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Database: UniProt
Entry: Q5ARK3
LinkDB: Q5ARK3
Original site: Q5ARK3 
ID   SWR1_EMENI              Reviewed;        1698 AA.
AC   Q5ARK3; C8VH70;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   31-JUL-2019, entry version 96.
DE   RecName: Full=Helicase swr1;
DE            EC=3.6.4.12;
GN   Name=swr1; ORFNames=AN9077;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Catalytic component of the SWR1 complex which mediates
CC       the ATP-dependent exchange of histone H2A for the H2A variant HZT1
CC       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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA61910.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AACD01000169; EAA61910.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; CBF82596.1; -; Genomic_DNA.
DR   RefSeq; XP_682346.1; XM_677254.1.
DR   SMR; Q5ARK3; -.
DR   STRING; 162425.CADANIAP00009538; -.
DR   PRIDE; Q5ARK3; -.
DR   EnsemblFungi; CBF82596; CBF82596; ANIA_09077.
DR   EnsemblFungi; EAA61910; EAA61910; AN9077.2.
DR   GeneID; 2868023; -.
DR   KEGG; ani:AN9077.2; -.
DR   HOGENOM; HOG000186095; -.
DR   InParanoid; Q5ARK3; -.
DR   KO; K11681; -.
DR   OMA; RQGWNND; -.
DR   OrthoDB; 188211at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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; PF07529; HSA; 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   1698       Helicase swr1.
FT                                /FTId=PRO_0000074368.
FT   DOMAIN      329    403       HSA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00549}.
FT   DOMAIN      837   1002       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1377   1527       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     850    857       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       953    956       DEAH box.
FT   COMPBIAS    470    609       Asp-rich.
SQ   SEQUENCE   1698 AA;  190547 MW;  FB023CCEF1AADA9D CRC64;
     MQNGTTIGIP PENERVTERA EPVPSDLLPN NSPVNSPTID PTLSEIKDVA ADHNEEPPSK
     RRKVAGSTPS RRSHSRAASP PWKKAGADGP TSKIVDGKRR STRVSNVGPV EQPPSDAKPT
     RSSQKQYVSK AVSSQRNAAV SSPLPMSPSR SGINRRSLAG VAVNGSPSTT AKGSIGRRRR
     ESPSPVSKRA STRTRPDNMD AYHPSNGVTP RSNSTKTRST RSFQLASSDF REETADDIGN
     DGQDEHGQRI QRLRIKVKKP ALSIQHPSHV LPTRKYGSFK EWLENEGTGP GRMLTMTDAL
     EEAQKRRQVT EAMEPGGLLS SEVCSAFLPE PQEELPQQFS HQDHLVAHAL YFKKLLDKEH
     RAHRQAAKSL AAACAEVWRK RNKDPEDILR EQQEEMRGKR KQLAKDLKKM FELARAEIDR
     VRLARWEEEQ KAKDQRALDR AIKQSTMLFE KRRLEILGET GSDAPETTTD DEEVETDNGS
     ENDDEEGESN MSTETEEEDG DDRDDDVGLT AEELRLKYAN LPDTNPHPDQ SPYSDEDSED
     SDDIAADNTP GDTSGGVNRS PPPDSSGQVE LDEVDPVLID DSDESTDMDD DMGDSDDDGY
     SEAESDDEDG GEPGLLGFFS AKDLSLSNLH QTNSGEGDTH QTGADGDRNE DSSFDESEFG
     SEDPDEVTLV PTGPTNKDLS TPATVTASAE LEPAAMTPSI DQTSTEEPIA IGTETPIETV
     AEDAAALADT EPVDVDVLDT STNDSVPPVM SPATNLLKQI ERQQHEPYHS RAASSEASPG
     TVATKPSEPE SVSSIEAPAE KHAQPSESPG PGLKTPIPHL LRGTLREYQH FGLDWLAGLY
     SNHINGILAD EMGLGKTIQT IALLAHLAVE HGVWGPHLVV VPTSVILNWE MEFKKWCPGF
     KIMTYYGNQE ERRQKRRGWM DDNSWNVLIT SYQLVLQDQQ VLKRRSWHYM ILDEAHNIKN
     FRSQRWQALL TFRTRARLLL TGTPLQNNLT ELWSLLFFLM PTDGDEAGIE GFADLRNFSE
     WFRRPVEQIL EHGRETMDDE AKQVVTKLHT VLRPYILRRL KADVEKQMPG KYEHVVYCRL
     SKRQRYLYDG FMSRAQTKET LASGNYLSII NCLMQLRKVC NHPDLFETRP ISTSFAMPRS
     VATEFETSEA LVRRRLLYQH PLEKLDLDFL NLVPISREDI SRRLADDSAR IMAYAPFNTL
     RERQYHRTNW EMKFNGSTVQ STLEALENDC RKRRMAELER SLYFESKRHG RRPVYGSSLI
     EFLTADSKQR PTAHGPLRKR SYADWLSSQS SVLASMMMSL EERSQAMDGY IQRFACVTPA
     AVAAGVTEAA LTPISTRHLT NKERFPPHDP FHEAQMRLSI AFPDKRLLQY DCGKLQRLDK
     LLRDLKAGGH RALIFTQMTK MLDVLEQFLN IHGHRYLRLD GTTKVEQRQI LTDRFNNDNR
     ILAFILSSRS GGLGINLTGA DTVIFYDLDW NPAMDKQCQD RCHRIGQTRD VHIYRFVSEY
     TIESNILRKA NQKRMLDDVV IQEGEFTTDY FTKLDVRDMI GNDEALKDEA SAAMDRVLEN
     RVTNTSRVFE QAEDKEDIDA AKNAQKELEH ADDGDFDDRA NANASGVTAA SASASGAGQT
     PTQAGTPLPD EAQQSLNANN AEVAEDTADS DPSVGHIDDY LLRFMEWNMK DEPLVLPVDK
     SMKKSKKGKE HRLRKRRR
//
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