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Database: UniProt
Entry: A0A165YF40_9AGAM
LinkDB: A0A165YF40_9AGAM
Original site: A0A165YF40_9AGAM 
ID   A0A165YF40_9AGAM        Unreviewed;       734 AA.
AC   A0A165YF40;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Actin-like protein Arp5p {ECO:0000313|EMBL:KZV61285.1};
GN   ORFNames=PENSPDRAFT_693545 {ECO:0000313|EMBL:KZV61285.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV61285.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV61285.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV61285.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the actin family.
CC       {ECO:0000256|RuleBase:RU000487}.
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DR   EMBL; KV424788; KZV61285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165YF40; -.
DR   STRING; 1314672.A0A165YF40; -.
DR   InParanoid; A0A165YF40; -.
DR   OrthoDB; 196861at2759; -.
DR   Proteomes; UP000077086; 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; -; 4.
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:UP000077086}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          287..314
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          423..453
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        375..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  81439 MW;  24EEB0EDEA7ECF3A CRC64;
     MASESDALNI VSLPPPPAIP NQPRHTYDAG AKLHHTPIVI DNGSSTLRFG WAGWADPICA
     QNAVSRFKER RQGKQLLLFG EAIDSESGAR AQSKQPWEGD ILVNPDALES ALDYVFTSLA
     LDTPTVTHPI LISERLASPL YSRTLTSELL FELYTVPSVV YAVDAPMSLY HNHLPPSPTA
     PFNQNALVVS FNTASTSVIP MVSGRGIMSA ARRLPFGAQH ANDYLLKLVQ LKYPSFGTRV
     TPAQTNWILR THCAVAPDYP LLMRTLADPL ELKRNEVVVQ FPYAAPVEKS EEEKAKLTER
     RREQGKKLQE MAAKARADKL AKTEDALRVL EDLKAQKGSV SRKEWMEMLA DEDFENEEKL
     DGAIRKLDAD VRKARKKDAT GEAMDEDKDI GEPSFPLVDT PDAELDEEGV KEKRRQKLMK
     AGYDARVRAR KEKEREREEL EAKERAEAEE RERDLAGWAG KLRTEHETIM NKIKERSRRR
     AALGDRKSAA AQARMKSIAS LAADERVPKK RRKGNGEDMF GADDSDWAIY RKINTAAPSS
     DEEDDLLHLT TLEEKLLAHD PTFSLSLTHA SLSTARSALL TSYRPIYPEE DSAGQMRIHL
     STERWRSVEP YFTPGMAGVD AAGLGELAGN VLSMFASDVR ARLASTIFLT GAPASLPGLG
     ERLANALRPN LPVGANLRVV RAQDPGNDAW RGMAAFAQTP GFRNVGVSKA EYEEWGGERV
     KRWWGGNWNA SVSL
//
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