GenomeNet

Database: UniProt
Entry: Q4P328
LinkDB: Q4P328
Original site: Q4P328 
ID   SWR1_USTMA              Reviewed;        1830 AA.
AC   Q4P328; A0A0D1BX16;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   31-JUL-2019, entry version 96.
DE   RecName: Full=Helicase SWR1;
DE            EC=3.6.4.12;
GN   Name=SWR1; ORFNames=UMAG_05485;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G.,
RA   Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CM003157; KIS66492.1; -; Genomic_DNA.
DR   RefSeq; XP_011391816.1; XM_011393514.1.
DR   SMR; Q4P328; -.
DR   STRING; 5270.UM05485P0; -.
DR   PRIDE; Q4P328; -.
DR   EnsemblFungi; KIS66492; KIS66492; UMAG_05485.
DR   GeneID; 23565365; -.
DR   KEGG; uma:UMAG_05485; -.
DR   EuPathDB; FungiDB:UMAG_05485; -.
DR   InParanoid; Q4P328; -.
DR   KO; K11681; -.
DR   OMA; NKPDAFH; -.
DR   OrthoDB; 188211at2759; -.
DR   Proteomes; UP000000561; Chromosome 18.
DR   Proteomes; UP000000561; 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; 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   SMART; SM00573; HSA; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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; Coiled coil;
KW   Complete proteome; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1830       Helicase SWR1.
FT                                /FTId=PRO_0000074373.
FT   DOMAIN      556    628       HSA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00549}.
FT   DOMAIN     1002   1167       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1537   1692       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND    1015   1022       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED      602    679       {ECO:0000255}.
FT   MOTIF      1118   1121       DEAH box.
FT   COMPBIAS    687    719       Asp-rich.
SQ   SEQUENCE   1830 AA;  206325 MW;  2FECC06A81803356 CRC64;
     MSPGDSALDY AKRQAGNVSS QAPSRPSSEN DANGTVSTSN EHPSNEAGPS RPRSMGSERS
     ASPQQGTTPK VPTKRRRLNA ELAFSSPGPA FQVEQHGSEA QSDSNDSSGR ARRPRRSTTL
     TKSGSNESQD RRSSAHIPKR KEEAGESRNL AESVPKNKLK LNNGKARASD EVELRESSLS
     LVLPSRSRSR SKSVVKLEPD QDSAFPQEVA TPTLQPTRPK PQITPLTALN PQAALSEILA
     RRRSERIALA QSDLEDVHDG HDMLVRELFH LTKFVTMVGY DPDVARTDQS DVFTTFKHAH
     DLRFSLDDSG SGAEASTAAR VTRRRVNARL ESLSLKRPDP PSTPSTPSFS KVKVDDDKKS
     APEGRRNRRF SSVTGAQPRV NGAHTLETGH SDDTDDSSEE EDSEGSDLDA YSPDGREKGD
     AKDYNASRKG DAKRARLSST PHKRHRAKVQ DASSNAPVKR TGPRKSKALD ELDAFILRQQ
     PRPLPDHPPP LHILAPHQIP AHRRFGGDLD ALYESFNMLQ DDEGGLEDDD LETYIKLDQR
     WRAGLPIHPE AGSTTRHAVQ KVPRNKSHHD HLLESVTSSY SQMRQYAKLK QQNSRKVARM
     IAQHWERQLG TSEREKKAEE RRLRALAKWT LREVLKQWRL AVNVVRARKA AAEKAEKEKS
     DKEQLNAILE QSTAMLKKQH EVMTRADSLD DSDDEGSDRT NYGSDGSAES EISDIDDDDN
     QLIQIQDELP SVSPEQSLDM LTPVPEEADG SKDRVSNTTD HEAATANGDP TVVVESESQP
     SRRPQRRTAR TKTFKARDSK LDADDIEFND AGNDDEQEDA ELERQMLEED EEDDSEDAGL
     AADANIPIEE LLKRYGYGQE ADQDAEDSDA GEDAVSNDDS LENSATKDGS EDVAAVASIK
     IQEDAEVEEE RPVQEDSMPD EAMDLEDDAV STALNRPSDA LLVDDHSDAE SAATSGRRSS
     RRSMTRASSI VSSDRHATRL RQPFLLRGQL RPYQQIGFEW LCSLYANGVN GILADEMGLG
     KTIQTISLLA HLACDKGVWG PHLVVAPTSV MLNWEVEFKK FLPGFKILSY YGNQKERKEK
     RIGWNTENSF NVCITSYQLV LADQHIFRRK PWVYLVLDEA HHIKNFRSQR WQTLLGFNSQ
     RRLLLTGTPL QNNLMDLWSL MYFLMPNGAT ELPGGGAFAN MKDFQDWFSN PLDKAIEGGT
     SMNDETRAMV QKLHAVLRPY LLRRLKSEVE KELPSKYEHV ITCRLSKRQR FLYNDFMSRA
     KTRESLASGN YLSIINCLMQ LRKVCNHPDL FEVRPIVTSF AMSRSVVADY EIKDLLVRRR
     LLQENVWEKV DLDVTNLRIT DGEEHLTAIE SRDLRRLNAA KKLPHFREAV PEPRELDTWT
     LEGFERSREQ RKLVDRMEKW KHMAYLNQYR CTKRPIYGSG LIKMLTEAGE AARLEPLEQH
     ESDRRGFLTR CDSVLRIVQS RSTRRENMQA LIDRFAFVTP RAVAVDMPRW ALPGLEAHQR
     PDMVKREFDT VHPVAVKLHI AFPDASLLQY DCGKLQQLDI LMRRLKEGGH RILIFTQMTR
     VLDILESFLN YHGYRYLRLD GATKVESRQA LTEQFNRDAR ISAFILSTRS GGLGINLTGA
     DTVLFYDLDW NAAIEAQCMD RAHRIGQTRD VHIYRFVTEH TIEENMLRKA NQKRLLDNVV
     IQQGEFNTET LAKRLDWTDM LDESGKIGDV EVVVADQGVG ARDVESAFLQ AEDDEDRQAA
     LRARHEMFID DADFEEHQPS TSRPNTASAT PLAHTASDGA RPDNGAHAAD ALDAHEIENE
     HQEQEQEQEQ AASIDDYMLA FVESDWPFFA
//
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