Legends: 1, Magnesium; catalytic. {ECO:0000250}; 2, REGION Bridging helix. {ECO:0000250}; 3, ipfam:RNA_pol_Rpb1_4 [T]; 4, ipfam:RNA_pol_Rpb1_2 [T]; 5, ipfam:RNA_pol_Rpb1_3 [T]; 6, ipfam:RNA_pol_Rpb1_1 [T].
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ID RPA1_RAT Reviewed; 1716 AA.
AC O54889;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 30-NOV-2016, entry version 113.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA1;
DE Short=RNA polymerase I subunit A1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase I largest subunit;
DE AltName: Full=DNA-directed RNA polymerase I subunit A;
DE AltName: Full=RNA polymerase I 194 kDa subunit;
DE Short=A194;
DE Short=RPA194;
GN Name=Polr1a; Synonyms=Rpa1, Rpo1-4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE RNA POL I COMPLEX,
RP AND PHOSPHORYLATION.
RX PubMed=9422795; DOI=10.1074/jbc.273.2.1257;
RA Hannan R.D., Hempel W.M., Cavanaugh A., Arino T., Dimitrov S.I.,
RA Moss T., Rothblum L.;
RT "Affinity purification of mammalian RNA polymerase I. Identification
RT of an associated kinase.";
RL J. Biol. Chem. 273:1257-1267(1998).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Largest and catalytic core component of RNA polymerase
CC I which synthesizes ribosomal RNA precursors. Forms the polymerase
CC active center together with the second largest subunit. A single
CC stranded DNA template strand of the promoter is positioned within
CC the central active site cleft of Pol I. A bridging helix emanates
CC from RPA1 and crosses the cleft near the catalytic site and is
CC thought to promote translocation of Pol I by acting as a ratchet
CC that moves the RNA-DNA hybrid through the active site by switching
CC from straight to bent conformations at each step of nucleotide
CC addition (By similarity). {ECO:0000250|UniProtKB:P10964}.
CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC + RNA(n+1).
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex
CC consisting of at least 13 subunits (PubMed:9422795). Interacts
CC with MYO1C (By similarity). Interacts with ERBB2 (By similarity).
CC Interacts with DDX11 (By similarity).
CC {ECO:0000250|UniProtKB:O35134, ECO:0000250|UniProtKB:O95602,
CC ECO:0000269|PubMed:9422795}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:9422795}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
DR EMBL; AF025425; AAB94601.1; -; mRNA.
DR PIR; T14103; T14103.
DR RefSeq; NP_113960.1; NM_031772.1.
DR UniGene; Rn.24877; -.
DR ProteinModelPortal; O54889; -.
DR MINT; MINT-1507847; -.
DR STRING; 10116.ENSRNOP00000013587; -.
DR PhosphoSitePlus; O54889; -.
DR PaxDb; O54889; -.
DR PRIDE; O54889; -.
DR GeneID; 83581; -.
DR KEGG; rno:83581; -.
DR UCSC; RGD:620824; rat.
DR CTD; 25885; -.
DR RGD; 620824; Polr1a.
DR eggNOG; KOG0262; Eukaryota.
DR eggNOG; COG0086; LUCA.
DR HOGENOM; HOG000205401; -.
DR HOVERGEN; HBG017741; -.
DR InParanoid; O54889; -.
DR KO; K02999; -.
DR PhylomeDB; O54889; -.
DR PRO; PR:O54889; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005736; C:DNA-directed RNA polymerase I complex; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009303; P:rRNA transcription; IDA:RGD.
DR GO; GO:0006360; P:transcription from RNA polymerase I promoter; IEA:GOC.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 4.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW Complete proteome; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1 1716 DNA-directed RNA polymerase I subunit
FT RPA1.
FT /FTId=PRO_0000073925.
FT REGION 968 980 Bridging helix. {ECO:0000250}.
FT METAL 64 64 Zinc. {ECO:0000250}.
FT METAL 67 67 Zinc. {ECO:0000250}.
FT METAL 74 74 Zinc. {ECO:0000250}.
FT METAL 77 77 Zinc. {ECO:0000250}.
FT METAL 595 595 Magnesium; catalytic. {ECO:0000250}.
FT METAL 597 597 Magnesium; catalytic. {ECO:0000250}.
