ID X0BZU2_FUSOX Unreviewed; 1531 AA.
AC X0BZU2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=NACHT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOQG_11489 {ECO:0000313|EMBL:EXK84453.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK84453.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK84453.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK84453.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the putative lipase ROG1 family.
CC {ECO:0000256|ARBA:ARBA00007920}.
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; JH658396; EXK84453.1; -; Genomic_DNA.
DR HOGENOM; CLU_000288_34_1_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR007751; DUF676_lipase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF05057; DUF676; 1.
DR SMART; SM00248; ANK; 12.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 70..193
FT /note="DUF676"
FT /evidence="ECO:0000259|Pfam:PF05057"
FT DOMAIN 368..517
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|Pfam:PF13401"
FT REPEAT 1190..1222
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1290..1322
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1323..1355
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1389..1421
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1531 AA; 173250 MW; 78617499DBA9F730 CRC64;
MKRLHTRTKH SAQGSNPVPE ASGASQLVHS GASTGQPKPV VETPVLGLIQ LWPDPDLESA
SHIQTEVDLV AIHGLGGHAY KTWREGEKLW LRDFLPHDVP TARVLTFGYN AGVAFTQSKS
NIRDFATSLL EGIRTFRRRN KEADRKMIFV CHSLGGIVFK QALVIAHEKE TRYGSIKEAV
AGVIFLGTPH RGADIAYWSK LLAKFANVLT AGKMREDLLK ALAPKSTELG TICSQFVERG
MRLQIFSLYE RHETSGLGSL VVDEFSAILH LPNETPIPME ADHRGLCKYL TPSDSCYRTV
FNCIEELMDS LIETSEQPYF DSSQREFLSK LRAVDHDTVL SKIPGGWTRS SRWFLELPEF
KSWRVLQGQQ TLWLYGVPGS GKTVLMKSIV EFLNSQSDIA SSPVIWKPIS FFFDDKDPER
KTSDSFIRSV LDQILGDSRC ASVIRYLDFD PSKIPDTEKS LWECFQTIVK RSRGIIFQLV
IDAMDEALRH NENPPTIVDK LRDLVESDAS GRVRMLLSHR EQPPYGFPQR TDAAVISIDN
ENTRKNVDEF VQMKVRSSLQ ESKLSLSMAS TIEAKIVKKA QGNFLFATLA WKQFSNGTVQ
WTRDKIKASL TGLDKTSDDL VDFYCQLLSN ISSRYRQKAK IAFTILRLCK ESISPTQLAT
MAVMVDMEGI EQDEDLEELK AQAADFEEYL VQACEYMVKI DNNSVQFVHV SVKDMLSMSL
GMHSPRNQSI ISELTVSNSE GQSIMLNICL KTMHLERRSP ESWLETYGAM TEALRSLRET
FSGLVPNHEQ LTQIDELTNS HVDSMSKTSC LAYAVRNWFQ HYKEASPSVE QDVKIINFLS
TMNGCLCYLL WYQLPTKDDG GKMPYLSRYP AAHLPLESSR TMTLFRVIAL GDLPRLVGAI
LRRGVNINYL AGTVTPLSWS IICRRRDSFQ ALLESNEIEV NYHAYRQRAS IHHAASCIED
TFYMERLLEF TNIDVNAVGD NGTPLHVAIS SKNIQGADKL LNHPGVNIYF KADMEESPYS
MAFRHKIWEP FLLRILDMTE KPKPPSTRQA YGTSQLLWAG VHGWTNMEER ILREDHNQVF
LVDQESRMNA LAHYAYFGRK EKLAWIIDRL PTHGLLLRGA SDRYDLLHLC ASQDWEDMVH
LLQRKYKLKS LKFDHQGRNM LHWIMEHGWD LDRFDLSYYS VSDLNSQDRD GLTPMHIAAS
NRNIHALEVL VISGADPYLK DKRGMSPAHL AAQVGWRKGV EYLTDTSHRE LGRTRDGATL
LHLVAIWFEG SLVSKLLCSR QGMTNARDGN RRTPLHYASI NDNASAMIAL LDAGGEINAR
DENGMTPLHE AIRCLSVKTA RLLLKRGADF KAIDGFGQTC LHLSVRYKHN YLLKKFIKIG
LAANAYDKFG MSPLHRACST GVSEHVQMLL EKGASYKARN THQRSPLDIA VHRENVKAIE
VLISWLDHSA KRGNKKPRRS RTSQELLDQA LLLAYQFGCE KASAKLRSAG AKADKSTISV
RQVYMDGPSP ESRWPLKPYK SQTRSAINKE L
//
