ID A0A165GX92_XYLHT Unreviewed; 726 AA.
AC A0A165GX92;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Actin-related protein 8 {ECO:0000256|RuleBase:RU364121};
GN ORFNames=L228DRAFT_247090 {ECO:0000313|EMBL:KZF22716.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF22716.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF22716.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF22716.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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}.
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DR EMBL; KV407458; KZF22716.1; -; Genomic_DNA.
DR RefSeq; XP_018188271.1; XM_018332558.1.
DR AlphaFoldDB; A0A165GX92; -.
DR STRING; 1328760.A0A165GX92; -.
DR GeneID; 28897695; -.
DR InParanoid; A0A165GX92; -.
DR OMA; AYKCMWA; -.
DR OrthoDB; 11729at2759; -.
DR Proteomes; UP000076632; 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 Gene3D; 3.30.420.580; -; 1.
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 Nucleotide-binding {ECO:0000256|RuleBase:RU364121};
KW Nucleus {ECO:0000256|RuleBase:RU364121};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632};
KW Transcription {ECO:0000256|RuleBase:RU364121};
KW Transcription regulation {ECO:0000256|RuleBase:RU364121}.
FT REGION 62..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 81466 MW; 95C7E84E68FB4E84 CRC64;
MVGKKSGKAL LREEGLERTD NNMDLTGWPQ VNMINQKNYY TEYLKRDDQI LVFRLQNEES
RNRMMRKAKD KDRALASSGK NDLPLPDADV DMDEEAQADE AGGAATEPLG SKVVVIHPGS
YNLRIGLASD ALPKSVPMVI ARKWKESEAE ERGGEPKPKR VKRESDGGVD HDRMFGEEFA
TQYTTMSSDL KIRMRNNKRR VLPNSKELVV NYNRRTTPDM ISEHNDPLRI DWTELPSNPR
EAPEVITGHA ALRIADDSKP RYKLFWPIQR GWCNEYEYTS RTLLYEDISV ILEEAIKSQV
GLNRKKDWNQ YSCVFVIPDL YERLYVTSIL EMLLREFRFG RVCFIQESLA ASFGAGYTTA
CIVDIGAQKT SICCVDEGMC IENSRVNLKY GGADVTDTFI KMMLFDHFPY SDINLKRRYD
FLLAEELKQK FCTMNEADIS VQLYDFHMRA PGEATKKYTF KTYDEVILAP LGYFQPSIFD
NSEKLLGRRK LIDRSYDIYD NSPNDPSSSA QLAILQAIAP APSVDATASS ANGDTANVAA
TPVRQQPYNL ANRFNDLENT PRSSVAGSPA PEGPGTPQPA GSSTPAVANG PTGPTSAEKT
LSASERDRII PVYPLDQAIL TSISNAVRDD ERKMRDLLGG IMVTGGGGQI PGFYAFLEER
LKALRPDLAK DIMIGTPPRE LDPQVVTWKG GSVFGKLKGT NDSWIGQMEY DRLGSRLLAY
KCMWAW
//