ID A0A3S4RKX6_9ACAR Unreviewed; 569 AA.
AC A0A3S4RKX6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Actin-related protein 8 {ECO:0000256|ARBA:ARBA00021608, ECO:0000256|RuleBase:RU364121};
GN ORFNames=B4U79_00492 {ECO:0000313|EMBL:RWS17459.1}, B4U79_09203
GN {ECO:0000313|EMBL:RWS17454.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS17454.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS17454.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS17454.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:RWS17454.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS17454.1};
RA Dong X.;
RT "Trombidioid mite genomics.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the functional organization of
CC mitotic chromosomes. Exhibits low basal ATPase activity, and unable to
CC polymerize. {ECO:0000256|ARBA:ARBA00025560,
CC ECO:0000256|RuleBase:RU364121}.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. {ECO:0000256|RuleBase:RU364121}.
CC -!- SUBUNIT: Component of the chromatin remodeling Ino80 complex. Exists as
CC monomers and dimers, but the dimer is most probably the biologically
CC relevant form required for stable interactions with histones that
CC exploits the twofold symmetry of the nucleosome core.
CC {ECO:0000256|RuleBase:RU364121}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364121}.
CC -!- SIMILARITY: Belongs to the actin family. ARP8 subfamily.
CC {ECO:0000256|ARBA:ARBA00007720, ECO:0000256|RuleBase:RU364121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS17454.1}.
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DR EMBL; NCKU01000072; RWS17454.1; -; Genomic_DNA.
DR EMBL; NCKU01000071; RWS17459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4RKX6; -.
DR STRING; 1965070.A0A3S4RKX6; -.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF13; ACTIN-RELATED PROTEIN 8; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364121};
KW DNA damage {ECO:0000256|RuleBase:RU364121};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU364121}; DNA repair {ECO:0000256|RuleBase:RU364121};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364121};
KW Nucleus {ECO:0000256|RuleBase:RU364121};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW Transcription {ECO:0000256|RuleBase:RU364121};
KW Transcription regulation {ECO:0000256|RuleBase:RU364121}.
SQ SEQUENCE 569 AA; 63494 MW; 13F41F52D7711533 CRC64;
MNGSGANASC LSTDANSASN VIVINPGSLY LKIGRASDSV PLIVPQVIAR RNKSKNNAFP
CLEDPFLVSA VKLDKETNKQ LCDVQHSVLN VLSSCLTSSG YSRNSTSKEK LSEFNKKVKP
VVLPKSSQTI RCWTCVENKP DVLIGEDALY LKPSEPYHVR WPIRRGQLNV HSGIGGSINS
IISDLERIWA YFIETKLNIN LKTLSNFKAV LTIPDVYNRN HVKELISMVL NGLGFGSCFI
HHEAVFATFG AGLSSATVID VGDQKTSVCC VEDGFSPRCT RITLEYGGSD ITQVFHYLLK
QRNFPYTECK SESRVGGLLL QELKENFCHL DINVCGVRER QFQVKIPEQP VLQYNILLGD
ECLVAPLALF HPELFAVTGN NKKIRTLSRN EGDSEDPFDE NYLIQTKRKY GETTEASGGN
ENLNNPNDQL CDEDLETCEV PVSGPDKEIK CDQLLGIDQA VMQCIDRCDN DDTKRRMYNC
VLVVGGGINF KGIDTWLQSR LSVQIPLQYR TGQCVDIITN PKDIDPRCVV WKGAAVMSLL
DTTQELWITK NEWENVGVRI VREKAPFVW
//
