ID A0A2T7DWK9_9POAL Unreviewed; 1687 AA.
AC A0A2T7DWK9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=GQ55_4G084800 {ECO:0000313|EMBL:PUZ59959.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ59959.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ59959.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; CM009752; PUZ59959.1; -; Genomic_DNA.
DR EnsemblPlants; PUZ59959; PUZ59959; GQ55_4G084800.
DR Gramene; PUZ59959; PUZ59959; GQ55_4G084800.
DR Proteomes; UP000244336; Chromosome 4.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000244336};
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 328..644
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 140..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1358
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1687 AA; 187955 MW; 992E256C591D82B5 CRC64;
MADLRGIEAA SEEVDSIHFS FYGDDEIKRI SVKKITKSER LDAKNHPVPG GLLDPAMGPI
NDTDTCKSCG QHSARCPGHF GHIELAKPLF NPLLFMSLTN LLHATCFHCH KFRLNKEQVD
RYVNELELLV KGDVARAKNL EDSGKEASLS EEDEDTTEAT SGDKSSPEKD KKTWTSIQLK
EILSIFSKIM KKRAKKCANC DMKNPSISSP IFGWLVKDRS ASAVRANAIA DFKLKGDGSA
PNSGETGVSG LDEKPTSPQS KGSINEGRHL SDDSIKEMVA SSGKKHLLPT EVEIILKDLW
KNEAKFCMLL CDFQQNTLSV SEKRRGYEMF FLNSLLVAPN RFRPSTSSSL GIMEHPQNVL
LSKVQEANLL LQNNSAGSNH MDLLRRWMDL QRSVNVLYDS SKGLAKSEKN AHGIRQLLEK
KEGVLRQKMM GKRVNYACRS VISPDPYLAV NEIGIPPVFA TRLTYPEKVT PWNAKKLQEA
VRNGADVHPG ATHYRDNDNM YKLQAAPAKR RAISKLLPAS RGSISQLGKD PNCEFESKVV
YRHLQDGDIV LVNRQPTLHK PSMMAHFVRV LPGEKTIRMH YANCSTYNAD FDGDEMNVHF
PQDEISRSEA MNIVDANKQY IGPRSGDAVR GLIQDHIVGA VLLTKQDTLL SREEYSQLVY
GSCMPSNCGP HQPGTKVSAI KDGGALELVP PAILRPKPLW TGKQVITTIL NHLTKGRHPF
TVEQKGKITK EFLIPGELHD AKDKDPSAEE LHDAKDKDPS AEEEERKKDI SELVLYVRGN
ELIKGMIDKA QFGKYGIVHT VHEFYGADTA GILLSTFSRL FTLFLQLHGF TCGIDDLLLR
QQSNKTRMEI LAESEKCSEI VHKKFTQRTE EGLEDPILQM EVEKVIRSNG EFATVKLDRM
MSNELNDITS VANKKLLPYG LQKPFPGNCL SLMTATGAKG GMVNMTQISS LLGQQALEGK
RVPRMVSGKT LPCFPPWDTS SRAGGFICDR FLTGLRPQEY YFHCMAGREG LVDTAVKTSR
SGYLQRCLIK CLESLKVSYD HTVRDVDGSI VQFCYGEDGV DVLKTSFLNK FKELADNKKV
VLDKIGGHNQ ISFDQKGEKN EQLPNFNCYI TELPKKLSDE AATFLQVSKE KKSCDIDEEE
LLKLLKIKYI YSLVDPGEAV GVVAAQSIGE PSTQMTLNTF HLAGRGEMNV TLGIPRLKEI
LMTASANIST PFMKCPLLKE KTRGDAERVA AKFRRVCVAH IVEKIEVCTV PFYNSNGHVS
TLYKLQMKLY PQERYPLSDL TVDECQTTLR KVFVDAMEHA IDKHLDLLRK INKIRDVKVE
DTEGSLSDGG EESESGHADG EDTGMSDGDD ENDDEDDLGA DAEKRKRQEK DEMEYDDDTE
NEGEIDSESE EVTNIKRQSE EDPAESGDDL QEAEEEHKTS KSEMTSVGEV SYSSKKGANS
KDKHKAAKLQ EKMQTDGKSD ESKPDQITYK RGKKIQRTVH VESKGLDFEI HYAFHDEPHI
LLAQIAQKTA RTIFVKACDN IDECSVLPRD DSPPMYLETS GVNFELFWNL ADYISINEIR
SNDIHAMLKT YGVEAARATI IQEVSGVFGA YGIEVDMRHL SMIADFMTFD GGFRPMNRLG
MGQLSTSPFG KMTFETATKF IVDAATHGEA DSLECPSASV CLGKPAKVGT GTFGLLQNLG
VEQPMVM
//
