ID X0HU43_FUSOX Unreviewed; 1628 AA.
AC X0HU43;
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:EXL79987.1};
GN ORFNames=FOPG_06222 {ECO:0000313|EMBL:EXL79987.1};
OS Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL79987.1};
RN [1] {ECO:0000313|EMBL:EXL79987.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54008 {ECO:0000313|EMBL:EXL79987.1};
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 PHW808.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXL79987.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=54008 {ECO:0000313|EMBL:EXL79987.1};
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 PHW808.";
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; JH658830; EXL79987.1; -; Genomic_DNA.
DR EMBL; JH658830; EXL79988.1; -; Genomic_DNA.
DR EMBL; JH658830; EXL79989.1; -; Genomic_DNA.
DR Proteomes; UP000030676; 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:EXL79987.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EXL79987.1};
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..1499
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..1499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1628 AA; 187959 MW; 0198C3B5823D6F7D 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 RDRDRDRDRE RERERAHDSH PQDERRAKAL
RRLDELRRIG DNKDKRAEDN DAMIWFLLKP VRENFERILS TTKDNVKSSK ERASIFGVEL
VVIGTFLDEK LAATAADEGL KSNFWDFLAA LWPVDDTSKS VTGKRLSNMY RTLHSRSKGS
GSTKTNGA
//