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Database: UniProt
Entry: J5JX34_BEAB2
LinkDB: J5JX34_BEAB2
Original site: J5JX34_BEAB2 
ID   J5JX34_BEAB2            Unreviewed;       294 AA.
AC   J5JX34;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=rRNA-processing protein EFG1 {ECO:0000256|ARBA:ARBA00018689};
DE   AltName: Full=rRNA-processing protein efg1 {ECO:0000256|ARBA:ARBA00019827};
GN   ORFNames=BBA_04144 {ECO:0000313|EMBL:EJP66851.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP66851.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP66851.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP66851.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
CC   -!- FUNCTION: Involved in rRNA processing. {ECO:0000256|ARBA:ARBA00002773}.
CC   -!- SIMILARITY: Belongs to the EFG1 family.
CC       {ECO:0000256|ARBA:ARBA00006916}.
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DR   EMBL; JH725158; EJP66851.1; -; Genomic_DNA.
DR   RefSeq; XP_008597463.1; XM_008599241.1.
DR   AlphaFoldDB; J5JX34; -.
DR   STRING; 655819.J5JX34; -.
DR   GeneID; 19887156; -.
DR   HOGENOM; CLU_066912_0_0_1; -.
DR   InParanoid; J5JX34; -.
DR   OrthoDB; 1333547at2759; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   InterPro; IPR019310; Efg1.
DR   PANTHER; PTHR33911; RRNA-PROCESSING PROTEIN EFG1; 1.
DR   PANTHER; PTHR33911:SF1; RRNA-PROCESSING PROTEIN EFG1; 1.
DR   Pfam; PF10153; Efg1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002762}.
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          93..120
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        199..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   294 AA;  33459 MW;  5094441DCB92DB71 CRC64;
     MEENRRNRGQ GGNSRQKYAA GKHKAKLGSA EWAKKRTRSI QRMMSRNGDI PANLRNDMER
     ELAAHKSTIN EKTFQRRRSA MISKYHMVRF FERKKATRLV KQLKRQLEAT TDDHERSKLQ
     ADLHIAEVDE AYTMHHPHAE TYISLYGTIK KDDDEDATEE EKKTAAAKAA LAAERPPMWK
     VVESTMEEGP DALRQLRERR SATGDDEASA PQPRSRDSRP APRKERMANV IAKQNQSKNA
     SKPTGDRKAA PASAGEQQSG AKTGGLNRRE RRRIMRETMA STDKEDDEGG FFEI
//
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