Polr1a
entrez
83581
canonical
uniprot
O54889
canonical
ensembl
ENSRNOG00000009545
resolver
ensp
ENSRNOP00000013587
resolver
enst
ENSRNOT00000013587
resolver
genesymbol
Polr1a
resolver
genesymbol_syn
Rpa1
resolver
genesymbol_syn
Rpo1-4
resolver
uniprot
G3V7B7
resolver
uniprot_entry
G3V7B7_RAT
resolver
uniprot_entry
RPA1_RAT
resolver
amino_acid_sequence
MLASKHTPWRRLQGISFGMYSAEELKKLSVKSITNPRYVDSLGNPSADGLYDLALGPADSKEVCSTCVQDFNNCSGHLGHIDLPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAAIHLLVCQLKVLDVGALQAVYELERILSRFLEETSDPSAFEIQEELEEYTSKILQNNLLGSQGAHVKNVCESRSKLVAHFWKTHMAAKRCPHCKTGRSVVRKEHNSKLTITYPAMVHKKSGQKDAELPEGAPAAPGIDEAQMGKRGYLTPSSAQEHLFAIWKNEGFFLNYLFSGLDDIGPESSFNPSMFFLDFIVVPPSRYRPINRLGDQMFTNGQTVNLQAVMKDAVLIRKLLAVMAQEQKLPCEMTEITIDKENDSSGAIDRSFLSLLPGQSLTDKLYNIWIRLQSHVNIVFDSDMDKLMLEKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSAVDATQREAVAKQLLTPSTGIPKPQGAKVVCRHVKNGDILLLNRQPTLHRPSIQAHRAHILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGANMTIRGCFFTREQYMELVYRGLTDKVGRVKLFPPAILKPFPLWTGKQVVSTLLINIIPEDYTPLNLTGKAKIGSKAWVKEKPRPVPDFDPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGRVLTCLARLFTAYLQLYRGFTLGVEDILVKPNADVMRQRIIEESTQCGPRAVRAALNLPEAASCDEIQGKWQDAIWRKDQRDFNMIDMKFKEEVNHYSNEINKACMPFGLHRQFPENNLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIRPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVIQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLASNYEVIMKSKHLHEVLSRADPQKVLRHFRAIKKWHHRHSSALLRKGAFLSFSQKIQAAVKALNLEGKTQNGRSPETQQMLQMWHELDEQSRRKYQKRAAPCPDPSLSVWRPDIHFASVSETFEKKIDDYSQEWAAQAEKSHNRSELSLDRLRTLLQLKWQRSLCDPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVFNTKKALRRVKSLKKQLTRVCLGEVLQKVDIQESFCMGEKQNKFRVYELRFQFLPHAYYQQEKCLRPEDILHFMETRFFKLLMEAIKKKNSKASAFRSVNTRRATQKDLDDTEDSGRNRREEERDEEEEGNIVDAEAEEGDADASDTKRKEKQEEEVDYESEEEGEEEEEEDVQEEENIKGEGAHQTHEPDEEEGSGLEEESSQNPPCRHSRPQGAEAMERRIQAVRESHSFIEDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHNAIVYTTKGITRCLLNETINSKNEKEFVLNTEGINLPELFKYSEVLDLRRLYSNDIHAVANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIQSSSSPLQQMTFETSFQFLKQATMMGSHDELKSPSACLVVGKVVKGGTGLFELKQPLR
uniprot
proteins
ec_number
2.7.7.6
uniprot
proteins
function
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (By similarity). Pol I-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol I pre-initiation complex (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex bound to the core promoter that precedes an rDNA repeat unit. The PIC assembly bends the promoter favoring the formation of the transcription bubble and promoter escape. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Highly processive, assembles in structures referred to as 'Miller trees' where many elongating Pol I complexes queue and transcribe the same rDNA coding regions. At terminator sequences downstream of the rDNA gene, PTRF interacts with Pol I and halts Pol I transcription leading to the release of the RNA transcript and polymerase from the DNA (By similarity). Forms Pol I active center together with the second largest subunit POLR1B/RPA2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and the template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. Has proofreading activity: Pauses and backtracks to allow the cleavage of a missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity is associated with decreased transcription fidelity (By similarity). {ECO:0000250|UniProtKB:O95602, ECO:0000250|UniProtKB:P10964}.
uniprot
proteins
mass_dalton
194192
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. {ECO:0000269|PubMed:9422795}.
uniprot
proteins
protein_family
RNA polymerase beta' chain family
uniprot
proteins
pubmed
9422795
uniprot
proteins
sequence_length
1716
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O95602}. Chromosome {ECO:0000250|UniProtKB:O35134}.
uniprot
proteins