ID   RPA1_TRYBB              Reviewed;        1744 AA.
AC   P16355;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-SEP-2026, entry version 116.
DE   RecName: Full=DNA-directed RNA polymerase I subunit RPA1;
DE            Short=TbRPA1;
DE            EC=2.7.7.6;
DE   AltName: Full=DNA-directed RNA polymerase I largest subunit;
GN   Name=TRP11;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=427;
RX   PubMed=2542092; DOI=10.1016/0014-5793(89)80029-8;
RA   Jess W., Hammer A., Cornelissen A.W.C.A.;
RT   "Complete sequence of the gene encoding the largest subunit of RNA
RT   polymerase I of Trypanosoma brucei.";
RL   FEBS Lett. 249:123-128(1989).
RN   [2]
RP   ERRATUM OF PUBMED:2542092, AND SEQUENCE REVISION.
RA   Jess W., Hammer A., Cornelissen A.W.C.A.;
RL   FEBS Lett. 258:180-180(1989).
RN   [3]
RP   IDENTIFICATION IN THE RNA POL I COMPLEX, AND PHOSPHORYLATION.
RX   PubMed=15664659; DOI=10.1016/j.molbiopara.2004.11.014;
RA   Walgraffe D., Devaux S., Lecordier L., Dierick J.F., Dieu M.,
RA   Van den Abbeele J., Pays E., Vanhamme L.;
RT   "Characterization of subunits of the RNA polymerase I complex in
RT   Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 139:249-260(2005).
RN   [4]
RP   IDENTIFICATION IN THE RNA POL I COMPLEX.
RX   PubMed=16730080; DOI=10.1016/j.molbiopara.2006.02.023;
RA   Nguyen T.N., Schimanski B., Zahn A., Klumpp B., Gunzl A.;
RT   "Purification of an eight subunit RNA polymerase I complex in Trypanosoma
RT   brucei.";
RL   Mol. Biochem. Parasitol. 149:27-37(2006).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Largest and catalytic core component of RNA polymerase I which
CC       synthesizes ribosomal RNA precursors. Forms the polymerase active
CC       center together with the second largest subunit. A single stranded DNA
CC       template strand of the promoter is positioned within the central active
CC       site cleft of Pol I. A bridging helix emanates from RPA1 and crosses
CC       the cleft near the catalytic site and is thought to promote
CC       translocation of Pol I by acting as a ratchet that moves the RNA-DNA
CC       hybrid through the active site by switching from straight to bent
CC       conformations at each step of nucleotide addition (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6;
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC       of at least 13 subunits. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P16355; Q381Y8: Tb11.01.6090; Xeno; NbExp=3; IntAct=EBI-8549756, EBI-8549776;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15664659}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000305}.
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DR   EMBL; X14399; CAA32572.1; -; Genomic_DNA.
DR   AlphaFoldDB; P16355; -.
DR   SMR; P16355; -.
DR   IntAct; P16355; 2.
DR   MINT; P16355; -.
DR   GO; GO:0005736; C:RNA polymerase I complex; IEA:TreeGrafter.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd01435; RNAP_I_RPA1_N; 1.
DR   FunFam; 2.40.40.20:FF:000019; DNA-directed RNA polymerase II subunit RPB1; 1.
DR   FunFam; 1.10.274.100:FF:000012; DNA-directed RNA polymerase subunit; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 6.10.250.2940; -; 1.
DR   Gene3D; 6.20.50.80; -; 1.
