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Database: UniProt
Entry: A0A427XNR0_9TREE
LinkDB: A0A427XNR0_9TREE
Original site: A0A427XNR0_9TREE 
ID   A0A427XNR0_9TREE        Unreviewed;       755 AA.
AC   A0A427XNR0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Actin-protein 5 {ECO:0000313|EMBL:RSH80549.1};
GN   Name=ARP5 {ECO:0000313|EMBL:RSH80549.1};
GN   ORFNames=EHS24_009131 {ECO:0000313|EMBL:RSH80549.1};
OS   Apiotrichum porosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Apiotrichum.
OX   NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH80549.1, ECO:0000313|Proteomes:UP000279236};
RN   [1] {ECO:0000313|EMBL:RSH80549.1, ECO:0000313|Proteomes:UP000279236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH80549.1,
RC   ECO:0000313|Proteomes:UP000279236};
RA   Aliyu H., Gorte O., Ochsenreither K.;
RT   "Genome sequence of Apiotrichum porosum DSM 27194.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RSH80549.1}.
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DR   EMBL; RSCE01000008; RSH80549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A427XNR0; -.
DR   STRING; 105984.A0A427XNR0; -.
DR   OrthoDB; 196861at2759; -.
DR   Proteomes; UP000279236; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:SF16; ACTIN-RELATED PROTEIN 5; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279236}.
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          292..319
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  85763 MW;  C22C6486BCA0316E CRC64;
     MDSAKAASAS SSSSPARENA VNVPETERFT GEPQAPYDYH SLDGRDPVIC IDNGSHSWRA
     GFSTMDSPYI DRPNIVSRYR ERKLGRNTLL FGNDVEVDAN SRSQSRTMFD GDMLIHGDLM
     ECALDFTFLT LGIDSNRIEQ PIVMTERLAN PLFTRAMTSE LLFELYGAPE VTYGIDSLFA
     FSRHKHRDGL SIHMGHNAST VIPVVDGKGV LTRAKRIPWG GSQSADLLLK LAQLKYPSFP
     LKVTQSQATF MYHETCYFAS DYDEELRSLA NPATMEAKTM VVQFPYNQPE VVEKTEEEIA
     AQLERRKEQG RRLQEMQAKQ RAEKLAAKVA ELDEYKMLVA ERGSLKKADW VQRISDTTPF
     ETEAELEAWI KKTELEVRRK QKREMGEEPE PEEEPSFPLA DRPDEELTEE EIKEKRRQRL
     MKAGWEARVK VREEKRKERE RLEELQRLDD EERVNNLPGW SAKLKVEHVS VIERMKERKK
     RRAQLGDRKS AAAQNRMKSI ASLAAEGSSG KKRKKGDEGA YTGKLGSSND AEKDDGFGRD
     DSDWAVYREI VAEDDSEAEE DDLAQLQTIE SKLLEHDPHF TDDHTLEGQV RVKNALLNAF
     TRGDALGRYD PDNIHQNYQI HLNVERIRVP ETWFQPSMFG VDSAGLGEVA GWLLNGFDED
     VRARLMQCVV LSGGSTKLPN LLPRMRNTLT PVLPFRTPLK IYGALNNADP RLETWRGMAE
     WASTSEGKAA RVTRAEYDEY GGEWVKEYAW GNAAP
//
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