SWR1_USTMA
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 03-AUG-2022, entry version 108.
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., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., 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., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT 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., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic component of the SWR1 complex which mediates the
CC ATP-dependent exchange of histone H2A for the H2A variant HZT1 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; CM003157; KIS66492.1; -; Genomic_DNA.
DR RefSeq; XP_011391816.1; XM_011393514.1.
DR AlphaFoldDB; Q4P328; -.
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 VEuPathDB; FungiDB:UMAG_05485; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_3_1; -.
DR InParanoid; Q4P328; -.
DR OMA; RKKWQYM; -.
DR OrthoDB; 188211at2759; -.
DR Proteomes; UP000000561; Chromosome 18.
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; 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-rel_dom; 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; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1830
FT /note="Helicase SWR1"
FT /id="PRO_0000074373"
FT DOMAIN 556..628
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 1002..1167
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1537..1692
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1754..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 602..679
FT /evidence="ECO:0000255"
FT MOTIF 1118..1121
FT /note="DEAH box"
FT COMPBIAS 13..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..839
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1788..1808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1015..1022
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
