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ESF2_PICST
ID   ESF2_PICST              Reviewed;         347 AA.
AC   A3LVD5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Pre-rRNA-processing protein ESF2;
DE   AltName: Full=18S rRNA factor 2;
GN   Name=ESF2; ORFNames=PICST_32082;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000499; ABN67100.2; -; Genomic_DNA.
DR   RefSeq; XP_001385129.2; XM_001385092.1.
DR   AlphaFoldDB; A3LVD5; -.
DR   STRING; 4924.XP_001385129.2; -.
DR   PRIDE; A3LVD5; -.
DR   EnsemblFungi; ABN67100; ABN67100; PICST_32082.
DR   GeneID; 4839724; -.
DR   KEGG; pic:PICST_32082; -.
DR   eggNOG; KOG3152; Eukaryota.
DR   HOGENOM; CLU_054086_0_0_1; -.
DR   InParanoid; A3LVD5; -.
DR   OMA; HILSNFG; -.
DR   OrthoDB; 1377351at2759; -.
DR   Proteomes; UP000002258; Chromosome 5.
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; PTHR12311; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..347
FT                   /note="Pre-rRNA-processing protein ESF2"
FT                   /id="PRO_0000285378"
FT   DOMAIN          146..236
FT                   /note="RRM"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..97
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  40620 MW;  874B4FEE0312FB91 CRC64;
     MSKRITKTSA IHDKHSIITR DTESGFEYDS DSESDVENVF PNIRVQRIRD KLYQDEDEDE
     DEQVDDEDEE DEEDKEDEED DADNFENENE EEVDDYIDGD GMRNFDMGES IEVGDVDSTS
     ERKNGKIKKL TSRQLQKEQK RIKRTGVCYL SRIPPYMKPA TLRSILSRFG KIDRLFLKPE
     DSAIYHKRVK YGGNKKKNFT EGWVEFVNKK DAKMCASTLN ANKLGGRKTS YYYDDVINMK
     YLSGFKWFDL TQQIAKENEV RQAKLSLELS QQQKLNKTFV NNVEKSKLVS TIQRKRKERD
     PEHESDSHIR RSFKQRKVTS TRADADEELK ARAQPDRKLS DVLSKVF
 
 
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