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UniProtKB/Swiss-Prot entry Q10233


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RPC2_SCHPO
Primary accession number Q10233
Secondary accession number Q0QYE4
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 54)
Name and origin of the protein
Protein name DNA-directed RNA polymerase III subunit RPC2
Synonyms RNA polymerase III subunit C2
RNA polymerase III subunit 2
EC 2.7.7.6
DNA-directed RNA polymerase III 130 kDa polypeptide
RPC130
C128
Gene name
Name: rpc2
ORFNames: SPAC4G9.08c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1093/nar/gkl421; PubMed=16877568 [NCBI, ExPASy, EBI, Israel, Japan]
Proshkina G.M., Shematorova E.K., Proshkin S.A., Zaros C., Thuriaux P., Shpakovski G.V.;
"Ancient origin, functional conservation and fast evolution of DNA-dependent RNA polymerase III.";
Nucleic Acids Res. 34:3615-3624(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
Comments
  • FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity).
  • CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits (By similarity).
  • SUBCELLULAR LOCATION: Nucleus (By similarity).
  • SIMILARITY: Belongs to the RNA polymerase beta chain family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
DQ156226; ABA54854.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAA93558.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T38867; T38867.
RefSeq NP_593690.1; -.
3D structure databases
HSSP P08518; 1I50. [HSSP ENTRY / PDB]
ModBase Q10233.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-001356-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC4G9.08c; -.
Gene expression databases
ArrayExpress Q10233; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005666; Cellular component: DNA-directed RNA polymerase III complex (non-traceable author statement from GeneDB_SPombe).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0003899; Molecular function: DNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006383; Biological process: transcription from RNA polymerase III promoter (non-traceable author statement from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR015712; DNA-dir_RNA_pol_su2.
IPR007120; DNA-dir_RNA_pol_su2_6.
IPR007121; RNA_pol_bsu_CS.
IPR007644; RNA_pol_bsu_protrusion.
IPR007642; RNA_pol_Rpb2_2.
IPR007645; RNA_pol_Rpb2_3.
IPR007646; RNA_pol_Rpb2_4.
IPR007647; RNA_pol_Rpb2_5.
IPR007641; RNA_pol_Rpb2_7.
Graphical view of domain structure.
PANTHER PTHR20856; RNA_pol_I_sub2; 1.
Pfam PF04563; RNA_pol_Rpb2_1; 1.
PF04561; RNA_pol_Rpb2_2; 1.
PF04565; RNA_pol_Rpb2_3; 1.
PF04566; RNA_pol_Rpb2_4; 1.
PF04567; RNA_pol_Rpb2_5; 1.
PF00562; RNA_pol_Rpb2_6; 1.
PF04560; RNA_pol_Rpb2_7; 1.
Pfam graphical view of domain structure.
PROSITE PS01166; RNA_POL_BETA; 1.
ProtoNet Q10233.
Genome annotation databases
GeneID 2543393; -.
KEGG spo:SPAC4G9.08c; -.
NMPDR fig|4896.1.peg.3660; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; Nucleus; Transcription; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1165  1165     DNA-directed RNA polymerase III subunit RPC2. PRO_0000048095
ZN_FING   1111   1126  16     C4-type (By similarity). 
METAL   1111   1111        Zinc (By similarity). 
METAL   1114   1114        Zinc (By similarity). 
METAL   1123   1123        Zinc (By similarity). 
METAL   1126   1126        Zinc (By similarity). 
Sequence information
Length: 1165 AA [This is the length of the unprocessed precursor] Molecular weight: 130238 Da [This is the MW of the unprocessed precursor] CRC64: 6690055F257EC0EB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGVNTAGDPQ KSQPKINKGG IGKDESFGAL FKPVYKGKKL ADPVPTIEDK WQLLPAFLKV 

        70         80         90        100        110        120 
KGLVKQHLDS YNYFVDVDLK KIVQANEKVT SDVEPWFYLK YLDIRVGAPV RTDADAIQAS 

       130        140        150        160        170        180 
ISPHECRLRD LTYGANIYVD IEYTRGKQVV RRRNVPIGRM PVMLRSNKCV LSGKNEMEMA 

       190        200        210        220        230        240 
ALNECPLDPG GYFIVKGTEK VILVQEQLSK NRIIVEAEPK KGLWQASVTS STHERKSKTY 

       250        260        270        280        290        300 
VITKNGKLYL KHNSVADDIP IVVVLKAMGL QSDQEIFELV AGAEASYQDL FAPSIEECAK 

       310        320        330        340        350        360 
LNIYTAQQAL EYIGARVKVN RRAGANRLPP HEEALEVLAA VVLAHINVFN LEFRPKAVYI 

       370        380        390        400        410        420 
GIMARRVLMA MVDPLQVDDR DYVGNKRLEL AGQLLALLFE DLFKKFNSDL KLNIDKVLKK 

       430        440        450        460        470        480 
PHRTQEFDAY NQLTVHSDHI TQGMVRALST GNWSLKRFKM ERAGVTHVLS RLSYISALGM 

       490        500        510        520        530        540 
MTRITSQFEK TRKVSGPRSL QASQFGMLCT SDTPEGEACG LVKNLALMTH ITTDEEEEPI 

       550        560        570        580        590        600 
IKLAYAFGIE DIHVISGREL HSHGTYLVYL NGAILGISRY PSLFVASFRK LRRSGKISPF 

       610        620        630        640        650        660 
IGIFINTHQR AVFISTDGGR ICRPLIIVQN GLPKVESKHI RLLKEGKWGF EDFLKQGLVE 

       670        680        690        700        710        720 
YVDVNEENDS LISVYERDIT PDTTHLEIEP FTILGAVAGL IPYPHHNQSP RNTYQCAMGK 

       730        740        750        760        770        780 
QAIGAIAYNQ LQRIDTLLYL MVYPQQPMVK TKTIELIGYD KLPAGQNATV AIMSYSGYDI 

       790        800        810        820        830        840 
EDALVLNKSS IDRGFGRCQV FHKHSVIVRK YPNGTHDRIG DPQRDPETGE VVWKHGVVED 

       850        860        870        880        890        900 
DGLAGVGCRV QPGQIYVNKQ TPTNALDNSI TLGHTQTVES GYKATPMTYK APEPGYIDKV 

       910        920        930        940        950        960 
MLTTTDSDQT LIKVLMRQTR RPELGDKFSS RHGQKGVCGV IVQQEDMPFN DQGICPDIIM 

       970        980        990       1000       1010       1020 
NPHGFPSRMT VGKMIELLSG KVGVLRGTLE YGTCFGGTKV EDASRILVEH GYNYSGKDML 

      1030       1040       1050       1060       1070       1080 
TSGITGETLE AYIFMGPIYY QKLKHMVMDK MHARARGPRA VLTRQPTEGR SRDGGLRLGE 

      1090       1100       1110       1120       1130       1140 
MERDCLIAYG ASQLLLERLM ISSDACDVDV CGQCGLLGYK GWCNSCQSTR EVVKMTIPYA 

      1150       1160 
AKLLFQELLS MNIVPRLALE DEFKY 

Q10233 in FASTA format

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