ESF1_SCHPO
ID ESF1_SCHPO Reviewed; 682 AA.
AC O74828;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Pre-rRNA-processing protein esf1;
GN Name=esf1; ORFNames=SPBC1734.01c, SPBC337.17c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; THR-121; SER-125 AND
RP SER-506, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved 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:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the ESF1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21287.1; -; Genomic_DNA.
DR PIR; T40270; T40270.
DR RefSeq; NP_595418.1; NM_001021325.2.
DR AlphaFoldDB; O74828; -.
DR BioGRID; 276614; 3.
DR STRING; 4896.SPBC1734.01c.1; -.
DR iPTMnet; O74828; -.
DR MaxQB; O74828; -.
DR PaxDb; O74828; -.
DR PRIDE; O74828; -.
DR EnsemblFungi; SPBC1734.01c.1; SPBC1734.01c.1:pep; SPBC1734.01c.
DR GeneID; 2540076; -.
DR KEGG; spo:SPBC1734.01c; -.
DR PomBase; SPBC1734.01c; esf1.
DR VEuPathDB; FungiDB:SPBC1734.01c; -.
DR eggNOG; KOG2318; Eukaryota.
DR HOGENOM; CLU_010564_0_1_1; -.
DR InParanoid; O74828; -.
DR OMA; LTWDETA; -.
DR PhylomeDB; O74828; -.
DR PRO; PR:O74828; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003723; F:RNA binding; ISO:PomBase.
DR GO; GO:0006364; P:rRNA processing; ISO:PomBase.
DR InterPro; IPR039754; Esf1.
DR InterPro; IPR012580; NUC153.
DR PANTHER; PTHR12202; PTHR12202; 1.
DR Pfam; PF08159; NUC153; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..682
FT /note="Pre-rRNA-processing protein esf1"
FT /id="PRO_0000352844"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 471..597
FT /evidence="ECO:0000255"
FT COMPBIAS 72..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 682 AA; 77754 MW; 05054661DB72023F CRC64;
MGKKQTKPIN AKSRSESNVV ADPRFQSVHS DPRFSRLKRG NFKVKVDERF KSLKEDKDFK
TTASVDRYGR PLNQDKATKE IDRLYELENE GSSSSSESSE ITDNEEVASA SSKSTKSEEL
TDEESEDEEV YDPARGEGII STSESSDESD AESETEAQPE ISELAGIEPE ENIPRGSETN
RLAVVNMDWD NLQAVDLFVA LSSFCPPGGK LLKVSIYPSE FGKSRMAAEH VQGPPRDIFT
PADNQPSSAE LHEAQKFGFD NNESDQDEED ALIEEDLGNE FDMVKLRQYQ LERLRYYYAV
VECDSVRTAK VIYETCDGAE YETSANIYDL RFIPDDVTFD DDESREVCTK APEKYEPRDF
VTDALQHSKV KLSWDAEDPH RKDLIKKAFT SQDIEDLDFS AYIASSESED EDVDVIRSRY
QKLLSGDADD FQANSNPFED DDKLEGANGE MEVTFTSGFD VDNNANSSEK DETTIEKYKR
KAAERKQRRK ELRQLKKTKD DEGEGSDVDL GFDDPFFKDK DASRNNKKNK KGKHTQIEDP
TAASKEELEN LVREDENDSE QLDHFDMKSI LKAEKFKKNR KLKKKASNLE GLQEGFEADV
SDPRFAALYT NHNFALDPTN PHFKRTKTVE KIMDESRKRR SNQLEQTQDG KPELKIKKRK
AEKGDQRQEL DRIVKSIKRS GK
