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Database: UniProt
Entry: A0A1J9SHS3_9PEZI
LinkDB: A0A1J9SHS3_9PEZI
Original site: A0A1J9SHS3_9PEZI 
ID   A0A1J9SHS3_9PEZI        Unreviewed;       745 AA.
AC   A0A1J9SHS3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Chromatin remodeling complex subunit {ECO:0000313|EMBL:OJD39927.1};
GN   ORFNames=BKCO1_2000315 {ECO:0000313|EMBL:OJD39927.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD39927.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD39927.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD39927.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) 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:OJD39927.1}.
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DR   EMBL; MNUE01000002; OJD39927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9SHS3; -.
DR   STRING; 236234.A0A1J9SHS3; -.
DR   OrthoDB; 196861at2759; -.
DR   Proteomes; UP000183809; 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   Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   745 AA;  85047 MW;  8E3B31F6CE6D5D55 CRC64;
     MVQPSLDGVA QDVRSAKPSP ERIWSLKDPP FEGIRDVDSE GYRRSDSNTA IVIDNGSSSV
     RAGWAFDESP RLSVAPMMAR YRDRKLNTTF QFIGNEVYAD GTARGQAKNV YEPGTNIINN
     WDAMEGVLDY VFTKMGVNGS GGGINRPVAM TEPVANLGYS RRTMSEILFE LYGAPSAAFG
     IDSLFSYNYN NGKNGLVVSS SYTSTHLIPV VESKAMLSHA TRINWGRFQS AEFLQKLLRL
     KYPTFPGKLP DVQAEDLVRE HCYVSQDYDG ELSKYLDWTG LEERNHVIQF PFTEQVVVQK
     TEEELARAAE KRKESGRRLQ EQAAKMRLEK LIAKEQELAY YKELQTRLSE TTKKEGKRIL
     EGEDFDDEAQ LEKRIRELDK SIRKARNKDV GDMEEEENEP PTFPLVDVPD DQLDEEGLKQ
     KRQQRLMKSN YEARQRAKAE KEREKARIAE EERLDNERRE NDPETWIEER RVARQAIIQK
     IKDRERLKAD LGNRKSLAAQ MRMKSIANLA SDTPNKKRRR GADEDTFGAD DADWGVYRTI
     ATGEGSDDEE EEDLNTSLKS IESQLLKHDP KFTEDSTRDA QMDWTKSLLH SFTHGPYSFD
     PESQRQAHQI HLNVERIRVP EVVFQPSIAG LDQAGIVEIA SSILTERLAD HPRQKDVLKD
     VFLTGGNTLF KGFEERLRDD LRAYLPIDAE LVVRKAKDPV LDAWRGAARW AKSGESKKSW
     VSKAEWAEKG GDYIKEHDLG NSYTW
//
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