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Database: UniProt
Entry: A0A2J6QCL9_9HELO
LinkDB: A0A2J6QCL9_9HELO
Original site: A0A2J6QCL9_9HELO 
ID   A0A2J6QCL9_9HELO        Unreviewed;       297 AA.
AC   A0A2J6QCL9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   RecName: Full=rRNA-processing protein EFG1 {ECO:0000256|ARBA:ARBA00018689};
DE   AltName: Full=rRNA-processing protein efg1 {ECO:0000256|ARBA:ARBA00019827};
GN   ORFNames=NA56DRAFT_643296 {ECO:0000313|EMBL:PMD24013.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD24013.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD24013.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD24013.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ613473; PMD24013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6QCL9; -.
DR   STRING; 1745343.A0A2J6QCL9; -.
DR   OrthoDB; 1333547at2759; -.
DR   Proteomes; UP000235672; 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   Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   297 AA;  34105 MW;  DE904D12AD7F0E30 CRC64;
     MSTKRKYQEE DPQEAIHESR QFQVYGNAPK PSKKPRRLEP RVQRKQAHAS SVNAIKKRIR
     DVTRKLERKE DLPANVRAED ERALAAYQQE LGSAQAEKTR QKMIKKYHMV RFFERQKATR
     LLKKLRKRLL ATESTEEVEI LKAQMHVAEV DLNYTQYCPL SEPYVSLYPQ KSSSADEPNQ
     LKEASSKPKP PMWSEVEKCM KDGTLNRLRN RLSVGPPQVS KPSARKQAKA KPETAAVDVT
     GMNRRERRSQ RGAKDSRTKN KSMAFAKNEA FGASQHAMAE ENADQDDDSE GGFFEEE
//
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