ID   RPA1_DICDI              Reviewed;        1615 AA.
AC   Q86H36; Q553A1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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;
GN   Name=polr1a; Synonyms=rpa1; ORFNames=DDB_G0275759;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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|UniProtKB:P10964}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000013; EAL69630.1; -; Genomic_DNA.
DR   RefSeq; XP_643519.1; XM_638427.1.
DR   AlphaFoldDB; Q86H36; -.
DR   SMR; Q86H36; -.
DR   STRING; 44689.DDB0216292; -.
DR   PaxDb; Q86H36; -.
DR   EnsemblProtists; EAL69630; EAL69630; DDB_G0275759.
DR   GeneID; 8620100; -.
DR   KEGG; ddi:DDB_G0275759; -.
DR   dictyBase; DDB_G0275759; rpa1.
DR   eggNOG; KOG0262; Eukaryota.
DR   HOGENOM; CLU_000487_2_3_1; -.
DR   InParanoid; Q86H36; -.
DR   OMA; RFFNRED; -.
DR   PhylomeDB; Q86H36; -.
DR   Reactome; R-DDI-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR   PRO; PR:Q86H36; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005736; C:RNA polymerase I complex; ISS:dictyBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISS:dictyBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; ISS:dictyBase.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   PANTHER; PTHR19376:SF11; PTHR19376:SF11; 1.
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   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..1615
FT                   /note="DNA-directed RNA polymerase I subunit rpa1"
FT                   /id="PRO_0000330755"
FT   REGION          155..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..967
FT                   /note="Bridging helix"
FT                   /evidence="ECO:0000250"
FT   REGION          1305..1411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1367..1395
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         593
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         595
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
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"
SQ   SEQUENCE   1615 AA;  181190 MW;  7B0970C64E5EE891 CRC64;
     MSMSQSALIK EEISSVSFQF YTSDDVRKLS VKQIVEIESF DMLGGPVPGG LHDPALGPTG
     PAERCATCSL DFIECPGHFG HIELAIPCYN PVSFQTIFKL LKNKCFHCHH FKHGKPIINQ
     FIEELTLLFK GDVVKARNLR ERNVLLRGYE EKKKGKSNEE GEEVMESDES DSDKMDTDEN
     KTNGKIICDG VFNAKEIYSG KATHIEDFKR EVFKEFFGSF SGYAIPCGNC GAYSPRLRNG
     DASKSKLFIM PLHDKYATKN SAIKLPTNFS SVKEQTEHGT WFAPWEVLDN MKKLFENEKE
     ILDMLLGHLV PIVTNKGGAK KNVGRQFTKE SNVDSLFMRV FPVTPARYRP PNFVNGRRSE
     HPQNSHYKGM VKSNKMIRQS IDAGEGKAKF LVNSVCDLQM HVNNMYDNSK SNSNTNEVAN
     GIKQILEKKE GLFRKHMMGK RVNYAARTVI SPDISLETNE MGVPQYFAKT LTFPQPVTSF
     NYNQLAQAVI NGPEQYPGAN FIEDENGHLI NLSKESQEKR IALSKTLLTS HPHAPRGVNK
     KVYRHLLSGD YVLANRQPTL HKPGIMGHRV KVLGKNEKTL RMHYSNCSTY NADFDGDEMN
     IHFPQSLLAS AEIREICANN YQYLVPRNGA PLRGLIQDHI LTGVLLTKRD TLFTKADFQA
     ILYASCWSVN TKHPIVTPPP CILKPVPLWS GKQLISAALN QLTIGRAPLN LEAPSKIPTK
     MWGTKGLEIT RDSHVIIRQN EMVAGILDKG HFGASSYGLV HTCYELYDPD VAGSLLTLLG
     RMFTNYLQSR GFTCGVDDLL MKNKEEKFRV ETLKKANEEG YTVAAKFADL SKYDEQKARD
     FFSKALQSER EVARLDGLLK KGLNQYTSKV IDTLIPGGQQ KPFPKNNFSL MTVSGAKGSV
     VNFSQVSCLL GQQELEGKRV PRMVSGKTLP SFQAYDASAR AGGFVMDRFL TGVRPQDYFF
     HCMAGREGLI DTAVKTSRSG YLQRCLIKHL EGLSVQYDNT VRESDGSVIQ FNYGEDSLEI
     GKTPYLTKFP IIAENYELFK SQFPMEQLIE QLKNQEVVEY NRSIKTQPEL DPVMSKFNPS
     SDLGCVSESF MNQLNHYIES NPQKLIKTTS NRDGKINEKD FRNLMYLYYS RSMVSPGESV
     GLLCAQSIGE PSTQMTLNTF HLAGRGEANV TLGIPRLREL IMTATTKPIT PLMEFQINDS
     TNKVETEKMA KYLEILKLSD IIKDITVQEY FQDTNRNYDI EIEFIPTLQQ VLSLHRIKEK
     QLNKLFGEFN KVIKRQVKSQ GKLKVNNGDI GLGSKVRGSD LVEDDSLTIN DDDAPANDDT
     TNNDENTSQQ QPSSQNKKSK SKVITQDDDS VAAKSKNKKK QNVNYEDGEE EAEEKDSDEG
     ESEAEESDDK SDVDSDSDEI SNSRSSNSFS DESIEFDQKK LTFTISVASD SKKVLMLGIV
     ETEASKFVLK SCKGITRCFV NEKQVGGKTH YSIQSEGVNL SEIFELRDKL KIDEIYTNDI
     YAILQKYGVE ACRQAVTSEI SNVFAAYGIS VDKRHLILLG DYMTFEGGYR ALNRIGIENN
     TSPFQKMSFE TTFSFLSKAS LMGDYDTVTS PSSRIVLGQI VKNGTGSFTI VAPVK