DR   PHI-base; PHI:5584; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IDA:PHI-base.
DR   GO; GO:0140320; F:PAMP receptor decoy activity; EXP:PHI-base.
DR   GO; GO:0140403; P:effector-mediated suppression of host innate immune response; IMP:PHI-base.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   Pfam; PF01607; CBM_14; 1.
DR   SMART; SM00494; ChtBD2; 1.
DR   SUPFAM; SSF57625; SSF57625; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chitin-binding; Disulfide bond; Signal; Virulence.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..29
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000020767"
FT   CHAIN           30..135
FT                   /note="Race-specific elicitor A4"
FT                   /id="PRO_0000020768"
FT   DOMAIN          47..111
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   REGION          19..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        86..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   HELIX           42..48
FT                   /evidence="ECO:0007829|PDB:6BN0"
FT   TURN            53..56
FT                   /evidence="ECO:0007829|PDB:6BN0"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:6BN0"
FT   STRAND          64..72
FT                   /evidence="ECO:0007829|PDB:6BN0"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:6BN0"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:6BN0"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:6BN0"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:6BN0"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:6BN0"
SQ   SEQUENCE   135 AA;  14559 MW;  CE2A2C29B7F2A7E0 CRC64;
     MHYTTLLLST LLVGTALAQP TNPPAKTPKK APKTQPYNPC KPQEVIDTKC MGPKDCLYPN
     PDSCTTYIQC VPLDEVGNAK PVVKPCPKGL QWNDNVGKKW CDYPNLSTCP VKTPQPKPKK
     GGVGGKKASV GHPGY