GenomeNet

Database: UniProt
Entry: Q7S133
LinkDB: Q7S133
Original site: Q7S133 
ID   SWR1_NEUCR              Reviewed;        1845 AA.
AC   Q7S133;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   31-JUL-2019, entry version 110.
DE   RecName: Full=Helicase swr-1;
DE            EC=3.6.4.12;
DE   AltName: Full=Chromatin remodeling factor 1-1;
GN   Name=crf1-1; Synonyms=swr1; ORFNames=NCU09993;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Catalytic component of the SWR1 complex which mediates
CC       the ATP-dependent exchange of histone H2A for the H2A variant
CC       H2A.Z leading to transcriptional regulation of selected genes by
CC       chromatin remodeling. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00549}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1
CC       subfamily. {ECO:0000305}.
DR   EMBL; CM002242; EAA29066.1; -; Genomic_DNA.
DR   RefSeq; XP_958302.1; XM_953209.2.
DR   SMR; Q7S133; -.
DR   EnsemblFungi; EAA29066; EAA29066; NCU09993.
DR   GeneID; 3874449; -.
DR   KEGG; ncr:NCU09993; -.
DR   EuPathDB; FungiDB:NCU09993; -.
DR   HOGENOM; HOG000186095; -.
DR   InParanoid; Q7S133; -.
DR   KO; K11681; -.
DR   OMA; RQGWNND; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0016458; P:gene silencing; IBA:GO_Central.
DR   GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Chromatin regulator; Complete proteome;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1   1845       Helicase swr-1.
FT                                /FTId=PRO_0000074371.
FT   DOMAIN      418    493       HSA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00549}.
FT   DOMAIN      957   1122       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1510   1660       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     970    977       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF      1073   1076       DEAH box.
FT   COMPBIAS      2     51       Thr-rich.
FT   COMPBIAS    246    292       Pro-rich.
SQ   SEQUENCE   1845 AA;  206953 MW;  4E19DC989ACFEE39 CRC64;
     MTTMMTDSGT ASDSGAGLVD STRNDTTTTT TTTTTPGDND ADDDNTNGTT TGHHDNNETD
     NNSKSYSSTH HVPAIDNTST TNANDNEDAA GFLDRDQSPL SSISSPLSEP DNFEFDTEPI
     PSILSPKSTT SDNHARDGET PELDEDGQPP AKRRRVRETT PHNHSRKPKP ESPPWKKFEA
     EGPTTIITED GRRKSGRVNP VLLGMKPSDK KVTRKAIQTS PVSNKSSAST SRKPAPASSS
     NSKHAPAKMP PPPPPPKAPA RKSATTHETR PSASRSRRRS PSPRRPATPP KPAAVGTRRS
     TRQALAHSRA SYDDGQLSPG ASRATPRIKL KVRPPLTVIP LVHPNQANVR PKLGPTFEEY
     FARAHEIPVE EGGQHIPDEE PKYTDEMALQ DAKVILRVEK EVEPGGLLAP DRCSAFEPEA
     EEEPPRQWAH LDHLTKAMTN FRKLMYREQQ LHMQAAKRIA IACEAEWRRR NPQPKTAEEI
     ELEEMEASKA KWRQVIRAFA GTWENVRVEV NRRRLVEWEA EEQRRVKAAL NQAVNLSEQK
     LQQRQAQVDG DEITDEDEDE DDEDLASGMP SVMGDEKESD EHSDQGSDEM SDENDEDEDE
     DNMSSSEDDD KKSTASDEGL TQEELRAKYA NLPTLGTTDE TEETTKDVEM ADAPAAMDGS
     VANDDDTSDE SVDMDDDLGS SEESDDDEEE EEDDEEEEES DDEPAGLLGL FFGKSELKKL
     KEEAVTEEPS VEPAGDVEMT DASAALRPEL QVNGHAHEAP ITNGTHTNEQ LASSQTEGAD
     DEVSLLVIPN DEIAAENTQT AAEPGSGVVE KDFLTNDSSL KYPNEIVQSE NQTLPAKESV
     EAGGDLPMVD APSTDDLQRE TAAAPSLEAP PNTRHDSQET VAATDMQSQS QTQSPKTTDT
     KPTDVDTPHS ELAVSVQKPD SRQSSPQPTT PTVKTEIPFL LRGTLREYQH HGLDWLAGLY
     ANNTNGILAD EMGLGKTIQT IALLAHLACH HEVWGPHLVI VPTSVMLNWE MEFKKWCPGF
     KILTYYGNQE ERKRKRQGWN NDDVWNVCIT SYQMVLQDQQ VFRRRRWHYM ILDEAHNIKN
     FKSQRWQTLL GFNTQARLLL TGTPLQNNLT ELWSLLYFLA PPENGEGGFV DLTEFHNWFA
     RPESQILESG REQLDDEARA IIAKLHKVLR PYLLRRLKAD VEKQMPAKYE HVEFCRLSKR
     QRELYDGFLS RADTRETLQS GNYMSIINCL MQLRKVCNHP DLFVDRPIMT SFRMSRSVPA
     DYEWKEKFIR NRLLATKPMT TVNLSFLNMI PTEYEDLSKT HTDRIAQLSS HRILLDLREA
     QKVRANNAYT ALDPSSVKSN LVYLESAARW GRFEELQHCV YINALRRQQR PIYGKRLTEF
     LTLDTHLRPY KPRPRVPAKI MSWFEEDSFL LHNAIPTLQQ RAESMEMTIT KFACVTPAVV
     TGPEMNRFLL GERGIQLFED LDLKLSAPVK YAPYMPPQPP PDPWHEARMR LTIQFPDKRL
     LQYDCGKLQA LDKLLRKLQA GGHRALIFTQ MTKVLDILEQ FLNIHGHKYL RLDGATKVEQ
     RQILTDRFNH DPRILCFILS TRSGGLGINL TGADTVIFYD QDWNPAMDKQ CQDRCHRIGQ
     TRDVHIYRLV SEHTIEANIL RKASQKQMLD DVVIQEGEFT TDYFNRLSVR DVLGSNGEVI
     ASNEDDVAAN LAMDRVLGGP STTGAGGYDG TADGGGGASQ PPVRNVGRVL EMAEDREDVD
     AAKAAEKEIM QDEADFGEAG STRPGTPGDG LADLDGQLLG GEENKEVEDE VIEYNAWGER
     MHTIDEYMLG FMAKALEGTP LELPRDRKKG RDRNRNRKGK DSRKR
//
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