ID K7TLU2_MAIZE Unreviewed; 1850 AA. AC K7TLU2; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 02-OCT-2024, entry version 76. DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279}; DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279}; GN Name=541967 {ECO:0000313|EnsemblPlants:Zm00001eb416050_P001}; GN ORFNames=ZEAMMB73_Zm00001d024583 {ECO:0000313|EMBL:AQK41527.1}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK41527.1}; RN [1] {ECO:0000313|Proteomes:UP000007305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. B73 {ECO:0000313|Proteomes:UP000007305}; RX PubMed=19965430; DOI=10.1126/science.1178534; RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S., RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D., RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K., RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M., RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B., RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E., RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J., RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E., RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A., RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R., RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A., RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E., RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A., RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T., RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L., RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P., RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A., RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C., RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A., RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C., RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W., RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C., RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K., RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K., RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S., RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.; RT "The B73 maize genome: complexity, diversity, and dynamics."; RL Science 326:1112-1115(2009). RN [2] {ECO:0000313|EMBL:AQK41527.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Seedling {ECO:0000313|EMBL:AQK41527.1}; RG Maize Genome Sequencing Project; RA Ware D.; RT "Update maize B73 reference genome by single molecule sequencing RT technologies."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb416050_P001} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb416050_P001}; RA Seetharam A., Woodhouse M., Cannon E.; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EnsemblPlants:Zm00001eb416050_P001} RP IDENTIFICATION. RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb416050_P001}; RG EnsemblPlants; RL Submitted (MAY-2021) to UniProtKB. 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|RuleBase:RU004279}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM000786; AQK41527.1; -; Genomic_DNA. DR RefSeq; NP_001292746.1; NM_001305817.1. DR IntAct; K7TLU2; 1. DR STRING; 4577.K7TLU2; -. DR PaxDb; 4577-GRMZM2G044306_P01; -. DR EnsemblPlants; Zm00001eb416050_T001; Zm00001eb416050_P001; Zm00001eb416050. DR GeneID; 541967; -. DR Gramene; Zm00001eb416050_T001; Zm00001eb416050_P001; Zm00001eb416050. DR KEGG; zma:541967; -. DR eggNOG; KOG0260; Eukaryota. DR HOGENOM; CLU_000487_1_1_1; -. DR OrthoDB; 7998at2759; -. DR Proteomes; UP000007305; Chromosome 10. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro. DR CDD; cd02584; RNAP_II_Rpb1_C; 1. DR CDD; cd02733; RNAP_II_RPB1_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; 3.30.1360.140; -; 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; 2. