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SLT11_USTMA
ID   SLT11_USTMA             Reviewed;         324 AA.
AC   Q4PGU6; A0A0D1EDH3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Pre-mRNA-splicing factor SLT11;
GN   Name=SLT11; ORFNames=UMAG_00667;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pre-mRNA splicing. Facilitates the cooperative
CC       formation of U2/U6 helix II in association with stem II in the
CC       spliceosome. Binds to RNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SLT11 family. {ECO:0000305}.
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DR   EMBL; CM003140; KIS72255.1; -; Genomic_DNA.
DR   RefSeq; XP_011386470.1; XM_011388168.1.
DR   AlphaFoldDB; Q4PGU6; -.
DR   SMR; Q4PGU6; -.
DR   STRING; 5270.UM00667P0; -.
DR   EnsemblFungi; KIS72255; KIS72255; UMAG_00667.
DR   GeneID; 23561903; -.
DR   KEGG; uma:UMAG_00667; -.
DR   VEuPathDB; FungiDB:UMAG_00667; -.
DR   eggNOG; KOG0153; Eukaryota.
DR   HOGENOM; CLU_027112_0_0_1; -.
DR   InParanoid; Q4PGU6; -.
DR   OMA; PYFRKGR; -.
DR   OrthoDB; 1272857at2759; -.
DR   Proteomes; UP000000561; Chromosome 1.
DR   GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0036002; F:pre-mRNA binding; IBA:GO_Central.
DR   GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR039171; Cwc2/Slt11.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR032297; Torus.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR14089; PTHR14089; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF16131; Torus; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   SUPFAM; SSF90229; SSF90229; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   3: Inferred from homology;
KW   Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..324
FT                   /note="Pre-mRNA-splicing factor SLT11"
FT                   /id="PRO_0000212430"
FT   DOMAIN          227..317
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         149..175
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          173..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   324 AA;  35874 MW;  46F456CFB9B56008 CRC64;
     MSSLTEDLET PILCESCLGP NPYIRMTKDP RGKSCKVCTR PFTVFRWNPG AGSRFKKTEI
     CATCAKVKNV CQTCILDLQY GLPVQVRDAA LGIKSDAGPT SSDKAKAYFA DTMEKQLEAT
     VGSSSRAGQE LVRKAARREI DYKRDRPVQS QKLCSAFARG RCERGDSCPF KHQLPTDDQL
     PGLQPSSNIN YPYSPTSSSP SKQAVAKILT SSTSSVGLPP PSDASVRSLF ISNLPPEHLE
     EPSIRQFFLD LAPPLQAQDI KSITLVRASN CAFVNFATRD HAELAARRCE PKMRLGDKEI
     RLMWGRSRPV KRNEENECKK AEVE
 
 
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