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CWC15_SCHPO
ID   CWC15_SCHPO             Reviewed;         265 AA.
AC   P78794; O74817;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Pre-mRNA-splicing factor cwf15;
DE   AltName: Full=Complexed with cdc5 protein 15;
GN   Name=cwf15; ORFNames=SPBC337.06c;
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 MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [2]
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   [3]
RP   IDENTIFICATION IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA   Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT   "Proteomics analysis reveals stable multiprotein complexes in both fission
RT   and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT   splicing factors, and snRNAs.";
RL   Mol. Cell. Biol. 22:2011-2024(2002).
CC   -!- FUNCTION: Involved in pre-mRNA splicing.
CC   -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC       spliceosome sub-complex reminiscent of a late-stage spliceosome
CC       composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC       cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC       cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC       cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC       cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC       prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC       smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CWC15 family. {ECO:0000305}.
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DR   EMBL; D89143; BAA13805.1; -; mRNA.
DR   EMBL; CU329671; CAA21276.1; -; Genomic_DNA.
DR   PIR; T40259; T40259.
DR   PIR; T42419; T42419.
DR   RefSeq; NP_595407.1; NM_001021314.2.
DR   PDB; 3JB9; EM; 3.60 A; h=1-265.
DR   PDBsum; 3JB9; -.
DR   AlphaFoldDB; P78794; -.
DR   SMR; P78794; -.
DR   BioGRID; 277499; 69.
DR   IntAct; P78794; 5.
DR   STRING; 4896.SPBC337.06c.1; -.
DR   iPTMnet; P78794; -.
DR   MaxQB; P78794; -.
DR   PaxDb; P78794; -.
DR   PRIDE; P78794; -.
DR   EnsemblFungi; SPBC337.06c.1; SPBC337.06c.1:pep; SPBC337.06c.
DR   GeneID; 2540983; -.
DR   KEGG; spo:SPBC337.06c; -.
DR   PomBase; SPBC337.06c; cwf15.
DR   VEuPathDB; FungiDB:SPBC337.06c; -.
DR   eggNOG; KOG3228; Eukaryota.
DR   HOGENOM; CLU_068312_0_1_1; -.
DR   InParanoid; P78794; -.
DR   OMA; NCARSEP; -.
DR   PhylomeDB; P78794; -.
DR   PRO; PR:P78794; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR   GO; GO:0000974; C:Prp19 complex; IDA:PomBase.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:PomBase.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   DisProt; DP02356; -.
DR   InterPro; IPR006973; Cwf_Cwc_15.
DR   PANTHER; PTHR12718; PTHR12718; 1.
DR   Pfam; PF04889; Cwf_Cwc_15; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Spliceosome.
FT   CHAIN           1..265
FT                   /note="Pre-mRNA-splicing factor cwf15"
FT                   /id="PRO_0000218242"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          155..205
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        71..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        238
FT                   /note="V -> L (in Ref. 1; BAA13805)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  30432 MW;  3F99C03BC06CD67B CRC64;
     MTTAHRPQFD PARGHSEMAP TRITSSRALP AHLKLKYRQE SQGTEEEVRK QDLREALLRA
     EAAHFATQEH GASSEEVSQN SKLIEGFTSP STDDKPNNDV EVDYQELLRQ TLEADEDASD
     SDDSVDSSNK NSEVSIKRRK TESNSQESVD SSNSESSDEE SDSEDETQQL LRELENIKQE
     RKREQMLQEE KNRALEQEKR EREIAFGNEL LNKASSGSFQ VKRRWDEDVV FRNTHKGVDD
     TPRPGFVNDM LRSEFHKKFL ARFVD
 
 
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