[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=(68)-VIII; DOI=10.1093/nar/20.17.4445; PubMed=1408746 [NCBI, ExPASy, EBI, Israel, Japan] Kaufmann J., Klein A.; "Gene dosage as a possible major determinant for equal expression levels of genes encoding RNA polymerase subunits in the hypotrichous ciliate Euplotes octocarinatus."; Nucleic Acids Res. 20:4445-4450(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94. DOI=10.1093/nar/20.22.5985; PubMed=1461731 [NCBI, ExPASy, EBI, Israel, Japan] Kaufmann J., Florian V., Klein A.; "TGA cysteine codons and intron sequences in conserved and nonconserved positions are found in macronuclear RNA polymerase genes of Euplotes octocarinatus."; Nucleic Acids Res. 20:5985-5989(1992).

Comments

FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. RNA polymerase I is essentially used to transcribe ribosomal DNA units.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
SUBUNIT: Each class of RNA polymerase is assembled from 9 to 14 different polypeptides. This subunit is the largest component of RNA polymerase I.
SUBCELLULAR LOCATION: Nucleus.
MISCELLANEOUS: Three distinct zinc-containing RNA polymerases are found in eukaryotic nuclei: polymerase I for the ribosomal RNA precursor, polymerase II for the mRNA precursor, and polymerase III for 5S and tRNA genes.
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

X66450; CAA47066.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S33884; S33884.

3D structure databases

HSSP

P04050; 1K83. [HSSP ENTRY / PDB]

ModBase

P28363.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
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:0006350;	Biological process: transcription (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000722; RNA_pol_A.
IPR006592; RNA_pol_N.
IPR007080; RNA_pol_Rpb1_1.
IPR015699; RNA_polyI.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.40.30; RNA_pol_A; 1.
G3DSA:3.90.1120.10; RNA_pol_Rpb1_1; 1.

PANTHER

PTHR19376:SF11; RNA_polyI; 1.

Pfam

PF04997; RNA_pol_Rpb1_1; 1.
PF00623; RNA_pol_Rpb1_2; 1.
Pfam graphical view of domain structure.

SMART

SM00663; RPOLA_N; 1.
SMART graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; Nucleus; Transcription; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >638`	`>638`	`DNA-directed RNA polymerase I subunit RPA1.`	`PRO_0000073927`
`ZN_FING`	`67 82`	`16`	`C2H2-type (Potential).`
`NON_TER`	`638 638`

Sequence information

Length: 638 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 73299 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: AB82F8BB9C22F5B5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATIFDSLIS SRLDGTRFSF YNDEEIQQMS VKEIHNPMAY DELNNPTSHG ICDESMGVSA 

        70         80         90        100        110        120 
LDKLSKCKTC GCDSVYCPGH MGHIKLTSTC YNPFTMKLLH SLLKSKCLVC HRLRISPKRI 

       130        140        150        160        170        180 
ELFEIRLKLI KLGYLVEAEK LSDFNHFSLE SIDSAIRILR KKTKGKTNKK EEKEDSEEVE 

       190        200        210        220        230        240 
EDKYAAKEAL ENLIQKEKEN REIFYSHISS ILQEDTPNES IGNAITVAIR DITKEIMNSV 

       250        260        270        280        290        300 
VPSKCPHCDV CNPRIKKDGA TKFFQMPLSN RDTKAMLSSH GRIDMRIDIS TMGAISEYDE 

       310        320        330        340        350        360 
EDDESSGESE VREGDEEQEK KQKYLSPIEV LEHMRRLWDV EDTLLNELFD NYKIFFMNNL 

       370        380        390        400        410        420 
LVSQNRFRPE SSGGKQSGDD RDYLHAHSAM LTKIINANIA FRRTIELKEN LTDDRNLETE 

       430        440        450        460        470        480 
SEKSKTQQID LSKTEITSKQ VIKAWAELQE SVNCYLDSSL AAKLENKEKP GLRQLLERKE 

       490        500        510        520        530        540 
GIFRMKMMGK RVNFAGRSVI SPDPYISTDQ IGVPEFIART ITFPEPAKNI EKLKRCVING 

       550        560        570        580        590        600 
AHKHPGANFI EYPNGERKAL ENMTLEEKKQ SSIIRKWRKI VYRHMQTGDP LLVNRQPTLH 

       610        620        630 
KPSIMAHNAI ILPKEQTIRM HYSNCKSYNA DFDGDEMK

P28363 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools