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SPF30_SCHPO
ID   SPF30_SCHPO             Reviewed;         311 AA.
AC   O94519;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Splicing factor spf30;
DE   AltName: Full=Survival of motor neuron-related-splicing factor 30 homolog;
GN   Name=spf30; ORFNames=SPCC1281.02c;
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-173, AND IDENTIFICATION BY
RP   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 spliceosome assembly.
CC       {ECO:0000250|UniProtKB:O75940}.
CC   -!- SUBUNIT: Associates with spliceosomes (By similarity).
CC       {ECO:0000250|UniProtKB:O75940}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- DOMAIN: The Tudor domain mediates association with dimethylarginines,
CC       which are common in snRNP proteins. {ECO:0000250|UniProtKB:O75940}.
CC   -!- SIMILARITY: Belongs to the SMN family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA22823.1; -; Genomic_DNA.
DR   PIR; T40921; T40921.
DR   RefSeq; NP_588166.1; NM_001023155.2.
DR   AlphaFoldDB; O94519; -.
DR   SMR; O94519; -.
DR   BioGRID; 275295; 30.
DR   STRING; 4896.SPCC1281.02c.1; -.
DR   iPTMnet; O94519; -.
DR   MaxQB; O94519; -.
DR   PaxDb; O94519; -.
DR   PRIDE; O94519; -.
DR   EnsemblFungi; SPCC1281.02c.1; SPCC1281.02c.1:pep; SPCC1281.02c.
DR   GeneID; 2538711; -.
DR   KEGG; spo:SPCC1281.02c; -.
DR   PomBase; SPCC1281.02c; spf30.
DR   VEuPathDB; FungiDB:SPCC1281.02c; -.
DR   eggNOG; KOG3026; Eukaryota.
DR   HOGENOM; CLU_069491_1_0_1; -.
DR   InParanoid; O94519; -.
DR   OMA; NKWQEFT; -.
DR   PhylomeDB; O94519; -.
DR   PRO; PR:O94519; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005681; C:spliceosomal complex; NAS:PomBase.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:PomBase.
DR   GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:PomBase.
DR   CDD; cd04508; TUDOR; 1.
DR   InterPro; IPR041297; Crb2_Tudor.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF18115; Tudor_3; 1.
DR   SMART; SM00333; TUDOR; 1.
PE   1: Evidence at protein level;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Spliceosome.
FT   CHAIN           1..311
FT                   /note="Splicing factor spf30"
FT                   /id="PRO_0000290648"
FT   DOMAIN          76..139
FT                   /note="Tudor"
FT   REGION          154..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   311 AA;  34626 MW;  30F798D17CA351FC CRC64;
     MEKELEEYKS QLALVQISLQ KTPQNEELQL LENDLKELIS LTENLLQESV ENDKNTFQNS
     QNGVAGFNTS KPVHIDFTPG NLVMARWVSG DYLFYPSRIT AVSGFGANKK YTVQFLDYPD
     IETVSLKHIK AMPEEKRQEI EGNKEILKKS TTIRSTPVRE PTKAISVASM STSPSNYASR
     ASSPDMKSSA AVTANVSPIQ NVAQHVSTLP KISPIPPSNP PPVPSVSYSQ KQQKQLKPKA
     ALEASQNSWK QFAARGVKTG RVGKRKKIGE SSIFKSTEDF PGRTNPKNFG NVARSGHREK
     HIYNYREDED S
 
 
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