RPC8_SCHPO
ID RPC8_SCHPO Reviewed; 203 AA.
AC O94285;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DNA-directed RNA polymerase III subunit rpc8;
DE Short=RNA polymerase III subunit C8;
DE AltName: Full=RNA polymerase III subunit C25;
GN Name=rpc25; ORFNames=SPBC2G5.07c;
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], FUNCTION, AND IDENTIFICATION IN THE RNA
RP POLYMERASE III COMPLEX.
RC STRAIN=972 / ATCC 24843;
RX PubMed=16877568; DOI=10.1093/nar/gkl421;
RA Proshkina G.M., Shematorova E.K., Proshkin S.A., Zaros C., Thuriaux P.,
RA Shpakovski G.V.;
RT "Ancient origin, functional conservation and fast evolution of DNA-
RT dependent RNA polymerase III.";
RL Nucleic Acids Res. 34:3615-3624(2006).
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 FUNCTION.
RX PubMed=15612920; DOI=10.1111/j.1365-2958.2004.04375.x;
RA Zaros C., Thuriaux P.;
RT "Rpc25, a conserved RNA polymerase III subunit, is critical for
RT transcription initiation.";
RL Mol. Microbiol. 55:104-114(2005).
RN [4]
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: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific peripheric component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNA. {ECO:0000269|PubMed:15612920,
CC ECO:0000269|PubMed:16877568}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. Rpc25/rpc8 and rpc17/rpc9 form a Pol III
CC subcomplex. {ECO:0000269|PubMed:16877568}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; DQ156221; ABA54849.1; -; mRNA.
DR EMBL; CU329671; CAA21883.1; -; Genomic_DNA.
DR PIR; T40164; T40164.
DR RefSeq; NP_596068.1; NM_001021979.2.
DR PDB; 3AYH; X-ray; 2.19 A; B=1-203.
DR PDBsum; 3AYH; -.
DR AlphaFoldDB; O94285; -.
DR SMR; O94285; -.
DR BioGRID; 277038; 6.
DR STRING; 4896.SPBC2G5.07c.1; -.
DR MaxQB; O94285; -.
DR PaxDb; O94285; -.
DR EnsemblFungi; SPBC2G5.07c.1; SPBC2G5.07c.1:pep; SPBC2G5.07c.
DR PomBase; SPBC2G5.07c; rpc25.
DR VEuPathDB; FungiDB:SPBC2G5.07c; -.
DR eggNOG; KOG3297; Eukaryota.
DR HOGENOM; CLU_073901_1_1_1; -.
DR InParanoid; O94285; -.
DR OMA; LGPTLWW; -.
DR PhylomeDB; O94285; -.
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 PRO; PR:O94285; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005666; C:RNA polymerase III complex; ISO: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:0006384; P:transcription initiation from RNA polymerase III promoter; ISO:PomBase.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013238; RNA_pol_III_Rbc25.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR004519; RNAP_E/RPC8.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR PANTHER; PTHR12709; PTHR12709; 1.
DR Pfam; PF08292; RNA_pol_Rbc25; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
DR TIGRFAMs; TIGR00448; rpoE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase; Nucleus;
KW Reference proteome; Transcription.
FT CHAIN 1..203
FT /note="DNA-directed RNA polymerase III subunit rpc8"
FT /id="PRO_0000362999"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:3AYH"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3AYH"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3AYH"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:3AYH"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3AYH"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3AYH"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:3AYH"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:3AYH"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3AYH"
SQ SEQUENCE 203 AA; 23243 MW; 61BFA0A832E76333 CRC64;
MFLLSRFSDI ISIHPSNFWK PTKEALAEEI HKKYANKVIQ NIGLAICVYD FLKIGEGIIK
YGDGSSYMNV VFRLIIFRPF RGEVMLGKIK SCSEEGIRVT ISFFDDIFIP KDMLFDPCVF
RPDERAWVWK IEGEDGSEGT ELYFDIDEEI RFQIESEDFV DISPKRNKNA TAITGTEALE
SVSPYTLIAS CSRDGLGIPA WWK
