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Database: UniProt
Entry: N1JEA7_BLUG1
LinkDB: N1JEA7_BLUG1
Original site: N1JEA7_BLUG1 
ID   N1JEA7_BLUG1            Unreviewed;      1134 AA.
AC   N1JEA7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   28-JUN-2023, entry version 52.
DE   SubName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0000313|EMBL:CCU81578.1};
GN   ORFNames=BGHDH14_bgh05263 {ECO:0000313|EMBL:CCU81578.1};
OS   Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS   (Oidium monilioides f. sp. hordei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX   NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU81578.1, ECO:0000313|Proteomes:UP000015441};
RN   [1] {ECO:0000313|EMBL:CCU81578.1, ECO:0000313|Proteomes:UP000015441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH14 {ECO:0000313|EMBL:CCU81578.1};
RX   PubMed=21148392; DOI=10.1126/science.1194573;
RA   Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA   Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA   Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA   Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA   Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA   Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA   Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA   Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA   Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA   Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA   Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA   Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT   "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT   extreme parasitism.";
RL   Science 330:1543-1546(2010).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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:CCU81578.1}.
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DR   EMBL; CAUH01005186; CCU81578.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1JEA7; -.
DR   STRING; 546991.N1JEA7; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_0_1; -.
DR   InParanoid; N1JEA7; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000015441; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR044754; Isw1/2_DEXHc.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000015441}.
FT   DOMAIN          194..359
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          490..641
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          857..909
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1067
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1095..1124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1134 AA;  130393 MW;  260FD4D9EF88B162 CRC64;
     MAPARSSRTR AAEFADNKSQ DSKIPVSNVS TEVGSAEPLD TDENIDPLDE SDAEVKSNKS
     SSATEQNLRE DIRKKRSEAT QLRRNDSIRR FRYLLGLTDL FRHFIETNPN PRVKEIITEI
     DRRNAETEKT NKGRDRQGGA AAERRRRTEA EEDAELLKDD NIGCSAETVF RDSPRFIQGG
     QMRDYQVAGL NWLISLHENG ISGILADEMG LGKTLQTISF LGYLRHIMHT SGPHLVIVPK
     STLDNWKREF GKWTPEVNVL VLQGAKEERQ NLISERLIDE DFDVCITSYE IILREKSHLR
     KLAWEYIIID EAHRIKNEES SLAQVIRLFD SRNRLLITGT PLQNNLHELW ALLNFILPDV
     FGDSEAFDQW FSGQSGDQDT VVKQLHRVLR PFLLRRVKSD VEKSLLPKKE INLYIGMSDM
     QVKWYKKILE KDIDAVNGAG GKRESKTRLL NIVMQLRKCC NHPYLFEGAE PGPPYTTDEH
     LIYNAGKMAM LDRLLIRLKK QGSRVLIFSQ MSRLLDILED YCVFRDFKYC RIDGSTAHED
     RIAAIDDYNK NDSEKFVFLL TTRAGGLGIN LTSADIVVLF DSDWNPQADL QAMDRAHRIG
     QKKQVIVYRL VTENAIEEKV LERAAQKLRL DQLVIQQGRA QTAAKAAANK DELLSMIQHG
     AEKVFNTKTA TGILAEKGSE LNDDDIDDIL KHGEQRTAEL NARYEKLGID DLQNFASESA
     YEWNGQDFTS RKKEINISWI NPAKRERKEQ SYSMDKYYKQ ALSTGGRTAD TKPKAPRAPK
     QVTVHDYQFF PGTLRDLQDR ETAHHRKEIG YKVPLPDGPE DELSNREAER ALDQAEIDNA
     TPLTEEEQEE KQRLSQMGFA DWNRRDFQQF INGSAKYGRK SYSAIAEEVD HKNEQEIKQY
     AKVFWSRYTE VADYSKYIGL IEAGEEKLRK VDHQRKMLRK KMAQYRVPLQ QLKVNYSVST
     TNKKVYTEEE DRFLLVSLDK YGVDSEGIHE RIRDDIRNSP LFRFDWFFLS RTPVEISRRC
     TTLLTTVARE FEESTSTKTL NSNASGKHKR EIEDDANDED SKRSTGPAKK KAKNSMKVVL
     NHFFRRNLES ANLRQKKVLE NSKVTRGNRN SIERSSQAAN GVSNRKGRTR GRKK
//
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