ID A0A2C9JR32_BIOGL Unreviewed; 602 AA.
AC A0A2C9JR32;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Actin-related protein 8 {ECO:0000256|ARBA:ARBA00021608, ECO:0000256|RuleBase:RU364121};
GN Name=106064396 {ECO:0000313|EnsemblMetazoa:BGLB006619-PB};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB006619-PB, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB006619-PB}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB006619-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR RefSeq; XP_013078405.1; XM_013222951.1.
DR AlphaFoldDB; A0A2C9JR32; -.
DR STRING; 6526.A0A2C9JR32; -.
DR EnsemblMetazoa; BGLB006619-RB; BGLB006619-PB; BGLB006619.
DR GeneID; 106064396; -.
DR KEGG; bgt:106064396; -.
DR VEuPathDB; VectorBase:BGLB006619; -.
DR OrthoDB; 11729at2759; -.
DR Proteomes; UP000076420; 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; 2.
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 Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364121};
KW Nucleus {ECO:0000256|RuleBase:RU364121};
KW Transcription {ECO:0000256|RuleBase:RU364121};
KW Transcription regulation {ECO:0000256|RuleBase:RU364121}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 67620 MW; 473BCD085C9AA15E CRC64;
MPSSVAKKPL FPPTPEPAAE QQTVQAPTVI VIQPGSVNLR IGRASDAFPI TVPHCVARKC
LDPSKRLADD YMLLRPECNH PEAGQQIRAG LASIEEMLLT RPTQTGEYRQ ITLPRQLMAF
NSQVPPETLK STESPTWTNI EKKPPYLVGD EALYIPSRES YRLSWPMRRG RLNIHDGPGG
SLTAVLADLE TIWGHVLQEH LEIPIKDLKH YRAVLLIPDV YVHKHVKVLV NLLLNTLGFA
AAIVHQESVC ATYGSGLTVA CVVDVGDQKT SVSCVEDGIS HRASRLTMEF GGSDVSRLFH
SLLARCGVAL PELNLTNPPD VIQMQGLKET CCHLNQDQYG ITQQCLEIHR PDNMLLKYKV
KLGDEPILAP MALFKPMAFG LLGDHLIRVQ SRFEGDPDDP HDEEYLRQTQ RQSWAGRMGS
SKKDTADMSR DTSEQNLSQL DDLNSGPLDD DSNDVPDVMT ATENKSTRRG DDEDDVEMDE
ENDLHLMGVD EAIIHSIEKC DSEELRRKLY SCVLVVGGGL QFEGAVRWLQ YQVWHSIPLT
MRQQLDNLEI ITKPKDMDAS CTSWKGGAIL ACLDSTQELW IRQREWKQFS VRLLRERVPF
IW
//