SNU66_SCHPO
ID SNU66_SCHPO Reviewed; 649 AA.
AC O94538;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=U4/U6.U5 tri-snRNP-associated protein snu66;
GN Name=snu66; ORFNames=SPAC167.03c;
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 FUNCTION, INTERACTION WITH HUB1, AND SUBCELLULAR LOCATION.
RX PubMed=15620657; DOI=10.1016/j.cub.2004.11.058;
RA Wilkinson C.R.M., Dittmar G.A.G., Ohi M.D., Uetz P., Jones N., Finley D.;
RT "Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and
RT localization of an essential splicing factor in fission yeast.";
RL Curr. Biol. 14:2283-2288(2004).
RN [3]
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).
CC -!- FUNCTION: Required for efficient splicing of pre-mRNA.
CC {ECO:0000269|PubMed:15620657}.
CC -!- SUBUNIT: Interacts with hub1. {ECO:0000269|PubMed:15620657}.
CC -!- INTERACTION:
CC O94538; O94650: hub1; NbExp=2; IntAct=EBI-607744, EBI-607734;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15620657,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNU66/SART1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA22848.1; -; Genomic_DNA.
DR PIR; T37740; T37740.
DR RefSeq; NP_593382.1; NM_001018814.2.
DR AlphaFoldDB; O94538; -.
DR BioGRID; 279223; 31.
DR IntAct; O94538; 2.
DR STRING; 4896.SPAC167.03c.1; -.
DR iPTMnet; O94538; -.
DR MaxQB; O94538; -.
DR PaxDb; O94538; -.
DR PRIDE; O94538; -.
DR EnsemblFungi; SPAC167.03c.1; SPAC167.03c.1:pep; SPAC167.03c.
DR GeneID; 2542774; -.
DR KEGG; spo:SPAC167.03c; -.
DR PomBase; SPAC167.03c; snu66.
DR VEuPathDB; FungiDB:SPAC167.03c; -.
DR eggNOG; KOG2217; Eukaryota.
DR HOGENOM; CLU_009379_2_0_1; -.
DR InParanoid; O94538; -.
DR OMA; EYARWEN; -.
DR PhylomeDB; O94538; -.
DR PRO; PR:O94538; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IC:PomBase.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:PomBase.
DR GO; GO:0000481; P:maturation of 5S rRNA; ISO:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR InterPro; IPR045347; HIND.
DR InterPro; IPR005011; SNU66/SART1.
DR PANTHER; PTHR14152; PTHR14152; 1.
DR Pfam; PF19252; HIND; 1.
DR Pfam; PF03343; SART-1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..649
FT /note="U4/U6.U5 tri-snRNP-associated protein snu66"
FT /id="PRO_0000290651"
FT REGION 27..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..93
FT /evidence="ECO:0000255"
FT COILED 516..583
FT /evidence="ECO:0000255"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 74734 MW; 27EC1138F612329D CRC64;
MSGNSGASES ISIEETNRIR ISLGLKPLDI SEEKPQKELS DASVKSSYVD QEQQAYENWK
KQEQEEINRK KEEELKSKFE KLRQKNERRR RTQGKTLAET LAEEDDQIDA NDTRAWILKM
RNSSLNKNGN GLNFEAKNDA PRRSTLHSQN AGPNVNSSLE GMKIAHGFQD LNKNDGLVLT
LKDADILDED NHDLLENVEM VQRKTKNERK EDNPYKPYED ENDFLQQSEA DQPSEDTFTT
IGPQNSLTVN STIEKHKSDN KKTFGTLVSF VEPTITGSEQ SDYRQIKIKK SKKKKSKSDR
RKRLVELDAE NENENDPSDF VLPNGQSNSD LSVEQDSAIF KEQKKMKIQK RMRELETQSF
ADDDDLQQSI AMQRRLAQKR AKILKPEDVA EQLQNAEEVT DMTDSDTASG LIFDDTRAFV
NSIKETENRE ALGSINEQAF EDSKDLNDTN SITGSSPTEE SNALVEDTSV DISATLEEAN
TQQENAEDEP LVSDNVGAVL SLLRNKGVIK VSDEAKEKIQ KEEEYNKWFA RKQQARVELE
EQRRKKKEQD RLSGKFEKMT QKEREQYAKK ENERWDKKIA EIELEQFHDY KPQVDIKYVD
EFGVELGPKE AYKYLLSHQF HGKGSGKAKT EKRLRRIVEK EREERKPIF