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Database: UniProt
Entry: X0MDF4_FUSOX
LinkDB: X0MDF4_FUSOX
Original site: X0MDF4_FUSOX 
ID   X0MDF4_FUSOX            Unreviewed;      1630 AA.
AC   X0MDF4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Chromodomain-helicase-DNA-binding protein 1 {ECO:0000313|EMBL:EXM36208.1};
GN   ORFNames=FOTG_00451 {ECO:0000313|EMBL:EXM36208.1};
OS   Fusarium oxysporum f. sp. vasinfectum 25433.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089449 {ECO:0000313|EMBL:EXM36208.1};
RN   [1] {ECO:0000313|EMBL:EXM36208.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=25433 {ECO:0000313|EMBL:EXM36208.1};
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 Cotton.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXM36208.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=25433 {ECO:0000313|EMBL:EXM36208.1};
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   "The Genome Annotation of Fusarium oxysporum Cotton.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the polycystin family.
CC       {ECO:0000256|ARBA:ARBA00007200}.
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DR   EMBL; JH657918; EXM36206.1; -; Genomic_DNA.
DR   EMBL; JH657918; EXM36207.1; -; Genomic_DNA.
DR   EMBL; JH657918; EXM36208.1; -; Genomic_DNA.
DR   Proteomes; UP000030701; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18659; CD2_tandem; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 6.10.140.1440; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR025260; CHD1-like_C.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014010; REJ_dom.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF13907; CHD1-like_C; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01176; DUF4208; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51111; REJ; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000313|EMBL:EXM36208.1};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EXM36208.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          1..29
FT                   /note="REJ"
FT                   /evidence="ECO:0000259|PROSITE:PS51111"
FT   DOMAIN          265..336
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          364..424
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          462..633
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          765..926
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1048..1092
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1317..1501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..94
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1092
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1339..1431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1439..1501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1630 AA;  188245 MW;  435B32BD1E664E74 CRC64;
     MMSTPTLGGP SNGHLSPVDG ISMSFDTGDH ATDSDSHDAP DLTLDQPSPA SSDEANNDSN
     IAHDNTHMSA SEQSSEDNAS DDGDFDMEES LPSQNEDAME DRDSSTDSNR ASKRKAPVEE
     DEYIKANPEL YGLRRSTRPR EQRKIVESDD SDSEPPVNRR TVKRRRVESS RPSSKIGTPT
     LRASTADSDS DSDTYGGARA KSLQKKARMQ REAQPDLALA EKRWSSRRAA QVQQGAYEES
     DVDEDDDDDE LAPMAYTVDY IDDSPYIEKV VRHRLKDGFE ISYGLTKNDF EYFIKWQGKS
     HLHDTWETFQ DIRDYRGYRK VENYFRKVIE YEVDIRVGDD IPPETKEQFF LDRERDEEAF
     EDYTKVERVV AVRDGEDDTE YLVKWKGLTY EECTWEVASE ISDAFQDQID QYLDRASRSW
     QSDRKETNLD TRSRMVKLEE QPDFIKGGEL RNFQLRGLNF LCLNWTKGNN VILADEMGLG
     KTVQTVSFLS WLRNARRQEG PSLVVAPLSV IPAWCDTFNH WSPDINYVVY LGPEDARKII
     REHELLVDGN PKKPKFNVLV TSYEFILQDW QFLQSIKWQT LAVDEAHRLK NRESQLYNRL
     VSFGIPCKIL ITGTPIQNNL AELSALLDFL NPGKVDIDED LDSLSASDAQ EKLQQLHKAI
     APFILRRTKE TVESDLPPKT EKIIRVELSD VQLEYYKNIL TRNYTALCDA TNGHKNSLLN
     IMMELKKISN HPYMFPGAEE KVLAGSVRRE DQIKGLIASS GKMMLLDQLL SKLNKDGHRV
     LIFSQMVKML DILGDYCSLR GYKFQRLDGT IAAGPRRMAI NHFNADDSDD FCFLLSTRAG
     GLGINLMTAD TVIIFDSDWN PQADLQAMAR AHRIGQKRPV NIYRLVSKET VEEEVLERAR
     NKLLLEYLTI QAGVTDDGKA AFKEELNKKG LRVEGPSSSE DIQMVLKMRS SKMFEQSGNQ
     ERLEQLDIDS ILENAEVTKT KVDDKINLSS GGIDWDNFMQ ITDVKVDDIN LDWDQIIPAD
     KIAEIKAEEE KKQHEAYVAK VAAESAPRRA AIKSRHRESE RDVRLKKRQK EQQDKEEDDR
     RPVPLDPKRP LNDKEQRSLI KAYFRYGSMD DRGDEIIKEA KLKERDPDYV KSVLDEFIKA
     AKEAVDDNYA QMVEEEKRLG KTLTKKDRKA VLIDFGDLKK VNAETAIERP KQLQLLRQVI
     RSHNDWHTFR LPDATKAASY SCAWGAKEDA MLLVGIDRHG FGAWPQIRDD PDLDMADKLF
     LEEHRVEKKE ERSKGNDKMK APGAVHLVRR SEYLLSVLQA KHSNDRGVQR AVENHHRNNK
     KSLANGHRGS ATASPAPHNG KKSRDRDRDH LHGDLHRSRS HAEERGTPRP DFKRKHLSHE
     DSRSPKHRRI EEHRRSSKHG EDRERSEKRR HRDDEDRRDE RRDERRDDRR HDKHRLSHSH
     RDDRREDRRD DRRDDRRDDR RHDRHREDRE RDRERDRDRD RERERERAHD SHPQDERRAK
     ALRRLDELRR IGDNKDKRAE DNDAMIWFLL KPVRENFERI LSTTKDNVKS SKERASIFGV
     ELVVIGTFLD EKLAATAADE GLKSNFWDFL AALWPVDDTS KSVTGKRLSN MYRTLHSRSK
     GSGSTKTNGA
//
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