DR   Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR   InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   1: Evidence at protein level;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..1744
FT                   /note="DNA-directed RNA polymerase I subunit RPA1"
FT                   /id="PRO_0000073928"
FT   REGION          953..965
FT                   /note="Bridging helix"
FT                   /evidence="ECO:0000250"
FT   REGION          1333..1484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1354
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1366..1376
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1464..1478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         597
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         599
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         601
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1744 AA;  191769 MW;  5D1D2C6C7B89229F CRC64;
     MSGIAFVEVR TRAGQEDRSA PWRPVVRNGE NHATFYDTRM GNFDANPFPP QTCQTCAASL
     TGKYGNERCH GHFGFVGMPR IRPGSAHSDS DRLVVLNPHL AMDADRLFRA KCFFCHKFRA
     PTFDVERFRQ ALVLADHGLP GDALHLLDTV PTAKGHDAML NHRRMANEEI VNDVSILQSY
     VDRILRQRAS GCSEEDAKAR VTMAQKGTVD VRNDICNMAI SHLRSFSGPC SHCTAISPTF
     LKRGGIIFFL FRKSNLVTNI AKGFLTQQEV SEWEAVNRLH GRTGTYFDGR QMLFHMKNLF
     AKEQAILGLL YPNLGEPSVF TKTNKVVPAS ERYKLFFLDR ILVPPLPLRL SSGVRVNDNG
     LIIPDEQTRA LSDILGFVEQ IECFHTLSAN STNGRSFITD AQRAVNESNL RNLQQKVDEF
     YAEIVNSFAK KEGLFRMNMM GKRVNQACRS VISPDPFVEP NEVLLPRPLA RALSFPEQVT
     CFAPARMNLL KHCVVNGPRK YPGATHIELR HANGEIRSVD LNVPEQTRRQ HAARFFAMAQ
     SGVTLIVYRH ILNGDRVIFN RQPTLHKPSM MGYRVKVLSG SKTIRFHYVN GNSFNADFDG
     DEMNVHVPQS IETRAEVETL MDANINYLVP TSGRPIRGLI QDHVAAGVLV TLRDKFFDHS
     TFVQLVYNGV GPYIQENVGI TLAELIPIPA ILMPRPMWTG KQLISVMVRF SSGLSAASDC
     GREIEGGITL KGTSQIQPSA FDRIPAGSCD AVRAKSGAVV DSTVMFANSE LITGFMCKKQ
     LGASNMSAPH HVYELYGPHR TGQLFAAFGR VLLLALRKEG LSLAMDDMFL VDEERRCDLL
     RKLDDIALDV PDEEATAAPM IADYATKIQQ EFVPQRMLVP FPKNHLLLMT ISGAKGSNLN
     ATQMSLQLGQ QLFDGLRVKR MNSSKTLPSF FTNEKRARSF GFAMGSFASG IRPAEYTIHA
     MAGRDGLIDT AVKTSRSGHL QRCLIKGLES LVVHWDRTVR DSNGSVIQFM YGGDGLDPCK
     ASTLTAWEMM KDNVVDVSKR FGGDASESVA GAEDGAAAGL KEMRNEDGKP TTEAVQNAHM
     EQQLSTYPLP ASLDKSLSEY LCKKADFPLF RKVSTLARWD AKQQLKERLQ QRRQKWVGAF
     EKTLADITAR RRLWALCEPG EPVGLLAAQA AGEPSTQMTL NTFHTAGSTV SHVTEGIPRL
     RELLIYASVN KAAVVVPVTN ATEEDEKVIA KMLRAGVAAK LTDCLAKVTD GAGGQSASSS
     MQRNLNTGFG KGYHYHVARG RTGMVITVSF LFSRSCLEEL RKRMCMSPSE HRQSFTEALK
     NVVRLIMRSL SAVPREKESG DGSGNTGGMK GGSGRADRKR KRSGPDDGGG PLGGTFGDEI
     MRIEEGTDSD DGMSERSSIG GGRAGSEVSS LHSDGTDTRG IAGSDTGGPQ RRRGSVESGR
     GDDASDSEAA DPDLYARRSG SPARDAEDGG EMQDRDGTDW GGTSMQGVVG YDNFPEIHMS
     FTKSNFGAVI APLSTAAAAR DGVVQLHEDF FIVNAVLRTA SDVIAVIPDV VDNALEAQRM
     PSWLPQFGSL TFTRLKDKGS GQLVFQGPGS TMRNVMSFLS LFTVGIKSIK LHQACSTDIR
     DMGTYFGIES GYAALYDELN KLFNRYNVDP RHLSLIADTS THRGRWENFN FTGVISTSAS
     PLFQMTFASS KRWLHRAVSR GMSDDLESFS SAIMVGERPR VGTASVRLST DTAILRDVLE
     RNFA
//