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Database: UniProt
Entry: F9F3X7_FUSOF
LinkDB: F9F3X7_FUSOF
Original site: F9F3X7_FUSOF 
ID   F9F3X7_FUSOF            Unreviewed;      1039 AA.
AC   F9F3X7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Helicase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS51194};
GN   ORFNames=FOXB_01102 {ECO:0000313|EMBL:EGU88381.1};
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:EGU88381.1};
RN   [1] {ECO:0000313|EMBL:EGU88381.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU88381.1};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EGU88381.1}.
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DR   EMBL; AFQF01000433; EGU88381.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9F3X7; -.
DR   STRING; 660025.F9F3X7; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF971; RNA POLYMERASE-ASSOCIATED PROTEIN RAPA; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          739..897
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1039 AA;  117948 MW;  389136F236B77F55 CRC64;
     MDSGFSVHQP EAISNPDPTL QNAMSIFGAS PSTTGQKRST SPTNDEPSKR AKTDGDPAGP
     SGDNQQLDNE NEASGVDSAD QAEEVPEVIE SPDNDTEDAP RIRLPYGFPP ISPDKLQELR
     EWLASHANLK GDNQVATGIH TQLLKSMEPR QQDLEEICRM MGVETNGINW RGGIRIPGVM
     EGGLKARPHQ IAGANWISTT LESPLRAALL ADECGTGKTV QIGLALAIHY YRVKAEVEAG
     TFRPRDEKRR FKPSIILCPP DLAYQTFREW CHWFPNFFNI RICHRTKFLT GDFFTRLHIM
     DHKNGLQAWV DQNAASHENI ETLRSIAIVP YHTAMRRMIT RKKKEDASEA QDHEENENGD
     NNGAGPARGR RQQRQARPRR KKGDTVEKQE IEFKITGQSY NWVICDDVYP IRGPRPITHK
     LIHQLEHEAT LWPFVFKPHH GNIDPQVYFD RRAWRAIQAG GEFGGLSINS IVQPNRFIGP
     LPARDQLMKD EYTAYIQEKK GPLFLMNPDL FQRFSEKIKS LRPEMAGKAI RPLLEMFCLR
     RGMLTPATMP DGTIVVPGEG IPPMHIRTVV LQPFNEDDKE KMYQIAKKHY PKLFAAANED
     DEEIGDGTID KAKLTWVNPA VLRTLALSTT NVEFYRLTQK RDRDGKTTFL NSKAVQRLLN
     NPSHFDRLHS FSLPGAAAPN AAADSKNIEN NLFNDGVGGL QWYFTEMQKG RGRGRRVEFP
     TIREDIPKAF CSRSAKLCWT INRVLELKEQ GKRVLIFVNQ PLTSTILTAL LTSLYVNTLS
     IRSKHDVDQR ASIVRQFNNP ENGAEALVMS SQLGGFGLNL QGACHHGIIV EYPENVPTML
     HAFGRLWRMG QEHEVHWDVL YLENSFDGWT ETRMVSKYAD ILAAEGEIPD MIQKEYRIIC
     AFELIKRYLG QDCNRYPRTR VTWYEQDHPL VAREGHFYSA VANYLMENPG HYERFLQSLS
     DIARRWSPDQ GELTLDMIEG RSPVLANGVI LDSRNPNTPG YVAVTAGDDM HQERKRAVEI
     QSNLRVDDSR LNLERERRV
//
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