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RPC9_SCHPO
ID   RPC9_SCHPO              Reviewed;         129 AA.
AC   Q9C0Z9;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=DNA-directed RNA polymerase III subunit rpc9;
DE            Short=RNA polymerase III subunit C9;
DE   AltName: Full=RNA polymerase III subunit C17;
GN   Name=rpc17; ORFNames=SPAPB1E7.10;
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], AND FUNCTION.
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   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 tRNAs. {ECO:0000269|PubMed:16877568}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RPC9 RNA polymerase subunit
CC       family. {ECO:0000305}.
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DR   EMBL; DQ156220; ABA54848.1; -; mRNA.
DR   EMBL; CU329670; CAC36927.1; -; Genomic_DNA.
DR   RefSeq; NP_594136.1; NM_001019560.2.
DR   PDB; 3AYH; X-ray; 2.19 A; A=1-129.
DR   PDBsum; 3AYH; -.
DR   AlphaFoldDB; Q9C0Z9; -.
DR   SMR; Q9C0Z9; -.
DR   BioGRID; 280067; 4.
DR   STRING; 4896.SPAPB1E7.10.1; -.
DR   MaxQB; Q9C0Z9; -.
DR   PaxDb; Q9C0Z9; -.
DR   EnsemblFungi; SPAPB1E7.10.1; SPAPB1E7.10.1:pep; SPAPB1E7.10.
DR   GeneID; 2543653; -.
DR   KEGG; spo:SPAPB1E7.10; -.
DR   PomBase; SPAPB1E7.10; rpc17.
DR   VEuPathDB; FungiDB:SPAPB1E7.10; -.
DR   eggNOG; KOG4168; Eukaryota.
DR   HOGENOM; CLU_092529_3_1_1; -.
DR   InParanoid; Q9C0Z9; -.
DR   OMA; VMIINLR; -.
DR   PhylomeDB; Q9C0Z9; -.
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:Q9C0Z9; -.
DR   Proteomes; UP000002485; Chromosome I.
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; IGI:PomBase.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IGI:PomBase.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IGI:PomBase.
DR   Gene3D; 1.20.1250.40; -; 1.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR006590; RNA_pol_Rpb4/RPC9_core.
DR   InterPro; IPR005574; Rpb4/RPC9.
DR   InterPro; IPR038324; Rpb4/RPC9_sf.
DR   InterPro; IPR038846; RPC9.
DR   PANTHER; PTHR15561; PTHR15561; 1.
DR   Pfam; PF03874; RNA_pol_Rpb4; 1.
DR   SMART; SM00657; RPOL4c; 1.
DR   SUPFAM; SSF47819; SSF47819; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA-directed RNA polymerase; Nucleus;
KW   Reference proteome; Transcription.
FT   CHAIN           1..129
FT                   /note="DNA-directed RNA polymerase III subunit rpc9"
FT                   /id="PRO_0000352805"
FT   STRAND          2..11
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   HELIX           13..34
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   HELIX           35..38
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   HELIX           43..57
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   HELIX           67..75
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   TURN            76..80
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   HELIX           84..93
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   HELIX           98..104
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   HELIX           108..112
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   TURN            113..116
FT                   /evidence="ECO:0007829|PDB:3AYH"
FT   HELIX           117..127
FT                   /evidence="ECO:0007829|PDB:3AYH"
SQ   SEQUENCE   129 AA;  14927 MW;  E51BA8A9525EC2BA CRC64;
     MKVLEARDAY LTNAEVFFHL KEMENEQNAR TQERGAAQAL VCENLRTIQF EILKYLSSQG
     NCEGLTKERF LDCIAIFNEF ELTKAEILVI LNNKPSSVPE LYACIEGIEE RFKEEDIFKL
     VEKINTTFP
 
 
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