SWR1_NEUCR
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 03-AUG-2022, entry version 122.
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 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; 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., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., 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., Paulsen I.,
RA 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 the
CC ATP-dependent exchange of histone H2A for the H2A variant H2A.Z leading
CC to transcriptional regulation of selected genes by chromatin
CC 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-ProRule:PRU00549}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CM002242; EAA29066.1; -; Genomic_DNA.
DR RefSeq; XP_958302.1; XM_953209.2.
DR AlphaFoldDB; Q7S133; -.
DR SMR; Q7S133; -.
DR STRING; 5141.EFNCRP00000009765; -.
DR PRIDE; Q7S133; -.
DR EnsemblFungi; EAA29066; EAA29066; NCU09993.
DR GeneID; 3874449; -.
DR KEGG; ncr:NCU09993; -.
DR VEuPathDB; FungiDB:NCU09993; -.
DR HOGENOM; CLU_000315_24_0_1; -.
DR InParanoid; Q7S133; -.
DR OMA; ERCLYFE; -.
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:ATP hydrolysis activity; IBA:GO_Central.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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-rel_dom; 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; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1845
FT /note="Helicase swr-1"
FT /id="PRO_0000074371"
FT DOMAIN 418..493
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 957..1122
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1510..1660
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1816..1845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1073..1076
FT /note="DEAH box"
FT COMPBIAS 1..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..605
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..704
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1845
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 970..977
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
