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O54889 (RPA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase I subunit RPA1
Short name=RNA polymerase I subunit A1
EC=2.7.7.6
Alternative name(s):
DNA-directed RNA polymerase I largest subunit
DNA-directed RNA polymerase I subunit A
RNA polymerase I 194 kDa subunit
Short name=A194
Short name=RPA194
Gene names
Name:Polr1a
Synonyms:Rpa1, Rpo1-4
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1716 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition By similarity.

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Subunit structure

Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. Interacts with MYO1C. Interacts with ERBB2 By similarity.

Subcellular location

Nucleus › nucleolus By similarity.

Post-translational modification

Phosphorylated. Ref.1

Sequence similarities

Belongs to the RNA polymerase beta' chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17161716DNA-directed RNA polymerase I subunit RPA1
PRO_0000073925

Regions

Region968 – 98013Bridging helix By similarity

Sites

Metal binding641Zinc By similarity
Metal binding671Zinc By similarity
Metal binding741Zinc By similarity
Metal binding771Zinc By similarity
Metal binding5951Magnesium; catalytic By similarity
Metal binding5971Magnesium; catalytic By similarity
Metal binding5991Magnesium; catalytic By similarity

Amino acid modifications

Modified residue15761Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
O54889 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: E8EE15BC23E60941

FASTA1,716194,192
        10         20         30         40         50         60 
MLASKHTPWR RLQGISFGMY SAEELKKLSV KSITNPRYVD SLGNPSADGL YDLALGPADS 

        70         80         90        100        110        120 
KEVCSTCVQD FNNCSGHLGH IDLPLTVYNP LLFDKLYLLL RGSCLNCHML TCPRAAIHLL 

       130        140        150        160        170        180 
VCQLKVLDVG ALQAVYELER ILSRFLEETS DPSAFEIQEE LEEYTSKILQ NNLLGSQGAH 

       190        200        210        220        230        240 
VKNVCESRSK LVAHFWKTHM AAKRCPHCKT GRSVVRKEHN SKLTITYPAM VHKKSGQKDA 

       250        260        270        280        290        300 
ELPEGAPAAP GIDEAQMGKR GYLTPSSAQE HLFAIWKNEG FFLNYLFSGL DDIGPESSFN 

       310        320        330        340        350        360 
PSMFFLDFIV VPPSRYRPIN RLGDQMFTNG QTVNLQAVMK DAVLIRKLLA VMAQEQKLPC 

       370        380        390        400        410        420 
EMTEITIDKE NDSSGAIDRS FLSLLPGQSL TDKLYNIWIR LQSHVNIVFD SDMDKLMLEK 

       430        440        450        460        470        480 
YPGIRQILEK KEGLFRKHMM GKRVDYAARS VICPDMYINT NEIGIPMVFA TKLTYPQPVT 

       490        500        510        520        530        540 
PWNVQELRQA VINGPNVHPG ASMVINEDGS RTALSAVDAT QREAVAKQLL TPSTGIPKPQ 

       550        560        570        580        590        600 
GAKVVCRHVK NGDILLLNRQ PTLHRPSIQA HRAHILPEEK VLRLHYANCK AYNADFDGDE 

       610        620        630        640        650        660 
MNAHFPQSEL GRAEAYVLAC TDQQYLVPKD GQPLAGLIQD HMVSGANMTI RGCFFTREQY 

       670        680        690        700        710        720 
MELVYRGLTD KVGRVKLFPP AILKPFPLWT GKQVVSTLLI NIIPEDYTPL NLTGKAKIGS 

       730        740        750        760        770        780 
KAWVKEKPRP VPDFDPDSMC ESQVIIREGE LLCGVLDKAH YGSSAYGLVH CCYEIYGGET 

       790        800        810        820        830        840 
SGRVLTCLAR LFTAYLQLYR GFTLGVEDIL VKPNADVMRQ RIIEESTQCG PRAVRAALNL 

       850        860        870        880        890        900 
PEAASCDEIQ GKWQDAIWRK DQRDFNMIDM KFKEEVNHYS NEINKACMPF GLHRQFPENN 

