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