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Database: UniProt/SWISS-PROT
Entry: ESF2_NEOFI
LinkDB: ESF2_NEOFI
Original site: ESF2_NEOFI 
ID   ESF2_NEOFI              Reviewed;         365 AA.
AC   A1DIN9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Pre-rRNA-processing protein esf2;
DE   AltName: Full=18S rRNA factor 2;
GN   Name=esf2; ORFNames=NFIA_092060;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Involved in the small subunit (SSU) processome assembly and
CC       function, and in the 18S rRNA synthesis. Required for the early
CC       cleavages at sites A0, A1 and A2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ESF2/ABP1 family. {ECO:0000305}.
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DR   EMBL; DS027696; EAW19246.1; -; Genomic_DNA.
DR   RefSeq; XP_001261143.1; XM_001261142.1.
DR   AlphaFoldDB; A1DIN9; -.
DR   STRING; 331117.A1DIN9; -.
DR   EnsemblFungi; EAW19246; EAW19246; NFIA_092060.
DR   GeneID; 4587701; -.
DR   KEGG; nfi:NFIA_092060; -.
DR   VEuPathDB; FungiDB:NFIA_092060; -.
DR   eggNOG; KOG3152; Eukaryota.
DR   HOGENOM; CLU_054086_0_1_1; -.
DR   OMA; TRKHNDF; -.
DR   OrthoDB; 5481521at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd12263; RRM_ABT1_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR039119; ABT1/Esf2.
DR   InterPro; IPR034353; ABT1/ESF2_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   PANTHER; PTHR12311; ACTIVATOR OF BASAL TRANSCRIPTION 1; 1.
DR   PANTHER; PTHR12311:SF7; ACTIVATOR OF BASAL TRANSCRIPTION 1; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..365
FT                   /note="Pre-rRNA-processing protein esf2"
FT                   /id="PRO_0000285375"
FT   DOMAIN          149..239
FT                   /note="RRM"
FT   REGION          1..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  40963 MW;  1B13B716DBB816EA CRC64;
     MTTRKRNEFL DIVSDDDEGS DRGYDSAAAE ESKGRLAKRR KTHTRADDLS DEESDFGRSE
     SEDESKTRLK GKPKSKSQTT ERSNDSDDED EADDGEKMQV DQYLDTTAAH SPSQSRSQSP
     SASSVSSKPT KLKKKPLDKV RPPKKNKTGV IYLSSLPPYL KPFALKSMLE TRGFGPITKV
     FLTPEVPSNS APRRRSNKRK SYADGWVEFA SKKTAKICAE TLNATIVGGK KGGWYHDDVW
     NMKYLKGFKW ADLMEQVQRE RSEREAKRRI EDTRARKEDK VFLQGVEQGK VLQGIQKKNE
     EKKKKKGETG PGEGEGSADA AAAAAASELK VRRLFKQSEV KMGRDKVKDI STLEDDAKRV
     LSKIF
//
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