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Database: UniProt
Entry: K3W250_FUSPC
LinkDB: K3W250_FUSPC
Original site: K3W250_FUSPC 
ID   K3W250_FUSPC            Unreviewed;      1671 AA.
AC   K3W250;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=CHD1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FPSE_02679 {ECO:0000313|EMBL:EKJ77035.1};
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ77035.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ77035.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ77035.1,
RC   ECO:0000313|Proteomes:UP000007978};
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(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:EKJ77035.1}.
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DR   EMBL; AFNW01000063; EKJ77035.1; -; Genomic_DNA.
DR   RefSeq; XP_009254073.1; XM_009255798.1.
DR   EnsemblFungi; EKJ77035; EKJ77035; FPSE_02679.
DR   GeneID; 20361298; -.
DR   KEGG; fpu:FPSE_02679; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   HOGENOM; CLU_000315_29_2_1; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000007978; Chromosome 4.
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; 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; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007978};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          267..338
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          366..426
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          464..635
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          767..928
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1320..1497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1519..1540
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        100..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        1051..1091
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1671 AA;  193972 MW;  02F3327EC6DA34E5 CRC64;
     MMSTPTFGDP SNGHLSAGDE ISMSFDTGDH ATDSDSHDAP DHTLDPPSPT SSDDANHDSN
     MIQDDTHMSA SEQSSEDNAS DDGDFDMEGS ILSQNEDVIE DRASSTDSTR TSKRKAPVEE
     EDYIKANPEL YGLRRSTRPR EQRKIVESDD SDSEPPVNRR IVKRRRVETS RPSSKIGTPT
     LRASTADSDS DSDNYGGARA KSLQKKARMQ REAQPDLALA EKRWSSRRAA QIQQGAYEES
     DVDEDEEDDD DELGLVSYTV DYVDDSPYIE KVVRHRLKDG LELSYNSTKN DFEYFIKWQG
     KSHLHDTWET FDDIRGYRGH RKVENYFKKF VDYELAIRFG TDIPPETKEQ FFLDRERDEE
     AYEDYTKVER VVAVRDGDDG TEYLVKWKGL TYEECTWEIT SDISDAFQDQ IDQYLDRASR
     SWQSDRKETN PETRSRMVKL EEQPDFIKNG ELRNFQLRGL NFLCLNWTKG NNVILADEMG
     LGKTVQTVSF LSWLRNARHQ EGPSLVVAPL SVIPAWCDTF NHWSPDLNYV VYLGPEDARN
     IIREHELLVD GNPKKPKFNI LVTSYEFILQ DWQFLQSIKW QTLAVDEAHR LKNRESQLYN
     RLVNFGIPCK VLITGTPIQN NLAELSALLD FLNPGKVDID EDLDSLSAND AQEKLQQLHK
     AIAPYILRRT KETVESDLPP KTEKIIRVEL SDVQLDYYKN ILTRNYSALC DATNGHKNSL
     LNIMMELKKI SNHPYMFPGA EEKVLAGSVR REDQIKGLIA SSGKMMLLDQ LLSKLNKDGH
     RVLIFSQMVK MLDILGDYCS LRGYKFQRLD GTIAAGPRRM AINHFNADDS DDFCFLLSTR
     AGGLGINLMT ADTVIIFDSD WNPQADLQAM ARAHRIGQKR PVNIYRLVSK ETVEEEVLER
     ARNKLLLEYL TIQAGVTDDG KAAFKEELNK KGLRVEGPSS SEDIQMVLKM RSSKMFEQSG
     NQERLEQLDI DSILENAEIT KTKVDDKINL SSGGIDWDNF MQITDVKVDD INLDWDQIIP
     ADKLAEIKAE EEKKQHEAYV AKVAAESAPR RATIKNRHNE NDRADRLKKR QREQRDKEDD
     DNRRILLADP KRPLTDKEQR GLIKAYFRYG SMDDRGDEII KDAKLKERDQ DYVKSVLDEF
     IKAAKEAVDE NLAQMVEEEK RLGKTLTKKD RKAVLIDFGD LKKVNAETAI ERPKQLQLLR
     QAIRSHSDWH SFRLPDATKA ANYSCAWGAK EDAMLLIGID RHGFGAWPQI RDDPDLDMTE
     KLFLEEHRVE KKEERSKGND KMKAPGAVHL VRRSEYLLSV LQAKHSNDRG VQRAVENHHR
     NNKKSLANGH RGSATASPAP HNGKKHRDRD RDRDREHLHG DPHRSRGHAD ERGTPRPDYK
     RKHLSHEDSR SPKHRRIEEH RRTSKHGDDR DRSEKRRYRD DDDRRDDRRD DRRDDRRDDR
     RADKHRLSHN HRDDRRDDRR DDRRDDRRDD RRDDRRDDRR DDRRDDRRDD RRDDRRDDRR
     DERRDDRRDD RRLDRHREDR DRERERERAQ DSYPQDERRA KALRRLDELR RIGDNKDQRA
     QDNDAMIWFL LKPVRENFER ILSTTKDNVK SSKERANIFK VELVVIGTFL DEKLAATAAD
     EGLKSNFWDF LAALWPVDDT SKSVTGKRLS NMYRTLHSRD KEPGSAKTNG V
//
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