AVX10_XANOO
ID AVX10_XANOO Reviewed; 1102 AA.
AC Q56830;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Avirulence protein AvrXa10 {ECO:0000305};
DE AltName: Full=TAL effector protein AvrXa10 {ECO:0000305};
GN Name=avrXa10 {ECO:0000312|EMBL:AAA92974.1};
OS Xanthomonas oryzae pv. oryzae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=64187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND REPEAT.
RC STRAIN=PXO86 {ECO:0000312|EMBL:AAA92974.1};
RX PubMed=1335800; DOI=10.1094/mpmi-5-451;
RA Hopkins C.M., White F.F., Choi S.H., Guo A., Leach J.E.;
RT "Identification of a family of avirulence genes from Xanthomonas oryzae pv.
RT oryzae.";
RL Mol. Plant Microbe Interact. 5:451-459(1992).
RN [2]
RP ACTIVATION DOMAIN, AND MUTAGENESIS OF 1064-GLU--THR-1101.
RX PubMed=9675896; DOI=10.1094/mpmi.1998.11.8.824;
RA Zhu W.G., Yang B., Chittoor J.M., Johnson L.B., White F.F.;
RT "AvrXa10 contains an acidic transcriptional activation domain in the
RT functionally conserved C terminus.";
RL Mol. Plant Microbe Interact. 11:824-832(1998).
RN [3]
RP BIOTECHNOLOGY USES REVIEW.
RX PubMed=25057889; DOI=10.1042/bj20140295;
RA Wright D.A., Li T., Yang B., Spalding M.H.;
RT "TALEN-mediated genome editing: prospects and perspectives.";
RL Biochem. J. 462:15-24(2014).
RN [4]
RP BIOTECHNOLOGY USES REVIEW.
RX PubMed=24602153; DOI=10.1111/tpj.12431;
RA de Lange O., Binder A., Lahaye T.;
RT "From dead leaf, to new life: TAL effectors as tools for synthetic
RT biology.";
RL Plant J. 78:753-771(2014).
CC -!- FUNCTION: Avirulence protein. Induces the hypersensitive response
CC (HR)in rice plants carrying the resistance gene Xa10. Activity depends
CC on the presence of the core repeat domains; replacement with repeat
CC domains from other proteins (AvrBs3 of X.euvesicatoria (AC P14727) or
CC AvrXa7 of this organism) does not elicit the HR. Probably acts as a
CC transcription factor in its host plant (rice) to induce plant
CC resistance or disease. {ECO:0000250|UniProtKB:P14727,
CC ECO:0000269|PubMed:1335800}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P14727}. Host
CC nucleus {ECO:0000250|UniProtKB:P14727}. Note=Secreted via a type III
CC secretions system (TTSS). Localizes to the plant cell nucleus.
CC {ECO:0000250|UniProtKB:P14727}.
CC -!- DOMAIN: The central DNA-binding region is composed of 23.5 tandem core
CC repeats with 1 base-specifying residue (BSR residue 13, also called
CC repeat variable diresidue, RVD, residues 12 and 13) each of which
CC recognizes 1 base in the target DNA. The BSR is probably the only
CC residue which contacts DNA in a sequence-specific manner.
CC {ECO:0000250|UniProtKB:P14727}.
CC -!- DOMAIN: The activation domain activates transcription of a reporter
CC gene upon expression in planta and in yeast. The 3 putative nuclear
CC localization signals seem to be highly redundant; only mutation of all
CC 3 knocks out the HR. {ECO:0000269|PubMed:9675896}.
CC -!- BIOTECHNOLOGY: By combining the central DNA-binding domain with the
CC catalytic domain of the restriction endonuclease FokI, TALE-nuclease
CC (TALEN) enzymes able to target specific dsDNA sequences can be created
CC that enable eukaryotic genome modification. Other potential uses as
CC transcriptional repressors, for transposon targeting, DNA methylation
CC or histone tail modifictions are also possible.
CC {ECO:0000303|PubMed:24602153, ECO:0000303|PubMed:25057889}.
CC -!- SIMILARITY: Belongs to the transcription activator-like effector (TALE)
CC family. {ECO:0000305}.
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DR EMBL; U50552; AAA92974.1; -; Genomic_DNA.
DR AlphaFoldDB; Q56830; -.
DR SMR; Q56830; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR InterPro; IPR005042; TAL_effector_rpt.
DR Pfam; PF03377; TAL_effector; 17.
PE 1: Evidence at protein level;
KW DNA-binding; Host nucleus; Hypersensitive response elicitation; Repeat;
KW Secreted; Transcription; Transcription regulation; Virulence.
