ID   RPC2_SCHPO              Reviewed;        1165 AA.
AC   Q10233; Q0QYE4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=DNA-directed RNA polymerase III subunit RPC2;
DE            Short=RNA polymerase III subunit 2;
DE            Short=RNA polymerase III subunit C2;
DE            EC=2.7.7.6;
DE   AltName: Full=C128;
DE   AltName: Full=DNA-directed RNA polymerase III 130 kDa polypeptide;
DE   AltName: Full=RPC130;
GN   Name=rpc2; ORFNames=SPAC4G9.08c;
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=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).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Second largest core component of RNA polymerase III which synthesizes
CC       small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the
CC       polymerase catalytic activity and forms the polymerase active center
CC       together with the largest subunit. Pol III is composed of mobile
CC       elements and RPC2 is part of the core element with the central large
CC       cleft and probably a clamp element that moves to open and close the
CC       cleft (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6;
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; DQ156226; ABA54854.1; -; mRNA.
DR   EMBL; CU329670; CAA93558.1; -; Genomic_DNA.
DR   PIR; T38867; T38867.
DR   RefSeq; NP_593690.1; NM_001019122.2.
DR   AlphaFoldDB; Q10233; -.
DR   SMR; Q10233; -.
DR   BioGRID; 279815; 6.
DR   DIP; DIP-29536N; -.
DR   IntAct; Q10233; 3.
DR   STRING; 4896.SPAC4G9.08c.1; -.
DR   iPTMnet; Q10233; -.
DR   MaxQB; Q10233; -.
DR   PaxDb; Q10233; -.
DR   PRIDE; Q10233; -.
DR   EnsemblFungi; SPAC4G9.08c.1; SPAC4G9.08c.1:pep; SPAC4G9.08c.
DR   GeneID; 2543393; -.
DR   KEGG; spo:SPAC4G9.08c; -.
DR   PomBase; SPAC4G9.08c; rpc2.
DR   VEuPathDB; FungiDB:SPAC4G9.08c; -.
DR   eggNOG; KOG0215; Eukaryota.
DR   HOGENOM; CLU_000524_5_1_1; -.
DR   InParanoid; Q10233; -.
DR   OMA; LAYCSWC; -.
DR   PhylomeDB; Q10233; -.
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:Q10233; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; NAS:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006386; P:termination of RNA polymerase III transcription; IMP:PomBase.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007646; RNA_pol_Rpb2_4.
DR   InterPro; IPR007647; RNA_pol_Rpb2_5.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR   Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   2: Evidence at transcript level;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Nucleus; Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1165
FT                   /note="DNA-directed RNA polymerase III subunit RPC2"
FT                   /id="PRO_0000048095"
FT   ZN_FING         1111..1126
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1165 AA;  130238 MW;  6690055F257EC0EB CRC64;
     MGVNTAGDPQ KSQPKINKGG IGKDESFGAL FKPVYKGKKL ADPVPTIEDK WQLLPAFLKV
     KGLVKQHLDS YNYFVDVDLK KIVQANEKVT SDVEPWFYLK YLDIRVGAPV RTDADAIQAS
     ISPHECRLRD LTYGANIYVD IEYTRGKQVV RRRNVPIGRM PVMLRSNKCV LSGKNEMEMA
     ALNECPLDPG GYFIVKGTEK VILVQEQLSK NRIIVEAEPK KGLWQASVTS STHERKSKTY
     VITKNGKLYL KHNSVADDIP IVVVLKAMGL QSDQEIFELV AGAEASYQDL FAPSIEECAK
     LNIYTAQQAL EYIGARVKVN RRAGANRLPP HEEALEVLAA VVLAHINVFN LEFRPKAVYI
     GIMARRVLMA MVDPLQVDDR DYVGNKRLEL AGQLLALLFE DLFKKFNSDL KLNIDKVLKK
     PHRTQEFDAY NQLTVHSDHI TQGMVRALST GNWSLKRFKM ERAGVTHVLS RLSYISALGM
     MTRITSQFEK TRKVSGPRSL QASQFGMLCT SDTPEGEACG LVKNLALMTH ITTDEEEEPI
     IKLAYAFGIE DIHVISGREL HSHGTYLVYL NGAILGISRY PSLFVASFRK LRRSGKISPF
     IGIFINTHQR AVFISTDGGR ICRPLIIVQN GLPKVESKHI RLLKEGKWGF EDFLKQGLVE
     YVDVNEENDS LISVYERDIT PDTTHLEIEP FTILGAVAGL IPYPHHNQSP RNTYQCAMGK
     QAIGAIAYNQ LQRIDTLLYL MVYPQQPMVK TKTIELIGYD KLPAGQNATV AIMSYSGYDI
     EDALVLNKSS IDRGFGRCQV FHKHSVIVRK YPNGTHDRIG DPQRDPETGE VVWKHGVVED
     DGLAGVGCRV QPGQIYVNKQ TPTNALDNSI TLGHTQTVES GYKATPMTYK APEPGYIDKV
     MLTTTDSDQT LIKVLMRQTR RPELGDKFSS RHGQKGVCGV IVQQEDMPFN DQGICPDIIM
     NPHGFPSRMT VGKMIELLSG KVGVLRGTLE YGTCFGGTKV EDASRILVEH GYNYSGKDML
     TSGITGETLE AYIFMGPIYY QKLKHMVMDK MHARARGPRA VLTRQPTEGR SRDGGLRLGE
     MERDCLIAYG ASQLLLERLM ISSDACDVDV CGQCGLLGYK GWCNSCQSTR EVVKMTIPYA
     AKLLFQELLS MNIVPRLALE DEFKY