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1. DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime. DR InterPro; IPR000722; RNA_pol_asu. DR InterPro; IPR000684; RNA_pol_II_repeat_euk. 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; IPR007075; RNA_pol_Rpb1_6. DR InterPro; IPR007073; RNA_pol_Rpb1_7. DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf. 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:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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 Pfam; PF04992; RNA_pol_Rpb1_6; 1. DR Pfam; PF04990; RNA_pol_Rpb1_7; 1. DR Pfam; PF05001; RNA_pol_Rpb1_R; 21. DR PRINTS; PR01217; PRICHEXTENSN. DR SMART; SM00663; RPOLA_N; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. DR PROSITE; PS00115; RNA_POL_II_REPEAT; 14. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|RuleBase:RU004279}; Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Plastid {ECO:0000256|ARBA:ARBA00022640}; KW Proteomics identification {ECO:0007829|PeptideAtlas:K7TLU2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007305}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, KW ECO:0000256|RuleBase:RU004279}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 241..547 FT /note="RNA polymerase N-terminal" FT /evidence="ECO:0000259|SMART:SM00663" FT REGION 1565..1850 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 693..720 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1565..1842 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1850 AA; 206101 MW; 9EEE2BB301177103 CRC64; MDARFPYSPA EVAKVEFVQF GILSPDEIRQ MSVIQIEHAE TMERGKPKPG GLSDPRLGTI DRKIKCETCM AGMAECPGHF GHLELAKPMF HIGFIKTVLS IMRCVCFNCS KILADEDETK FKQALKIRNP KNRLKRIYDA CKSKKVCAGG DDLDVQEQDT DEPIKKRGGC GAQQPNITVD GMKMVAEFKA PKKKTDDQDQ LPEPVERKQI LSAERVLNVL KRISDEDCLL LGLNPKYARP DWMILQVLPV PPPPVRPSVM MDTSSRSEDD LTHQLAMIIR HNENLRRQER NGAPAHIITE FAQLLQFHIA TYFDNDLPGQ PRATQRSGRP IKSICSRLKA KEGRIRGNLM GKRVDFSART VITPDPNINI DELGVPWSIA LNLTYPETVT PYNIERLKEL VEYGPHPPPG KTGAKYIIRE DGQRLDLRYV KKSSDQHLEL GYKVERHLND GDFVLFNRQP SLHKMSIMGH RIKIMPYSTF RLNLSVTSPY NADFDGDEMN MHVPQSFETR AEVLELMMVP KCIVSPQSNR PVMGIVQDTL LGCRKITKRD TLIEKDVFMN ILMWWQDFDG KIPAPTILKP RPIWTGKQVF NLIIPKQINL IRFSAWHSEE EKGFITPGDT MVRIEKGELL SGTLCKKSLG TGSGSLIHVI WEEVGPDAAR KFLGHTQWLV NYWLLQNGFS IGIGDTIADA STMETINDTI SKAKNAVKEL IKKAHEKQLE AEPGRTMMES FENRVNQVLN KARDDAGSSA QNSLSESNNL KAMVTAGSKG SFINISQMTA CVGQQNVEGK RIPFGFIDRT LPHFTKDDYG PESRGFVENS YLRGLTPQEF FFHAMGGREG LIDTAVKTSE TGYIQRRLVK AMEDIMVKYD GTVRNSLGDV IQFLYGEDGM DAVWIESQKL DSLKMKKPEF DNVFRYELDD ENWRPNYMLP EHVDDLKTIR EFRNVFEAEV QKLEADRYQL GSEITTTGDN SWPMPVNLKR LIWNAQKTFK IDFRRPSDMH PMEIVEAIDK LQERLKVVPG DDAMSIEAQK NATLFFNILL RSTFASKRVL KEYRLTKEAF EWVIGEIESR FLQSLVAPGE MIGCVAAQSI GEPATQMTLN TFHYAGVSAK NVTLGVPRLR EIINVAKKIK TPSLSVYLKP QVNQKKELAK NVQCALEYTT LRSVTHATEI WYDPDPLGTI IEEDTEFVQS YYEMPDEDID PDKISPWLLR IELNREMMVD KKLSMADIAE KINREFDDDL SCIFNDDNAD KLILRIRITN DEAPKGEIQD ESAEDDVFLK KIEGNMLTEM ALRGIPDINK VFIKEGKVNT FYQDDGFKAA NEWMLDTEGV NLLAVMCHED VDATRTTSNH LIEVIEVLGI EAVRRSLLDE LRVVISFDGS YVNYRHLAIL CDTMTYRGHL MAITRHGINR NDTGPLMRCS FEETVDILLD AAVYAESDHL RGVTENIMLG QLAPIGTGGC ALYLNDQMLQ QAIELQLPSY VEGLDFGMTP ARSPITGTPY HEGMMSPSYL LSPNIRASPI NTDASFSPYV GHMAFSPFPS PGGYSPSSGG YSPSSPVFTP EKGYSPLSPS YSPASPSYSP TSPSYTPGSP TYSPTSPNYS PTSPTYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPVYSPTSP AYSPTSPAYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPAYSP TSPGYSPTSP SYSPTSPSYS PTSPSYNPSS AKYSPSHAYS PSSPRMSPYS QTSPSYSPTS PTYSPTSPSY SQPSPSYSPT SPFNTSGGPS PDYSPTSPNY SPSGSYSPTA PGYSPSSTGQ GNDKDDKSAR //