FT CHAIN 1..1102
FT /note="Avirulence protein AvrXa10"
FT /id="PRO_0000430622"
FT REPEAT 288..321
FT /note="Core repeat 1"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 322..355
FT /note="Core repeat 2"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 356..389
FT /note="Core repeat 3"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 390..423
FT /note="Core repeat 4"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 424..457
FT /note="Core repeat 5"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 458..491
FT /note="Core repeat 6"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 492..525
FT /note="Core repeat 7"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 526..559
FT /note="Core repeat 8"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 560..593
FT /note="Core repeat 9"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 594..627
FT /note="Core repeat 10"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 628..661
FT /note="Core repeat 11"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 662..695
FT /note="Core repeat 12"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 696..729
FT /note="Core repeat 13"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 730..763
FT /note="Core repeat 14"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 764..797
FT /note="Core repeat 15"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REPEAT 798..809
FT /note="Core repeat 15.5"
FT /evidence="ECO:0000303|PubMed:1335800"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1093
FT /note="Activation domain"
FT /evidence="ECO:0000303|PubMed:9675896"
FT MOTIF 951..954
FT /note="Nuclear localization sequence A (NLSA)"
FT /evidence="ECO:0000303|PubMed:9675896"
FT MOTIF 997..1000
FT /note="Nuclear localization sequence B (NLSB)"
FT /evidence="ECO:0000303|PubMed:9675896"
FT MOTIF 1034..1037
FT /note="Nuclear localization sequence C (NLSC)"
FT /evidence="ECO:0000303|PubMed:9675896"
FT COMPBIAS 978..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1064..1101
FT /note="Missing: No hypersensitive response (HR) activity in
FT planta, no reporter gene activation."
FT /evidence="ECO:0000269|PubMed:9675896"
SQ SEQUENCE 1102 AA; 116185 MW; 4D459D6A9A260318 CRC64;
MDPIRSRTPS PARELLPGPQ PDRVQPTADR GGAPPAGGPL DGLPARRTMS RTRLPSPPAP
SPAFSAGSFS DLLRQFDPSL LDTSLLDSMP AVGTPHTAAA PAECDEVQSG LRAADDPPPT
VRVAVTARPP RAKPAPRRRA AQPSDASPAA QVDLRTLGYS QQQQEKIKPK VRSTVAQHHE
ALVGHGFTHA HIVALSQHPA ALGTVAVTYQ DIIRALPEAT HEDIVGVGKQ WSGARALEAL
LTEAGELRGP PLQLDTGQLL KIAKRGGVTA VEAVHAWRNA LTGAPLNLTP DQVVAIASNI
GGNQALETVQ RLLPVLCQAH GLTPDQVVAI ASHGGGKQAL ETVQRLLPVL CQAHGLTPDQ
VVAIASNIGG KQALATVQRL LPVLCQDHGL TPDQVVAIAS HGGGKQALET VQRLLPVLCQ
DHGLTPDQVV AIASNIGGKQ ALETVQRLLP VLCQDHGLTP DQVVAIASNI GGKQALETVQ
RLLPVLCQDH GLTPDQVVAI ASNNGGKQAL ETVQRLLPVL CQTHGLTPDQ VVAIANHDGG
KQALETVQRL LPVLCQDHGL TPDQVVAIAS NIGGKQALAT VQRLLPVLCQ AHGLTPDQVV
AIASHDGGKQ ALETVQRLLP VLCQDHGLTP DQVVAIASNN GGKQALETVQ RLLPVLCQDH
GLTPAQVVAI ANHGGGKQAL ETVQRLLPVL CQDHGLTPVQ VVAIASNSGG KQALETVQRL
LPVLCQDHGL TPVQVVAIAS NGGGKQALAT VQRLLPVLCQ DHGLTPVQVV AIASHDGGKQ
ALETVQRLLP VLCQDHGLTP DQVVAIASNG GKQALESIVA QLSRPDPALA ALTNDHLVAL
ACLGGRPALD AVKKGLPHAP ELIRRINRRI PERTSHRVAD LAHVVRVLGF FQSHSHPAQA
FDDAMTQFGM SRHGLAQLFR RVGVTELEAR YGTLPPASQR WDRILQASGM KRVKPSPTSA
QTPDQASLHA FADSLERDLD APSPMHEGDQ TRASSRKRSR SDRAVTGPST QQSFEVRVPE
QQDALHLPLS WRVKRPRTRI GGGLPDPGTP IAADLAASST VMWEQDAAPF AGAADDFPAF
NEEELAWLME LLPQSGSVGG TI
