ID   ESF2_NEUCR              Reviewed;         340 AA.
AC   Q7S8W7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Pre-rRNA-processing protein esf-2;
DE   AltName: Full=18S rRNA factor 2;
GN   Name=esf-2; ORFNames=NCU08668;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002239; EAA32781.1; -; Genomic_DNA.
DR   RefSeq; XP_962017.1; XM_956924.2.
DR   AlphaFoldDB; Q7S8W7; -.
DR   SMR; Q7S8W7; -.
DR   STRING; 5141.EFNCRP00000004040; -.
DR   EnsemblFungi; EAA32781; EAA32781; NCU08668.
DR   GeneID; 3878165; -.
DR   KEGG; ncr:NCU08668; -.
DR   VEuPathDB; FungiDB:NCU08668; -.
DR   HOGENOM; CLU_054086_0_1_1; -.
DR   InParanoid; Q7S8W7; -.
DR   OMA; TRKHNDF; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0034462; P:small-subunit processome assembly; IBA:GO_Central.
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   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR12311; PTHR12311; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..340
FT                   /note="Pre-rRNA-processing protein esf-2"
FT                   /id="PRO_0000285376"
FT   DOMAIN          124..214
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..64
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   340 AA;  38109 MW;  14F8E629AE6818BD CRC64;
     MPEDDVRNKF LDAGDSDDDA GHGSDSEDDF QKGGRNAKRR RVSDDEDSEA DDFTDAEEEH
     DQDDAESKDA PAKDGQETTD GKEKKDGKKE KEKKSVLASD LPGMTKPLTK KNLIVTEEAI
     KKSGVVYISR VPPFMTPAKL RSLLEPYGKL NRIFLAPEDP VARRKRIRSG GNKKKMFTEG
     WIEFVKKKDA KKACELLNAR PIGGKKGSYY RDDIWNLLYL KGFKWHNLTE QIAAENAERS
     SRMRAEISKT TKENKEFVRN VERAKVLQGI QAKKASKGSK AGGEGAAQVT ESTIPSAAAT
     TTTTTNDDKR RTFKQIPLAK KRKLDETQPE QVQRVLSKIF