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 27-MAR-2024, entry version 111.
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; 284812.O94519; -.
DR iPTMnet; O94519; -.
DR MaxQB; O94519; -.
DR PaxDb; 4896-SPCC1281-02c-1; -.
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; IEA:UniProtKB-KW.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:PomBase.
DR CDD; cd20446; Tudor_SpSPF30-like; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR InterPro; IPR041297; Crb2_Tudor.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR46297; ZINC FINGER CCCH-TYPE WITH G PATCH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46297:SF1; ZINC FINGER CCCH-TYPE WITH G PATCH DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF18115; Tudor_3; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 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
//
