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Database: UniProt
Entry: A0A2C9JR32_BIOGL
LinkDB: A0A2C9JR32_BIOGL
Original site: A0A2C9JR32_BIOGL 
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
//
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