FT METAL 599 599 Magnesium; catalytic. {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 851 958 ipfam:RNA_pol_Rpb1_4 [T]
FT MYHIT 302 649 ismart:RPOLA_N [T]
FT MYHIT 441 620 ipfam:RNA_pol_Rpb1_2 [T]
FT MYHIT 624 809 ipfam:RNA_pol_Rpb1_3 [T]
FT MYHIT 11 356 ipfam:RNA_pol_Rpb1_1 [T]
FT MYHIT 965 1664 ipfam:RNA_pol_Rpb1_5 [T]
SQ SEQUENCE 1716 AA; 194192 MW; E8EE15BC23E60941 CRC64;
MLASKHTPWR RLQGISFGMY SAEELKKLSV KSITNPRYVD SLGNPSADGL YDLALGPADS
KEVCSTCVQD FNNCSGHLGH IDLPLTVYNP LLFDKLYLLL RGSCLNCHML TCPRAAIHLL
VCQLKVLDVG ALQAVYELER ILSRFLEETS DPSAFEIQEE LEEYTSKILQ NNLLGSQGAH
VKNVCESRSK LVAHFWKTHM AAKRCPHCKT GRSVVRKEHN SKLTITYPAM VHKKSGQKDA
ELPEGAPAAP GIDEAQMGKR GYLTPSSAQE HLFAIWKNEG FFLNYLFSGL DDIGPESSFN
PSMFFLDFIV VPPSRYRPIN RLGDQMFTNG QTVNLQAVMK DAVLIRKLLA VMAQEQKLPC
EMTEITIDKE NDSSGAIDRS FLSLLPGQSL TDKLYNIWIR LQSHVNIVFD SDMDKLMLEK
YPGIRQILEK KEGLFRKHMM GKRVDYAARS VICPDMYINT NEIGIPMVFA TKLTYPQPVT
PWNVQELRQA VINGPNVHPG ASMVINEDGS RTALSAVDAT QREAVAKQLL TPSTGIPKPQ
GAKVVCRHVK NGDILLLNRQ PTLHRPSIQA HRAHILPEEK VLRLHYANCK AYNADFDGDE
MNAHFPQSEL GRAEAYVLAC TDQQYLVPKD GQPLAGLIQD HMVSGANMTI RGCFFTREQY
MELVYRGLTD KVGRVKLFPP AILKPFPLWT GKQVVSTLLI NIIPEDYTPL NLTGKAKIGS
KAWVKEKPRP VPDFDPDSMC ESQVIIREGE LLCGVLDKAH YGSSAYGLVH CCYEIYGGET
SGRVLTCLAR LFTAYLQLYR GFTLGVEDIL VKPNADVMRQ RIIEESTQCG PRAVRAALNL
PEAASCDEIQ GKWQDAIWRK DQRDFNMIDM KFKEEVNHYS NEINKACMPF GLHRQFPENN
LQMMVQSGAK GSTVNTMQIS CLLGQIELEG RRPPLMASGK SLPCFEPYEF TPRAGGFVTG
RFLTGIRPPE FFFHCMAGRE GLVDTAVKTS RSGYLQRCII KHLEGLVIQY DLTVRDSDGS
VVQFLYGEDG LDIPKTQFLQ PKQFPFLASN YEVIMKSKHL HEVLSRADPQ KVLRHFRAIK
KWHHRHSSAL LRKGAFLSFS QKIQAAVKAL NLEGKTQNGR SPETQQMLQM WHELDEQSRR
KYQKRAAPCP DPSLSVWRPD IHFASVSETF EKKIDDYSQE WAAQAEKSHN RSELSLDRLR
TLLQLKWQRS LCDPGEAVGL LAAQSIGEPS TQMTLNTFHF AGRGEMNVTL GIPRLREILM
VASANIKTPM MSVPVFNTKK ALRRVKSLKK QLTRVCLGEV LQKVDIQESF CMGEKQNKFR
VYELRFQFLP HAYYQQEKCL RPEDILHFME TRFFKLLMEA IKKKNSKASA FRSVNTRRAT
QKDLDDTEDS GRNRREEERD EEEEGNIVDA EAEEGDADAS DTKRKEKQEE EVDYESEEEG
EEEEEEDVQE EENIKGEGAH QTHEPDEEEG SGLEEESSQN PPCRHSRPQG AEAMERRIQA
VRESHSFIED YQYDTEESLW CQVTVKLPLM KINFDMSSLV VSLAHNAIVY TTKGITRCLL
NETINSKNEK EFVLNTEGIN LPELFKYSEV LDLRRLYSND IHAVANTYGI EAALRVIEKE
IKDVFAVYGI AVDPRHLSLV ADYMCFEGVY KPLNRFGIQS SSSPLQQMTF ETSFQFLKQA
TMMGSHDELK SPSACLVVGK VVKGGTGLFE LKQPLR
//
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