(data stored in ACNUC8465 zone)

SWISSPROT: SWR1_CANGA

ID   SWR1_CANGA              Reviewed;        1450 AA.
AC   Q6FK48;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 95.
DE   RecName: Full=Helicase SWR1;
DE            EC=3.6.4.12;
GN   Name=SWR1; OrderedLocusNames=CAGL0M01188g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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: ATP + H(2)O = ADP + phosphate.
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; CR380959; CAG62372.1; -; Genomic_DNA.
DR   RefSeq; XP_449396.1; XM_449396.1.
DR   ProteinModelPortal; Q6FK48; -.
DR   SMR; Q6FK48; -.
DR   STRING; 284593.XP_449396.1; -.
DR   PRIDE; Q6FK48; -.
DR   EnsemblFungi; CAG62372; CAG62372; CAGL0M01188g.
DR   KEGG; cgr:CAGL0M01188g; -.
DR   CGD; CAL0137511; CAGL0M01188g.
DR   EuPathDB; FungiDB:CAGL0M01188g; -.
DR   eggNOG; KOG0388; Eukaryota.
DR   eggNOG; KOG0391; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   HOGENOM; HOG000186095; -.
DR   InParanoid; Q6FK48; -.
DR   KO; K11681; -.
DR   OMA; YFLMPSS; -.
DR   OrthoDB; EOG092C1YH4; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000812; C:Swr1 complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:EnsemblFungi.
DR   GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
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; 3.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK48.
DR   SWISS-2DPAGE; Q6FK48.
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   1450       Helicase SWR1.
FT                                /FTId=PRO_0000074365.
FT   DOMAIN      344    417       HSA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00549}.
FT   DOMAIN      640    805       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1179   1332       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     653    700       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       756    759       DEAH box.
SQ   SEQUENCE   1450 AA;  167290 MW;  120C95082280BBED CRC64;
     MSKNNKLNGK DNRQSKIEKL SELKLRHDQL TNELYHLHEY ISLVEYDPFY IPNSENYERL
     LEEKDVTWGS IFQEKKQLHN ESSGKKVRRS VRHLRDSGSS TINELDTMSE NDINLLKEVD
     ILAKQKLQDL KLQFSNSHIK KKGNTKRAKI VKQVPNHQDK SESPQISERD VKTVVKDLKP
     NHRGSEIKPE IMESSDVKNE IENCDFNEKQ LKLYKDDDIA SESDFYFTTS SEDELPNKRR
     GTIKRRKRIN LYVNPPKAVI TNPDNIANSH YPTLHEYLDS FKILEDDMTN EEYNTFIKEQ
     QRFAKMIKKG IETGALKYDP VTETVQPSAR KVPNMFSHAK VDPIQYMYKE QNLHIHQEHL
     INQGLFSSKL VQNRKKQRIA GAKKIAQMIE QHFKHIAGAE DRRLKENEKQ RKAIARNIIQ
     SVKKRWNLAE KAYRILKKDE EEQLKRIQGK EHLSKMLEKS SKLLGAQLKQ HPNEDDIENS
     TSDDFSSTGD SDNLSSSSDE ESDDEINDLS EDQKNNINEL KTSSTSAFSS PEISSPSKNP
     DLGLNSLLTN DFENESNSSD TNEEFIMGDS DTSHSDDENL TDDSEDSNDG EHDTTSDNEK
     SDLFPADTTN DPLAVQDVPT PSLLRGTLRT YQKQGLNWLA SLYNNNTNGI LADEMGLGKT
     IQTISLLSYL ACEKHNWGPH LIVVPTSVLL NWEMEFKRFA PGFKVLTYYG NPQQRKEKRK
     GWNKPDAFHV CIVSYQLIVQ DQHSFKRKKW QYMVLDEAHN IKNFRSTRWQ ALLNFNTQRR
     ILLTGTPLQN NIAELWSLLY FLMPQTVIDG QKVSGFADLD AFQQWFGRPV DKLIETGGTY
     EQDNETKRTV EKLHQVLRPY LLRRLKADVE KQIPGKYEHI VYCKLSKRQR FLYDDFMSRA
     QTKATLASGN FMSIVNCLMQ LRKVCNHPDL FEVRPIKTSF LFGESVIARY SERANSITRR
     IHFHDKDTLV DLQNINLQFT NNDLEKTSYH TNTINKLACI NEFVEEVQKL RKQNAEEERQ
     KSRHLKINTQ NISNFYEEFM QQKLDEQENK INFIGYLNSQ RCSRKTVYGM NLIRLLEMPH
     VSNNCIDDPN YDDLIKPLQT RLLDGRTTIE KFAVLTPGAV TSNIGELTLG MDEFVTPNSK
     SGIIPYEELV QLDNPFHQVQ TKLTIAFPDK SLLQYDCGKL QKLAILLQQL KDGGHRALIF
     TQMTKVLDIL EQFLNYHGYL YMRLDGATKI EDRQILTERF NSDPKITVFI LSSRSGGLGI
     NLTGADTVIF YDSDWNPAMD KQCQDRCHRI GQTRDVHIYR FVSEHTIESN ILKKANQKRQ
     LDDVIIQKGE FTTDYFSKLS VKDLFGSDVV GDLPVIDTKP LLGSDSEAIK DPKKLEKLLA
     QAEDEDDVKA ANSALREVNV DDEDFDESST NKTGGNILNG DDIDEDVDEY EGTNHVEEYM
     LRFIANGFYF
//

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