ID   ARP6_DEBHA              Reviewed;         409 AA.
AC   Q6BML9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Actin-like protein ARP6;
GN   Name=ARP6; OrderedLocusNames=DEHA2F04268g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC       dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC       transcriptional regulation of selected genes by chromatin remodeling.
CC       Involved in chromosome stability (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SWR1 chromatin remodeling complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP6 subfamily. {ECO:0000305}.
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DR   EMBL; CR382138; CAG88868.2; -; Genomic_DNA.
DR   RefSeq; XP_460552.2; XM_460552.1.
DR   AlphaFoldDB; Q6BML9; -.
DR   SMR; Q6BML9; -.
DR   STRING; 4959.XP_460552.2; -.
DR   EnsemblFungi; CAG88868; CAG88868; DEHA2F04268g.
DR   GeneID; 2903208; -.
DR   KEGG; dha:DEHA2F04268g; -.
DR   VEuPathDB; FungiDB:DEHA2F04268g; -.
DR   eggNOG; KOG0680; Eukaryota.
DR   HOGENOM; CLU_027965_1_1_1; -.
DR   InParanoid; Q6BML9; -.
DR   OMA; FFEEYEC; -.
DR   OrthoDB; 649708at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR030054; Arp6.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF47; PTHR11937:SF47; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Cytoplasm; Cytoskeleton; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..409
FT                   /note="Actin-like protein ARP6"
FT                   /id="PRO_0000089115"
SQ   SEQUENCE   409 AA;  46452 MW;  C3515C25CE4BDBDB CRC64;
     MSQQYFVIDN GSYNIKAGFS NQDAPIKHQN ALSKARDGLI YVGNEYLVQT NNYSGMIFKR
     PYDHGHLISW ETEKAVWDYT FNKASPNQEL DASITHLTLT ETPFQLPQLS MNTDQIVFEE
     YGFNEYYRCA PASLVPWSNL GSSESKNNDF TLVVDSGYSG TWIVPIIYQN VYWKGVKKLP
     IGGAALNGLL REIISFRHYD IADEPVLINT IKEKTCFMAT DFEKSLANRK KYRCEFILPD
     FKTTTTGFVK TKDTPIDTTG DVQSLALIDE RFTIPESFYH PEIIFDNTTS STSTIQNASF
     KNITDLVVEC IMSCPKVTQP LLSGNIITVG GNTNLPGFTD RLRHELVKEL PIDWHVQVKE
     TEHNPDEASW FGGAQLTNDE IINNISISKK DYFEHGSNWC QKQFGFKNL