       910        920        930        940        950        960 
LQMMVQSGAK GSTVNTMQIS CLLGQIELEG RRPPLMASGK SLPCFEPYEF TPRAGGFVTG 

       970        980        990       1000       1010       1020 
RFLTGIRPPE FFFHCMAGRE GLVDTAVKTS RSGYLQRCII KHLEGLVIQY DLTVRDSDGS 

      1030       1040       1050       1060       1070       1080 
VVQFLYGEDG LDIPKTQFLQ PKQFPFLASN YEVIMKSKHL HEVLSRADPQ KVLRHFRAIK 

      1090       1100       1110       1120       1130       1140 
KWHHRHSSAL LRKGAFLSFS QKIQAAVKAL NLEGKTQNGR SPETQQMLQM WHELDEQSRR 

      1150       1160       1170       1180       1190       1200 
KYQKRAAPCP DPSLSVWRPD IHFASVSETF EKKIDDYSQE WAAQAEKSHN RSELSLDRLR 

      1210       1220       1230       1240       1250       1260 
TLLQLKWQRS LCDPGEAVGL LAAQSIGEPS TQMTLNTFHF AGRGEMNVTL GIPRLREILM 

      1270       1280       1290       1300       1310       1320 
VASANIKTPM MSVPVFNTKK ALRRVKSLKK QLTRVCLGEV LQKVDIQESF CMGEKQNKFR 

      1330       1340       1350       1360       1370       1380 
VYELRFQFLP HAYYQQEKCL RPEDILHFME TRFFKLLMEA IKKKNSKASA FRSVNTRRAT 

      1390       1400       1410       1420       1430       1440 
QKDLDDTEDS GRNRREEERD EEEEGNIVDA EAEEGDADAS DTKRKEKQEE EVDYESEEEG 

      1450       1460       1470       1480       1490       1500 
EEEEEEDVQE EENIKGEGAH QTHEPDEEEG SGLEEESSQN PPCRHSRPQG AEAMERRIQA 

      1510       1520       1530       1540       1550       1560 
VRESHSFIED YQYDTEESLW CQVTVKLPLM KINFDMSSLV VSLAHNAIVY TTKGITRCLL 

      1570       1580       1590       1600       1610       1620 
NETINSKNEK EFVLNTEGIN LPELFKYSEV LDLRRLYSND IHAVANTYGI EAALRVIEKE 

      1630       1640       1650       1660       1670       1680 
IKDVFAVYGI AVDPRHLSLV ADYMCFEGVY KPLNRFGIQS SSSPLQQMTF ETSFQFLKQA 

      1690       1700       1710 
TMMGSHDELK SPSACLVVGK VVKGGTGLFE LKQPLR

« Hide

References

[1]"Affinity purification of mammalian RNA polymerase I. Identification of an associated kinase."
Hannan R.D., Hempel W.M., Cavanaugh A., Arino T., Dimitrov S.I., Moss T., Rothblum L.
J. Biol. Chem. 273:1257-1267(1998) [PubMed: 9422795] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE RNA POL I COMPLEX, PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF025425 mRNA. Translation: AAB94601.1.
IPIIPI00199160.
PIRT14103.
RefSeqNP_113960.1. NM_031772.1.
UniGeneRn.24877.

3D structure databases

ProteinModelPortalO54889.
ModBaseSearch...

Protein-protein interaction databases

STRINGO54889.

PTM databases

PhosphoSiteO54889.

Proteomic databases

PRIDEO54889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83581.
KEGGrno:83581.
UCSCNM_031772. rat.

Organism-specific databases

CTD25885.
RGD620824. Polr1a.

Phylogenomic databases

eggNOGroNOG13453.
HOVERGENHBG017741.
InParanoidO54889.
OrthoDBEOG41VK23.
PhylomeDBO54889.

Gene expression databases

ArrayExpressO54889.
GenevestigatorO54889.

Family and domain databases

InterProIPR015699. DNA-dir_RNA_pol1_lsu.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
KOK02999.
PANTHERPTHR19376:SF11. RNA_polyI. 1 hit.
PfamPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTSM00663. RPOLA_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616111.

Entry information

Entry nameRPA1_RAT
AccessionPrimary (citable) accession number: O54889
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents