ID A0A367XQA7_9ASCO Unreviewed; 894 AA.
AC A0A367XQA7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=Actin-related protein 8 {ECO:0000256|RuleBase:RU364121};
GN Name=ARP8_0 {ECO:0000313|EMBL:RCK55788.1};
GN ORFNames=Cantr_05060 {ECO:0000313|EMBL:RCK55788.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK55788.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK55788.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK55788.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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:RCK55788.1}.
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DR EMBL; QLNQ01000029; RCK55788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367XQA7; -.
DR STRING; 5486.A0A367XQA7; -.
DR Proteomes; UP000253472; 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; -; 1.
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; 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:UP000253472};
KW Transcription {ECO:0000256|RuleBase:RU364121};
KW Transcription regulation {ECO:0000256|RuleBase:RU364121}.
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 101147 MW; 622CC62AA38E2F5F CRC64;
MLDAINPPTS PPYDSGANTP LLSSQADGIP PSDPVQPPAI SLDSPSDTTT SSTSPQTQQQ
QGEDDDPALK RHKPGPVAGK KPSAEALQRR KEGRIKAAAT LAQNLAKTGI GRFETENGFG
LTSVKTIPLI NQKNYFTEYL KKDEQVGFIR NWRHERALQQ KLKKLKQDQA AAQGQAQSQG
QTPGVLTPLN GAGDKKGEIR NFDDFNLNEI EAEMKKEMTA EVVVDDDEDD DEENETEEIR
EEKAKIGEDV IILQPGTRYI RIGKATDAVP MVVPNVIAVR KDGKVPKTDE IMPARQLDDG
DGDIVIDEDF DAQKAVMTKD FRARMRFYKR RVLPNSRETV SNFNRKREPE KIHDHNDPNK
KEWIKGEKEF YVGEDALKLV LNDGWVLRHP MINGNFNEYS YDYESREEVL GDLANIIKVC
LEQLEISNIP KLKVMLLIPD LYDKSYVETW VELLFKFVGF GRVGILQEAV AATFGATAST
ACIVDVGAQT TKISCVDEGM IINDSRILLN YGGDNITETF IKLTLEDQFP YKDINLIDSY
DWELAQELKE KFITFQDADI AVQLYDFYMR HPFKQTEKYE FKVFDEVMLA PMGLFFPKIF
QLGKKKPSIP NYHASAVSNK LTVDRLFPKS LDQYTSKPNN PSSKSQEELR RQLNYCDLTD
EELLLKLTGE EIPKDATTEG DERLYDVPLE KAIIESITNA GLSSDLSKIK KYYDNILIVG
GGLAKINGYD LLLTDRLNIW RPKILSTSAL GDIVAHLNGE VKANTAKRQA LIEEAEQKIK
DSLPPEQQQA LQADQQQQQQ QAEIELPEET IEKINNETEL KLDIEYIDEL IEKNGQHLPV
TILPSPREFD PSMITWKGGS VYGRLKVVNE MWITQKDWDL LGSRCLYYKS IFNY
//