ID G3C9T0_HYAAE Unreviewed; 573 AA.
AC G3C9T0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=RxLR effector candidate {ECO:0000313|EMBL:CCC55856.1};
DE Flags: Fragment;
GN Name=RxLL429 {ECO:0000313|EMBL:CCC55856.1};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EMBL:CCC55856.1};
RN [1] {ECO:0000313|EMBL:CCC55856.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Emoy2 {ECO:0000313|EMBL:CCC55856.1};
RC TISSUE=Conidiospore {ECO:0000313|EMBL:CCC55856.1};
RX DOI=10.1371/journal.ppat.1002348;
RA Fabro G., Steinbrenner J., Coates M., Ishaque N., Baxter L.,
RA Studholme D.J., Koerner E., Allen R., Piquerez S.J.M., Rougon-Cardoso A.,
RA Greenshields D., Lei R., Badel J.L., Caillaud M.C., Van den Ackerveken G.,
RA Parker J.E., Beynon J., Jones J.D.G.;
RT "Multiple candidate effectors from the oomycete pathogen Hyaloperonospora
RT arabidopsidis suppress host plant immunity.";
RL PLoS Pathog. 7:E1002348-E1002348(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; HE574778; CCC55856.1; -; mRNA.
DR AlphaFoldDB; G3C9T0; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031099; BRCA1-associated.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13763:SF0; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN; 1.
DR PANTHER; PTHR13763; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN BRCA1; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 10..48
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 92..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCC55856.1"
SQ SEQUENCE 573 AA; 63830 MW; 771111E52C842760 CRC64;
VETFSGQLQC AICLCAYENP VSLPCNHFFC EECIHRALEL KTLCPICKTP ANKRRLRYDT
TLRELLRAME MLSAAPGAVA IDKTVAAKEE VPSKREVAKV ADPQPSLRRS RRNSTATSSL
SIDVQVDGKA PLLGDHAEIK EERNAVLGTD LAERRSSPRR ALLQDVKSPT TQLDPLTIGS
INMATPRCVN ARACKTIKGD SVETVVLQPH IDVDDGKTVN VVAARTQLDD VVEQKQQRTT
RRRRQLRMTS DTVQDDDTQR VPNTRLRSAT NQVVVAGIKP EMSSLQTPTL RKRRRSAIIG
VAPDAVESIA LKKKAVSSGQ TSPRLESAGT LSLAVDYQTQ PLPNVEAKVI YQVGDLVDVI
ERQWVGINKR GGAARITKVH GDGFYAVRFV MGCKDKCVPE SYIRRPAEEL IAETTPSHVV
KQRLRRRVSN TIISPDSAAT KTKGSTDTSE VKVKKVTKQK RSGMVFLCSG FEKQRMQQIN
EWADELEAEV VQFWTHDVTH LIVECIHDDD VEDGDSSIED FDSSSSQPEH HHDKPRLFIN
SKSGRWVKTR SLKYLKALVG GRWIVSDEWL QGQ
//
