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Database: UniProt
Entry: X0CWQ9_FUSOX
LinkDB: X0CWQ9_FUSOX
Original site: X0CWQ9_FUSOX 
ID   X0CWQ9_FUSOX            Unreviewed;       922 AA.
AC   X0CWQ9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=ATP-dependent helicase C23E6.02 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOQG_01458 {ECO:0000313|EMBL:EXK98601.1};
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:EXK98601.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK98601.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK98601.1,
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.
RN   [2] {ECO:0000313|EMBL:EXK98601.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK98601.1};
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 PHW815.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; JH658363; EXK98601.1; -; Genomic_DNA.
DR   EMBL; JH658363; EXK98602.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000315_2_0_1; -.
DR   Proteomes; UP000030663; 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:InterPro.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd16449; RING-HC; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 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; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          214..404
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          562..614
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          756..910
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          99..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..665
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  103725 MW;  2E9C783226AAFB9C CRC64;
     MNSQPALSTT LDDTDDDLFR IPGAYDARWD DSSGAGPAFN IPQRRMVPQY IPMATSPNHN
     AIKDDPDLIF AGSVTRQIPS PSGRPILASG MNYPDLSRRH PGAPRAGVWP KYHSSPGSSS
     NSSELANLTR WSSGIDFVSG LDADGRPINP HLMSYAREAD SFHTPQLDQG ELDALLKNIS
     ADMDLPKAGL GEAPEGLKRP LYPHQDIALA WMKKMESGTN KGGILADDMG LGKTISTLSL
     LLDRRAPTRP KTNLIVAPVA LLRQWEEEIA TKTKPTHRLS VYVHHGKKAS IDELLRYDVV
     LTTYGTVAQE LKRFEKIVED HNERGGNINW NDTTISSKLS LLHPVKAQFY RVILDEAQCI
     KNKDTKGAKA CTQLKSIHRW CLTGTPMMNG IIELYSLVKF LRIKPYSKWE EFRQGFGVLF
     GRNGDPKHVA MDKLQALLKA IMLRRKKSSK LNGKPILVLP EKTEEIVYAE LSPEERDFYS
     QLEKHARVQF SKYLREGTVS KNYSNILVLL LRLRQACCHP HLNLDVDEAA PSSIPDEDKK
     QLVKELDQAI VDRIKEVEAF ECPICYDAVQ CPSFFIPCGH DSCSECLVRI VESASAVNLQ
     EGSESSRAKC PVCRGQFDPA KCFSYETFRE VHMPETVKKE SGMEPADDES DSGDDSETGS
     ESDYESDDEV DKKGNLKGFI VNDELSVEDE KISVKKERKG KGKRKDKGKG KSLDVKPAML
     KTLRKEAYKN REAFKKYMRY LRKTWEPAAK VTECMNLIKQ IEETGEKTII FSQWTLLLDL
     LQVAMSHEKM AKPERYDGSM SATLRNVAAQ NFRERKDTKV MLVSLRAGNA GLNLTAASRV
     IIMDPFWNPY IEMQAVDRAY RIGQQQEVKV YRILTKETVE DRIVDLQNKK KEMVEAALDE
     TAGSKIGRLS INDLKNLFGF NR
//
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