ID C5YGY9_SORBI Unreviewed; 1857 AA.
AC C5YGY9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=SORBI_3007G044100 {ECO:0000313|EMBL:EES13372.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EES13372.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EES13372.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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 -!- 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}.
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DR EMBL; CM000766; EES13372.1; -; Genomic_DNA.
DR RefSeq; XP_002443877.1; XM_002443832.1.
DR STRING; 4558.C5YGY9; -.
DR EnsemblPlants; EES13372; EES13372; SORBI_3007G044100.
DR GeneID; 8076592; -.
DR Gramene; EES13372; EES13372; SORBI_3007G044100.
DR KEGG; sbi:8076592; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR InParanoid; C5YGY9; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 7998at2759; -.
DR Proteomes; UP000000768; Chromosome 7.
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; 16.
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 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
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 Reference proteome {ECO:0000313|Proteomes:UP000000768};
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..1857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1857 AA; 206898 MW; 8EE0901BC100159E CRC64;
MDARFPYSPA EVAKVELVQF GILSPDEIRQ MSVVQIEHAE TMERGKPKPG GLSDPRLGTI
DRKIKCETCM AGMAECPGHF GHLELAKPMF HIGFIKTVLS IMRCVCFNCS KILADEDETK
FKQALKIRNP KNRLKRIYDA CKSKKVCAGG DDLDVQEQDT DEPVKKRGGC GAQQPNITVD
GMKMVAEFKA PKKKSDDQDQ LPEPVERKQI LSAERVLNVL KRISDEDCLL LGLNPKYARP
DWMILQVLPV PPPPVRPSVM MDTSSRSEDD LTHQLAMIIR HNENLRRQER NGAPAHIITE
FAQLLQFHIA TYFDNELPGQ 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 KIPAPAILKP RPIWTGKQVF NLIIPKQINL
IRFSAWHSEE EKGFITPGDT MVRIEKGELL SGTLCKKSLG TGTGSLIHII WEEVGPDAAR
KFLGHTQWLV NYWLLQNGFS IGIGDTIADA STMQTINDTI CKAKDEVKEL IKKAHEKQLE
AEPGRTMMES FENRVNQVLN KARDDAGSSA QKSLSESNNL KAMVTAGSKG SFINISQMTA
CVGQQNVEGK RIPFGFIDRT LPHFTKDDYG PESRGFVENS YLRGLTPQEF FFHAMGGREG
LIDTAVKTSE TGYIQRRLVK AMEDIMVKYD GTVRNSLGDV IQFLYGEDGM DAVWIESQKL
DSLKMKKPEF DNLFRYELDD ENWRPNYMLP EHVDDLKTIR EFRNVFEAEV QKLEADRYQL
GTEIATTGDN SWPMPVNLKR LIWNAQKTFR IDFRRPSDMH PMEIVEAVDK LQERLKVVPG
DDPMSIEAQK NATLFFNILL RSTFASKRVL KEYRLTKEAF EWVIGEIESR FLQSLVAPGE
MIGCVAAQSI GEPATQMTLN TFHYAGVSAK NVTLGVPRLR EIINVAKKIK TPSLSVYLKP
EVNQKKELAK NVQCALEYTT LRSVTHATEI WYDPDPLGTI IEEDAEFVQS YYEMPDEDID
PDKISPWLLR IELNREMMVD KKLSMADIAD KINREFDDDL SCIFNDDNAD KLILRIRITN
DEAPKGEIQD ESAEDDVFLK KIEGNMLTEM ALRGIPDINK VFIKEGKVNT FYQDEGFKAA
NEWMLDTEGV NLLAVMCHED VDATRTTSNH LIEVIEVLGI EAVRRSLLDE LRVVISFDGS
YVNYRHLAIL CDTMTYRGHL MAITRHGINR NDTGPLMRCS FEETVDILLD AAVYAESDHL
RGVTENIMLG QLAPIGTGGC ALYLNDQMLQ QAIELQLPSY VEGLDFGMTP ARSPISGTPY
HEGMMSPSYL LSPNIRASPI NTDASFSPYV GHMAFSPFPS PGGYSPSSGG YSPSSPVFTP
EKGYSPLSPS YSPASPSYSP TSPSYTPGSP TYSPTSPNYS PTSPTYSPTS PSYSPTSPSY
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPVYSPTSP AYSPTSPAYS PTSPSYSPTS
PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPAYSPTSP GYSPTSPSYS
PTSPSYSPTS PSYNPSSAKY SPSHAYSPSS PRMTPYSQTS PSYSPTSPTY SPTSPSYSQP
SPSYSPTSPF NTSGGPSPDY SPTSPNYSPS GSYSPTAPGY SPSSTGQGND KDDESNR
//
