ID E2AMT3_CAMFO Unreviewed; 538 AA.
AC E2AMT3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Actin-related protein 8 {ECO:0000256|ARBA:ARBA00021608, ECO:0000256|RuleBase:RU364121};
GN ORFNames=EAG_11730 {ECO:0000313|EMBL:EFN65256.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN65256.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 EMBL; GL440893; EFN65256.1; -; Genomic_DNA.
DR AlphaFoldDB; E2AMT3; -.
DR STRING; 104421.E2AMT3; -.
DR InParanoid; E2AMT3; -.
DR OMA; AYKCMWA; -.
DR Proteomes; UP000000311; 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 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:UP000000311};
KW Transcription {ECO:0000256|RuleBase:RU364121};
KW Transcription regulation {ECO:0000256|RuleBase:RU364121}.
FT REGION 401..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 61178 MW; 99E697DDB4AA9E3E CRC64;
MPVYQEAEQI QAQTIIVIHP GSMYLRMGRA SDLKPVTLLH AVARRRLPSG IKYKDSFLPS
AVILTKELTQ AMEESRLQVS HTLQSCLQSD GCRRYATPPQ QIAAFNRRSI PEISSPCNMK
WTKTGHDIVV GDDILSLDPE EESNFNIHFP YKRGELNIHM GPGGSLKAIM ADLKTIWEYV
LTEKLDIPLR DLKHYRAVLV VPDIYHRSYL KELTTLLLDE IGFGRCILLQ DHVGALFGAG
LGYACVVDVG AQKISVSCVE DAISHKDTRV RMDYGSADVT QTFFWLLQKS AFPYKLCDPI
NKLDALLLDQ LKIDFCHVDL NVCGSQEKTF VIRKPKKQTE TYTLQVGDEC LIAPLSLFQP
ELFRITGIHN VHVQKRSLGD PEDPYDENYL RETSRRGMKE SLDHSSEIQE ETANIPTNAG
EDEVVVDTVN DNVPSLSNRD LEAPRDFVIP QQLLGLDQAI LQSIERCSNE DFKRKMYSCV
LVVGSGLKFK GIGTWLRNRI SLQTPYMYRP GKYLKKQLYD ILRNIYIVVF QKRKTFSF
//
