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Database: UniProt
Entry: F9FLM9_FUSOF
LinkDB: F9FLM9_FUSOF
Original site: F9FLM9_FUSOF 
ID   F9FLM9_FUSOF            Unreviewed;      2102 AA.
AC   F9FLM9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DUF676 domain-containing protein {ECO:0000259|Pfam:PF05057};
GN   ORFNames=FOXB_07309 {ECO:0000313|EMBL:EGU82178.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU82178.1};
RN   [1] {ECO:0000313|EMBL:EGU82178.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU82178.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- SIMILARITY: Belongs to the putative lipase ROG1 family.
CC       {ECO:0000256|ARBA:ARBA00007920}.
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:EGU82178.1}.
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DR   EMBL; AFQF01002185; EGU82178.1; -; Genomic_DNA.
DR   STRING; 660025.F9FLM9; -.
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; 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; PTHR24133; ANKYRIN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR24133:SF40; SOCS BOX DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 6.
DR   Pfam; PF05057; DUF676; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 19.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 10.
DR   PROSITE; PS50088; ANK_REPEAT; 11.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          55..207
FT                   /note="DUF676"
FT                   /evidence="ECO:0000259|Pfam:PF05057"
FT   REPEAT          1085..1117
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1118..1150
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1151..1183
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1283..1315
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1316..1348
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1347..1379
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1382..1414
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1417..1449
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1487..1519
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1559..1591
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1627..1659
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1884..1926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1945..1966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..963
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1895..1909
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1910..1926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2102 AA;  234301 MW;  76EA6013C9A97050 CRC64;
     MRLGRRREES LSSSDDTTIS DQDDEPHYEY ILKEMYVPFL NDNSFADQKD LVDLVFVHGL
     GGNLRTTWKK EGTTEPWFTK PEFLGRLKDS VRVLSFGYNA HRFGDVANTR IIHHANDLLR
     NLVLKRLDHP DRPLIFIAHS LGGLVVKRAI LLCATNDDWK AVKQATKSII FMGTPHMGSE
     KAEDLVVVQK LASLMKLQTA VATNLTKELR AFSNSVQDIN MEFTIDVHRS IKLLCCYESH
     PQRLPNGTKE IIVPQWSAVL QGVDNIDLNC THSGLPKFAS PLHPRFELFW GEVERLVRLA
     ESPPIKPIKK APTWTDDDAT QYETPLTCPK NANFPRPSPP RPRQNAPLRR RHEVGKASKS
     SRESAIRSSV DKLLKEVTSR INVDLPTQHE TAVSQAQNRT QPEKFDVKDF NDFTRLLRSV
     TPENKGLDRE APHWQTCSWI LEDPAFVKWK ENKNGSLLFI TGSPGCGKSN LAKYIQGAMK
     DSSDERWEEN LVIPFYCDSL ESSRHNPPIL DLVVQSMLSK YTTMSQATRK KLESVLETLG
     VDRQKSRSPL ETENSGHFIQ LMEIVQLLAT AEDARPTCLI IDGLDQCEDE FIIRLLRGLD
     TIFRRESSAS ALKVVVTSRM ADSIRGFALA NNHIEVTPDM ILKDIQKVVD EEVDRIILSR
     RIATVGRASV SAVIVERSNG SFLFASAVLK ELWHIKDTGA NSVFTLVTSC PPTMEAIYQQ
     DMDRIQNERN DLFQLIQIIC IARSTLRIEE AKEILRFLNP SVTRTYDLVG DLTRTCQRLI
     RFGAEDTLEL LHQTLYDFIL DTYDLKLVHQ TLATACLKYV REIDWEPYHD PWTDYCRDAL
     ADRYVFLEYS SAWFRYHLKF FGPDTYKISW DLWDFIRSPA GEKWRYYTFQ KRAWGSRSPS
     PTRSFALFRA QTPSPSRSRS RSSNGSRTRS PPAIERPQTP SSAAGKQTED MTEAGYLSDS
     TDDSVSKCDS DGSGGRGRLI TTTQSSIQSA KPPLVLLAQW DADLVIKEIF SKALELNPNS
     FLHKIYDLLL HISPKSKQEV EEDLETLVNN IWEGTTAIHY AAAQPGAALE VLLPFARNVD
     LPDNDGSTPL ILAAVRGHCR SVRALLKAGA KVDAVDPWNQ TALFTAVDVG AVDVVQTLLE
     FGADPNISSI NGHSPLALAT GKNSSEMVEI LLEFSADLDA PAFDGKPIPF LASWMGSTDA
     LEILVQHVDV DQVWRNERLI HMACFKGWKG VVDKLIEKHA NLNDPPRDLP KASPVALAVE
     SGHSDILRTL LAAGAAVECP VKGMSSPLHI AVAAQNLLGC ELLLDAGCQV NAEDRDGSTA
     LSIAADLNDL DIVECLVSHG ADPSKPDYET PLHIAVDWGN LEMVEIILSS RFFIDIDAKD
     EKEYTALGIA ATTGRLDIVS MLLDHGADPN MRNGQRNSSA PLHIAANKGH RSIVIELLKR
     GADPYPETTK ESSAFHAACI GGWLDVMETF LEVVDDVGEL VNFEWGWAGT PLKAAASGGR
     LDAVKLLLSK GADPKNQLQS KINRGQTIIH AAAEGGNTQV LETILEAVDD SSLEIRDRAQ
     RTPLWYACVE GHEDMVKYLL ERGASTDVIF DDGDNIIPII VSGGSEKNLK LVLEKNPNLD
     TDCILPDGET PLFKAVNSGH DKVVPSLLER GADVNRKSKY GNVPIFGAIT NRQYDTLRIL
     LEHESIDLTQ RDSFDRTALQ IAQQSGTRLM PAIVLGAAQD SDVERILTEN RDMYGLNAYD
     LTRPEANNPA PFDRCVEGVR RDAQSLLDDF DLHGLGSYSF AQIALQRSAR AVETTPLVLQ
     HDNYCDMCLA TIAGPRYVCC TCCTVDLCEL CVRQDKKPGN RTWGCDYHSF LTVNLPKIQA
     PDVMLRTEID FHVPTLLSPI EEVASETSQG GAESDGDEPF REPSSLQDDE KAQDGVSLSS
     GDTSNSYTMA IEPLTTQSST AVTGYSVDDG ELPDTATNKS SALAKEEWSD RTEDELREFL
     EAVLKTFTTY QTPNGISKWN FSVDGWTLRY KDDALKSSWT EGDENAKIVQ PAREWMPLQP
     LTEAYYYLSG LSYLMADVPL YLVATGLAFH GYEDEALRRR KRLQRLHHKV IFPVTRHGEV
     VV
//
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