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RPAB2_SCHPO
ID   RPAB2_SCHPO             Reviewed;         142 AA.
AC   P36595;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC2;
DE            Short=RNA polymerases I, II, and III subunit ABC2;
DE   AltName: Full=DNA-directed RNA polymerases I, II, and III 15 kDa polypeptide;
DE   AltName: Full=RPC16;
GN   Name=rpb6; Synonyms=rpo15; ORFNames=SPCC1020.04c;
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 [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8088549; DOI=10.1016/0378-1119(94)90039-6;
RA   Shpakovski G.V.;
RT   "The fission yeast Schizosaccharomyces pombe rpb6 gene encodes the common
RT   phosphorylated subunit of RNA polymerase and complements a mutation in the
RT   corresponding gene of Saccharomyces cerevisiae.";
RL   Gene 147:63-69(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RA   Williams M.R., Konoha G., Yanagida M., Young R.F.;
RT   "Sequence of the rpo15 gene from S. pombe - a subunit common to all three
RT   RNA polymerases.";
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
CC   -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Common component of RNA polymerases I, II and III which synthesize
CC       ribosomal RNA precursors, mRNA precursors and many functional non-
CC       coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
CC       Pol II is the central component of the basal RNA polymerase II
CC       transcription machinery. Pols are composed of mobile elements that move
CC       relative to each other. In Pol II, RPB6 is part of the clamp element
CC       and together with parts of RPB1 and RPB2 forms a pocket to which the
CC       RPB4-RPB7 subcomplex binds (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC       (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC       least 14, 12 and 17 subunits, respectively. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC       subunit family. {ECO:0000305}.
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DR   EMBL; L00597; AAA52084.1; -; Genomic_DNA.
DR   EMBL; L25592; AAB04116.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA18992.1; -; Genomic_DNA.
DR   PIR; T40837; T40837.
DR   RefSeq; NP_587956.1; NM_001022947.2.
DR   PDB; 3H0G; X-ray; 3.65 A; F/R=1-142.
DR   PDB; 5U0S; EM; 7.80 A; f=1-142.
DR   PDB; 7AOC; EM; 3.84 A; F=1-142.
DR   PDB; 7AOD; EM; 4.50 A; F/R=1-142.
DR   PDB; 7AOE; EM; 3.90 A; F=1-142.
DR   PDBsum; 3H0G; -.
DR   PDBsum; 5U0S; -.
DR   PDBsum; 7AOC; -.
DR   PDBsum; 7AOD; -.
DR   PDBsum; 7AOE; -.
DR   AlphaFoldDB; P36595; -.
DR   SMR; P36595; -.
DR   BioGRID; 275655; 14.
DR   IntAct; P36595; 1.
DR   STRING; 4896.SPCC1020.04c.1; -.
DR   iPTMnet; P36595; -.
DR   MaxQB; P36595; -.
DR   PaxDb; P36595; -.
DR   EnsemblFungi; SPCC1020.04c.1; SPCC1020.04c.1:pep; SPCC1020.04c.
DR   GeneID; 2539083; -.
DR   KEGG; spo:SPCC1020.04c; -.
DR   PomBase; SPCC1020.04c; rpb6.
DR   VEuPathDB; FungiDB:SPCC1020.04c; -.
DR   eggNOG; KOG3405; Eukaryota.
DR   HOGENOM; CLU_112527_0_1_1; -.
DR   InParanoid; P36595; -.
DR   OMA; MLVRRTW; -.
DR   PhylomeDB; P36595; -.
DR   Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR   Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-SPO-72086; mRNA Capping.
DR   Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-SPO-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-SPO-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR   Reactome; R-SPO-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR   Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR   EvolutionaryTrace; P36595; -.
DR   PRO; PR:P36595; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005736; C:RNA polymerase I complex; IGI:PomBase.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IDA:PomBase.
DR   GO; GO:0005666; C:RNA polymerase III complex; IGI:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0006354; P:DNA-templated transcription, elongation; TAS:PomBase.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IC:PomBase.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IC:PomBase.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; IC:PomBase.
DR   Gene3D; 3.90.940.10; -; 1.
DR   HAMAP; MF_00192; RNApol_arch_Rpo6; 1.
DR   InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR   InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR   InterPro; IPR028363; RPB6.
DR   InterPro; IPR036161; RPB6/omega-like_sf.
DR   InterPro; IPR006111; Rpo6/Rpb6.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   PIRSF; PIRSF500154; RPB6; 1.
DR   PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR   SMART; SM01409; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; SSF63562; 1.
DR   PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription.
FT   CHAIN           1..142
FT                   /note="DNA-directed RNA polymerases I, II, and III subunit
FT                   RPABC2"
FT                   /id="PRO_0000133796"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          26..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   142 AA;  15729 MW;  FDC4E7AD5B495D79 CRC64;
     MSDYEEDEAF GMDGAVMEEE VDELEMIDEN GQSQQGVSHP GEPSTTVITE DVASSKTAQS
     GKAVAKEDRT TTPYMTKYER ARILGTRALQ ISMNAPVLVD LEGETDPLQI AMKELAQKKI
     PLLVRRYLPD GSYEDWSVAE LI
 
 
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