GenomeNet

Database: UniProt
Entry: X0AQS6_FUSOX
LinkDB: X0AQS6_FUSOX
Original site: X0AQS6_FUSOX 
ID   X0AQS6_FUSOX            Unreviewed;      1458 AA.
AC   X0AQS6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=ATP-dependent helicase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOMG_05688 {ECO:0000313|EMBL:EXK42953.1};
OS   Fusarium oxysporum f. sp. melonis 26406.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK42953.1};
RN   [1] {ECO:0000313|EMBL:EXK42953.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK42953.1};
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 melonis.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXK42953.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK42953.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT   26406.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JH659331; EXK42953.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:FOMG_05688; -.
DR   HOGENOM; CLU_001592_2_0_1; -.
DR   Proteomes; UP000030703; Unassembled WGS sequence.
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   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18070; DEXQc_SHPRH; 1.
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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR   PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          326..526
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1107..1145
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1222..1377
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          40..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1164..1193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1458 AA;  166870 MW;  954961FDB1E1BEC7 CRC64;
     MARNKARSRR STAEAVHLHV GLDDLMPTSF VEGLISIMIP ENETSDQPSS SHENGPPTKR
     RKTESSLALN AIPIAKKEFT ISRPCAGPSS KSQSFVCKSV DRYMSIHFMD NRLRMKSRKD
     YPSEPLDVTV RLRRAEEDDQ MKISYILDST SQRASQPNAL WSTFDLELEW QGRQVKMTYY
     RNFYWNESPS PHSQYRSSLD RKNSQPFINL LLRGSISTGT PYRAPTWSPV DFYEAAFVPK
     KDEKTPETIQ VDALESKLFP YQKRTLQWLL QREGVQWSAD MRRIVPYVPE NQDSVYDFKK
     MTDVAGNEYY FSELFHTVTR DISLFQQAEA SIKGGILAEE MGLGKTLEVL GLILLHQRSR
     PLIQSEYESQ AKLTPSGATL IVTPPSLKDQ WVSEIARHAP GLSVKVYEGR KRISEADEQQ
     ATDELAGHDI ILTTYSVLSS ELHFTTAPPE RSRRHARVYD RPRSPLVQIS WWRVCLDEAQ
     MIESGYSQAA KVARVLPRIN AWGITGTPVK NDVEDLQGLL LFLQYEPYCS VNQIWQDLIR
     HHKSVFQRLF NRIAIRHTKS MVRDELVLPS QKRFVISMPF TAVEEQHYQS LYREMAEACG
     LSLEGAPIVD GWKPEDHEED MRTWLVRLRQ TALHPEVAGY NRRTLGNSKN RPMRTVDEVL
     DAMLEQSESA IRSDERAYLS SKLTRGQLYE NSPRVKEALE IWLSGRDEAQ KLVSKSRDEL
     KSLTGSRLRP ASHEDSDIDD DSEVEEKGQL FESRRRLRGA LEMYHRAVFF CANAYFQIRE
     NPEMTEPESE EFLRIKKLED EHYEEAKAIR REILQEPHHK ATRLMAKVAQ KASEQSFVEI
     PELTVNEERG IESGRIVDDL EALYGELNDQ ANAIDEWREH LVGLVLKPLV DEEDDAETTG
     DEYGESAKIQ DELMVYVQAL RAIIADRQDA LTGQTNELIK HETQTSLRLA ANEEGPAPEK
     LIELLTLRDQ IKPRSTSMRK AISEFRGLTS KLARDTTRSV LEGRIADRQL KATQAILNTQ
     SKLTTALEAE VDKFKNIMNL RLEYYRQLQV VSDSVLPYEE PVTEELMTRL KTTEENMRQR
     LSAAEAKHRY LLHLKEAGNK SNEPRMCVIC QTNFTIGVLT VCGHQFCKEC MMLWFKAHHN
     CPVCKRKLKS SNLHDITINP QQLKVHSDEP TQCQDSTENS PEQKQTDSPK KTGIYSEFNS
     DKLAEIQKIE LDGPSFTTKV DTLVKHLMWL RESDPGAKSI VFSQYKGFLG ILRNAFSRFR
     IGYASIDDPD GIRRFKENAS VECFLLHARA HSSGLNLVNA SHVFLCEPLL NTALELQAIA
     RVDRIGQMHE TTVWLYLVSG TVEESIYNLS VQRRMEHMGR VNKGKSKEST PELLDVNIEA
     ANTLELEQAS LSRLMSKDKS AGENVEENDL WECLFGHIAR KDTEHEKDIR LQEKAVMGYL
     AAEAAEERMD RTDQIPGS
//
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