ID A0A2H3H4Z7_FUSOX Unreviewed; 1366 AA.
AC A0A2H3H4Z7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=NACHT domain-containing protein {ECO:0000259|PROSITE:PS50837};
GN ORFNames=AU210_005664 {ECO:0000313|EMBL:PCD37160.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD37160.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD37160.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD37160.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD37160.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD37160.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCD37160.1}.
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DR EMBL; MABQ02000004; PCD37160.1; -; Genomic_DNA.
DR STRING; 327505.A0A2H3H4Z7; -.
DR OrthoDB; 2330391at2759; -.
DR Proteomes; UP000219602; Chromosome 5.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.1020; Prion-inhibition and propagation, HeLo domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR029498; HeLo_dom.
DR InterPro; IPR038305; HeLo_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF14479; HeLo; 1.
DR Pfam; PF05729; NACHT; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 12.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 8.
DR PROSITE; PS50088; ANK_REPEAT; 8.
DR PROSITE; PS50837; NACHT; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000219602};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 251..394
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT REPEAT 759..791
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 792..824
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 825..857
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 858..890
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 891..917
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1011..1043
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1044..1076
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1077..1098
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 89..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1366 AA; 150741 MW; 37492830D97CDE98 CRC64;
MEPVGLAVGL VGLFSTCMDV MQRIDSYRTA GRDSRQLDAQ LNATMHLLEK WGDGVGISKG
KLSDNHHPDL DNPRTFAVVQ GLLNSIKDFS ATSDEPPSPR GLQKTPSFPS SGDLSSHGSK
ISRWQKTSWA LRGKLKQTSH VQALASLVSD LYSVVSPDTT GSKALTRTPS FKDLSISADE
QPYAVEIREL LQKIEEEMEA DKIRDLHLWL GAPPPNDVFS DSNDKRIQKT CEWILHRDEF
LEWQKPSSSS KLIWIKGPAG FGKTVLCARI VQELERTAQE PVAYFFLSSR YDGRDDPFSA
IRAWLTMMIQ RSPAARDIVT KTRLSQHEPL ASQATILRAF RELIVGVPGC ILVLDGLDEC
TGMTNTDTKS VPHFLQELRI AITNTTTKIL ISSRGDPVIQ QGISDFTGYS EYAIIPDDVG
PDLMAYSSEL VKAKLPNKDE PTRASIAQKM TNRSEGQFQW VKLQEGSLRK GRSRKQLERE
IDETPSGLDS LYDREWNRIN AMGDSDRERA LSLLRWTAFA LRPLTVHEIT EAVLLTEGMD
ELPVDEMPDC VDQDYVDSMI LELCGSLIEV RHVSSSESIK HPECIQQSEE DSVGFQEVHL
SHFSVKEYLL LKTFPGTGTL LCNEKLRVTN GTIHNTTLAK HCLRFISFPG AWESLKMSDN
KRPTMHFMPY AADSWYQHCR DVKTIDPDLQ QAINALLDTR NQNWPFVREF VATKVFGDDT
DVQERSISPF VFAVCSGLTD TVAHLIREGR FDMNDRSFGN STPLFWACFT ESKNIVELLV
ENGADINARC YQGQVPLHNS VQDGNDGIME LLISKGADVS VVDDERQTPL NLASMSGNTK
AARQLIDRGA DISHETTAGF TPLSMASSRG HVELAKLLIK RGADVNQVVA NGPPPLLLAV
CDDHSELAEL LIDEGAERTG IQIKGQVFSL LAMAAGYGHL NTAKALISKG FNPTEAQPLL
LAASYGSYSG FSRDFIPETA TTSPDFPCLA YHQVLELLLQ SGADVNTSDV RGYTPLYMAS
LGGFIDIVEI LTQKGAGLNV KTVAGETPLH ASSAMGHLRV TQLLIQHGAD AASKDNSGRN
PLHYACRSGD LEVVNLIIGS SQTQTLDEAD HWGSTPLSLA ARFGGVGILM ALIDTGVVEV
KSSDMFGRTT TWWATSHNHD AVARLLAGTD GHRDLGTDVE EGEAVQEQGL EMGTYCDICW
LFISGQTHVR CVICRTCHQA IKMKLISSLL TTMLAGSMVS AKYTVEIPDD AVWVTNWDEL
HAAPRFEGVL LPKYGGFVIE VDEKIVLATN ERMSKEVFDL LTDLEKNDPQ PEDEQQTPNK
RDTEIRGYGN RCSHPPCFGP GLCSQYSHCH VCSGLTGVVF KRGRCI
//
