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Database: UniProt
Entry: B8C4Z8_THAPS
LinkDB: B8C4Z8_THAPS
Original site: B8C4Z8_THAPS 
ID   B8C4Z8_THAPS            Unreviewed;      1671 AA.
AC   B8C4Z8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   Name=RPA1 {ECO:0000313|EMBL:EED91031.1};
GN   ORFNames=THAPSDRAFT_40884 {ECO:0000313|EMBL:EED91031.1};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128 {ECO:0000313|EMBL:EED91031.1, ECO:0000313|Proteomes:UP000001449};
RN   [1] {ECO:0000313|EMBL:EED91031.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED91031.1};
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2] {ECO:0000313|EMBL:EED91031.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED91031.1};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000256|RuleBase:RU004279}.
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; Evidence={ECO:0000256|ARBA:ARBA00024550,
CC         ECO:0000256|RuleBase:RU004279};
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; CM000643; EED91031.1; -; Genomic_DNA.
DR   RefSeq; XP_002290924.1; XM_002290888.1.
DR   STRING; 35128.B8C4Z8; -.
DR   PaxDb; 35128-Thaps40884; -.
DR   EnsemblProtists; EED91031; EED91031; THAPSDRAFT_40884.
DR   GeneID; 7451111; -.
DR   KEGG; tps:THAPSDRAFT_40884; -.
DR   eggNOG; KOG0262; Eukaryota.
DR   HOGENOM; CLU_000487_2_2_1; -.
DR   InParanoid; B8C4Z8; -.
DR   OMA; NREDYQQ; -.
DR   Proteomes; UP000001449; Chromosome 6.
DR   GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IEA:GOC.
DR   CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR   CDD; cd01435; RNAP_I_RPA1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.70.2850; -; 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; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR   InterPro; IPR047107; DNA-dir_RNA_pol1_lsu_C.
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; 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; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU004279};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001449};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          347..669
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          260..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1372..1470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1404..1454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1671 AA;  183826 MW;  411E97A4D34A2B93 CRC64;
     MANLNQAIIR HQPTSVQFGV YTDDEVRQRS VCEISSSVAY DALNTPLPRG LYDPLLGPTA
     GGGGGASAYC ITCGNVQNLC PGHFGHIELC VPVYHPLFFP KLLLFMKMKC LACHHFRLSK
     RACRVFCTKL HLVDVGRMGE AMGLDEEMAA LASKASVGGG DGKMSKQVKQ EMMSSAAVLI
     DELLDQKMAL RPPDGQSAEE VTHTMHERAV RRKILKEFQQ ACTKCLKCAN CNAFSNKIRH
     DQFNKMFQVA LPARNAKVSD VSREDFPANT KGKKKKKSTS SSTVDEEIDP TGGPISRKAT
     VSTTKNIEAS KQDNFMHALE VEAQCRLTWN NEPFLCSKFF GWGKGYTLFF LRAVPVPPSR
     FRPPVIMGNM TVEHSQNFYL SKVLELNARI RSAFATIHEL TQEEADLKNT DKGQANMLEI
     WVDLQTTVNC FMDSTRDPKG TANNAPNGIR QLLEKKEGIF RKHMMGKRVN FACRSVISPD
     PYIGTNEIGL PLYFAKTLTF PTPVTALNIA EMRKLVQRGP LQYPGAVWVE FPNGQRIDLS
     KMKEGNRHAI AARLLADNGV VKVGRQLRDG DMVLMNRQPT LHKPGIMAHR VRVLFSPTQN
     TLRMHYANCN TYNADYDGDE MNCHFPQSYL AAAESQFIAG TDLQFIVPTD GSPLRGLIQD
     HVDAGVKLTC MNTFIEREVY QQLLFAALGS LPGLELIRSD ANIELLPPAI RKPKELWTGK
     QVISTLLNHL RKGNDRDEDP SFNFPGLSME RKAKTPATAF GASWNEHMVI VRDGDLVQGI
     LDKAAFGASE FSLVHAVYEA YGPSRAGLLL NALGRLFTAY IQYYTGHSCR MEDLILTPDA
     DEKRRQLVKV ESDGGKVEIP PVAQNPKSKQ PLKPHEKATV ASKIGELLSG GDGKENAAAL
     DGFMQSQVNP LASDIIKICL PDGLAVPFPE NTFGLMTTTG AKGSMVNQSQ VSCSLGQQAL
     EGRRVPRMSS GRTLPSFAPY DPNPRADGFI TDRFLTGVRP QEYYFHCMAG REGLVDTAVK
     TSRSGYLQRC LIKHLEELKV SYDHTVRDGE GGVVQFVYGE DGIDPTKAAH LDCESRTFQF
     LARNHESLKK RYPALPGSTL DIAVKDSRRA QETTPAESFH CEIIKPGVPD PIVSDTAREN
     GAHRLGSSGA CVSEHVANLA SNAMKDTGVK KALENSGLSK EGFSALVAAK YSSALAHPGE
     AVGSIAAQSI GEPSTQMTLN TFHLAGAGAN VTLGIPRLRE IIMTASKELK TPTMSIPLSE
     SVSDREALRL TRYFSKVSLM DLLASHGGIT VREVLEKGAG SNWERCYYVT LKLHPAERIN
     EAFGLRLEDI AAVVTKTFIP KLARVMKAEM KRNETNEGYA SIEVIGGAST DFMESDVSGG
     ESSKSKASKR PKDDEYDDEV ANDEDGVTGT RFGHRKEMTS YGDMDDDDKY IAKRSAKDDS
     DEDEDNRLPA VITEGEESDD ELESKSSNTA RISRSKNSII LDPLRVDPST CPLLMVGLVE
     RAAETTIVRA RPKINEGFVN NEEGRGRCLQ TAGCNFEEMW SLDEGVVDHN KLVSNDIWGI
     RCAYGVEAAR MSIADQIRGV FAVYGISVDP RHLSLIADFM TYDGEYKPMN RIGMADISST
     FLQMSFESTS VFMVDAALHK RNDPMMSPSA NIVMGHPIRH GTGAFECIAK A
//
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