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RPAC2_SCHPO
ID   RPAC2_SCHPO             Reviewed;         125 AA.
AC   Q09177; Q9UUF9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=DNA-directed RNA polymerases I and III subunit RPAC2;
DE            Short=RNA polymerases I and III subunit AC2;
DE   AltName: Full=AC19;
DE   AltName: Full=DNA-directed RNA polymerases I and III 14 kDa polypeptide;
GN   Name=rpc19; Synonyms=rpa17; ORFNames=SPAC1687.01, SPAPYUL23.01;
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 [MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8972853; DOI=10.1093/nar/24.23.4676;
RA   Javerzat J.-P., Cranston G., Allshire R.C.;
RT   "Fission yeast genes which disrupt mitotic chromosome segregation when
RT   overexpressed.";
RL   Nucleic Acids Res. 24:4676-4683(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=10102372; DOI=10.1007/s004380050977;
RA   Imai K., Imazawa Y., Yao Y., Yamamoto K., Hisatake K., Muramatsu M.,
RA   Nogi Y.;
RT   "The fission yeast rpa17+ gene encodes a functional homolog of AC19, a
RT   subunit of RNA polymerases I and III of Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 261:364-373(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10079952;
RA   Shpakovskii G.V., Shematorova E.K.;
RT   "Molecular cloning and characteristics of rpc19+ and rpc40+
RT   Schizosaccharomyces pombe genes, coding for common subunits of nuclear RNA
RT   polymerase I and III.";
RL   Bioorg. Khim. 24:933-937(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10541858; DOI=10.1007/s002940050492;
RA   Shpakovski G.V., Shematorova E.K.;
RT   "Rpc19 and Rpc40, two alpha-like subunits shared by nuclear RNA polymerases
RT   I and III, are interchangeable between the fission and budding yeasts.";
RL   Curr. Genet. 36:208-214(1999).
RN   [5]
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 polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Common core component of RNA polymerases I and III which synthesize
CC       ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs,
CC       respectively.
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I) and RNA polymerase
CC       III (Pol III) complexes consisting of 14 and 17 subunits, respectively.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC       polymerase subunit family. {ECO:0000305}.
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DR   EMBL; U50769; AAC49604.1; -; mRNA.
DR   EMBL; AB013499; BAA33719.1; -; mRNA.
DR   EMBL; AF116919; AAF24657.1; -; Genomic_DNA.
DR   EMBL; AF079779; AAD45538.1; -; mRNA.
DR   EMBL; AB017152; BAA36760.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB50921.1; -; Genomic_DNA.
DR   PIR; T43414; T43414.
DR   RefSeq; NP_593118.2; NM_001018515.2.
DR   PDB; 7AOC; EM; 3.84 A; K=1-125.
DR   PDB; 7AOD; EM; 4.50 A; K/W=1-125.
DR   PDB; 7AOE; EM; 3.90 A; K=1-125.
DR   PDBsum; 7AOC; -.
DR   PDBsum; 7AOD; -.
DR   PDBsum; 7AOE; -.
DR   AlphaFoldDB; Q09177; -.
DR   SMR; Q09177; -.
DR   BioGRID; 279247; 8.
DR   STRING; 4896.SPAC1687.01.1; -.
DR   iPTMnet; Q09177; -.
DR   MaxQB; Q09177; -.
DR   PaxDb; Q09177; -.
DR   EnsemblFungi; SPAC1687.01.1; SPAC1687.01.1:pep; SPAC1687.01.
DR   GeneID; 2542799; -.
DR   KEGG; spo:SPAC1687.01; -.
DR   PomBase; SPAC1687.01; rpc19.
DR   VEuPathDB; FungiDB:SPAC1687.01; -.
DR   eggNOG; KOG3438; Eukaryota.
DR   HOGENOM; CLU_090381_3_0_1; -.
DR   InParanoid; Q09177; -.
DR   OMA; MRIQMYD; -.
DR   PhylomeDB; Q09177; -.
DR   PRO; PR:Q09177; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005736; C:RNA polymerase I 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IGI:PomBase.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; IGI:PomBase.
DR   CDD; cd07029; RNAP_I_III_AC19; 1.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   HAMAP; MF_00261; RNApol_arch_Rpo11; 1.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR009025; RBP11-like_dimer.
DR   InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS.
DR   InterPro; IPR033898; RNAP_AC19.
DR   Pfam; PF13656; RNA_pol_L_2; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   PROSITE; PS01154; RNA_POL_L_13KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleus; Reference proteome;
KW   Transcription.
FT   CHAIN           1..125
FT                   /note="DNA-directed RNA polymerases I and III subunit
FT                   RPAC2"
FT                   /id="PRO_0000149318"
SQ   SEQUENCE   125 AA;  13722 MW;  54EAD1BE07C12439 CRC64;
     MAAMTDVTDP SSVAMESATE KIIILPGHSA DLTSVTFQIQ KEDHTLGNSL RYVIMKNPEV
     EFCGYSIPHP SEAKMNFRIQ TAPSTTAVDV LRKGLDDLID LCDAVTEKFT EQLPRDTSTT
     MEVDG
 
 
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