ID A0A0W0G785_9AGAR Unreviewed; 549 AA.
AC A0A0W0G785;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=Actin-related protein 8 {ECO:0000256|RuleBase:RU364121};
GN ORFNames=WG66_3002 {ECO:0000313|EMBL:KTB44420.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB44420.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB44420.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB44420.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably involved in transcription regulation via its
CC interaction with the INO80 complex, a chromatin remodeling complex.
CC {ECO:0000256|RuleBase:RU364121}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364121}.
CC -!- SIMILARITY: Belongs to the actin family.
CC {ECO:0000256|RuleBase:RU000487}.
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:KTB44420.1}.
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DR EMBL; LATX01000930; KTB44420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0G785; -.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU364121};
KW Nucleus {ECO:0000256|RuleBase:RU364121};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Transcription {ECO:0000256|RuleBase:RU364121};
KW Transcription regulation {ECO:0000256|RuleBase:RU364121}.
FT REGION 44..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 61740 MW; 42C495B64B634E12 CRC64;
MPRGIPNAKR DDTGIRYTTF HVPLATNPKQ LGSTYLKSEN QTVWHRNAQK KTKQSQEEGT
SPEARRGSQV LVIHPGSRFL RIGRASDVNP VTVPNVVARK TAPPVAASTF VEGVSRPRKA
KRNQRQSEVD ENADEYMVST SSDDPFEEKL SAIMSSLRDR MRFYKLRVTP NASNIATTFN
EQFKPEYIQE HNDPYRVDWI TDNKEDILVG EKALRLADPQ NSNYVVRWPI YGSNFNTRDY
SSIQMILNDM ETILRNTLKD KLGIEPKDYS KYSIVLVIPD LYDRTYVRDL VHLLLVSMGF
KQLCAQQESL AATYGAGISS ACVVDIGAKT TSIACVDEGL VISDTRMSLN FGGDDITELF
YVLLNRIGFP YRELNLARSY DWNVIDTLKC NLCTLSEVDV ALNLYDFVVR KPGQPAEKYG
LRTYDEVILA PMAIFEPRVI EFDRKRVGFW DIPNADVTEE ILELSNDHIT SAMMISTQHL
MPGPSPSIEQ NADQKECLQC ALYIEADPQT QEAIPGGTGE GDNTAAAVPS ETSTEQIFGS
TTDSFQKRH
//
