EFS2_DICDI
ID EFS2_DICDI Reviewed; 296 AA.
AC Q54BL2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Putative pre-rRNA-processing protein esf2;
GN Name=esf2; ORFNames=DDB_G0293576;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: May be involved in the small subunit (SSU) processome
CC assembly and function, and in the 17S rRNA synthesis. {ECO:0000250}.
CC -!- SUBUNIT: Component of the 90S pre-ribosomes. {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; AAFI02000218; EAL60600.1; -; Genomic_DNA.
DR RefSeq; XP_629017.1; XM_629015.1.
DR AlphaFoldDB; Q54BL2; -.
DR SMR; Q54BL2; -.
DR STRING; 44689.DDB0266368; -.
DR PaxDb; Q54BL2; -.
DR EnsemblProtists; EAL60600; EAL60600; DDB_G0293576.
DR GeneID; 8629301; -.
DR KEGG; ddi:DDB_G0293576; -.
DR dictyBase; DDB_G0293576; esf2.
DR eggNOG; KOG3152; Eukaryota.
DR HOGENOM; CLU_941432_0_0_1; -.
DR InParanoid; Q54BL2; -.
DR OMA; TRKHNDF; -.
DR PhylomeDB; Q54BL2; -.
DR PRO; PR:Q54BL2; -.
DR Proteomes; UP000002195; Chromosome 6.
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 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..296
FT /note="Putative pre-rRNA-processing protein esf2"
FT /id="PRO_0000327515"
FT DOMAIN 110..193
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 35333 MW; 9F9F5F4963BA3FBD CRC64;
MAQKRKNDKI ETSKKEEIDP RFVNKFEDLE ENDFKDDDED DFINDVNEGE EEEEEEDNED
NIEFNQEEDD EDEDDEENKD NKNKIKKVIK IKPMDIEKMK KLKEQNENKG IIYLSTIPSR
MKPAKLKQLL AKYGKVTRMH LVRANVERKN HRNDMFKEGW IEFEDKALAR KIATILNNIP
MGGKARDIHK DCLWNLRYLP KFKWHHLQDK LVSQRMERDK KLRLEINQVR KQNLILLEQV
ELSKHVNQKH ESKGKPIKEK VVRTFKQRSS HEDSLNSNIS SKVLEKVVSN KKQKIN