ID A0A1S3XM16_TOBAC Unreviewed; 1630 AA.
AC A0A1S3XM16;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=LOC107766442 {ECO:0000313|RefSeq:XP_016440712.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016440712.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016440712.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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|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 RefSeq; XP_016440712.1; XM_016585226.1.
DR SMR; A0A1S3XM16; -.
DR STRING; 4097.A0A1S3XM16; -.
DR PaxDb; 4097-A0A1S3XM16; -.
DR GeneID; 107766442; -.
DR KEGG; nta:107766442; -.
DR OMA; QAFPIPH; -.
DR OrthoDB; 7998at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; 6.
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; 4.
PE 3: Inferred from homology;
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};
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:UP000084051};
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 242..548
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1538..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 694..721
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1538..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1630
FT /evidence="ECO:0000313|RefSeq:XP_016440712.1"
SQ SEQUENCE 1630 AA; 183163 MW; 209388C292FE1003 CRC64;
MDLRFPFSPA EVAKVRVVQF GIVSPDEIRQ MSVVHIEHGE TTERGKPKPG GLSDPRLGTI
DRKMKCETCM ANMAECPGHF GHLELAKPMF HIGFMKPVLS ILRCVCFNCS KILADEDDPK
FKQAMRIRNP KNRLKKMLDA CKNKTKCEGG DEIDVRGEEP EAPVKKSRGG CGAQQPKISI
DGMKMVAEYK LQKKKSDDPE QMPEPVERKQ QLSAERVLSI LKRVSDEDCL LLGLNPEYAR
PDWMILQVLP IPPPPVRPSV MMDTSSRSED DLTHQLAMII RHNENLKRQE RNGAPAHIIS
EFAQLLQFHI ATYFDNDLPG QPRATQRSGR PIKSICSRLK SKEGRIRGNL MGKRVDFSAR
TVITPDPTIN IDQLGVPWSI ALNLTYPETV TPYNIERLKE LVEYGPHPPP GKTGAKYIIR
DDGQRLDLRY LKKSSDQHLE LGYKVERHLN DGDFVLFNRQ PSLHKMSIMG HRIKIMPYST
FRLNLSVTSP YNADFDGDEM NMHVPQSFET RAEVLELMMV PKCIVSPQAN RPVMGIVQDT
LLGCRKITKR DTFIEKDVFM NILMWWEDFD GKVPAPAILK PRPLWTGKQV FNLIIPKQIN
LLRYSAWHND SEKGPITPGD TQVRIEKGEL LTGTLCKKTL GTSTGSLIHV IWEEVGPDAA
RKFLGHTQWL VNYWLLQNAF SIGIGDTIAD ASTMEKINET ISNAKSKVKE LIKAAQEKQL
EAEPGRTMME SFENRVNQVL NKARDDAGSS AEKSLSESNN LKAMVTAGSK GSFINISQMT
ACVGQQNVEG KRIPFGFIDR TLPHFTKDDY GPESRGFVEN SYLRGLTPQE FFFHAMGGRE
GLIDTAVKTS ETGYIQRRLV KAMEDIMVKY DGTVRNSLGD VIQFLYGEDG MDAVWIETQK
LDSLKAKKLT FDDMYAYEID DPNWNPSYML PEAIEDLKTI REIRSVFDAE VQKLQADRKQ
LGTEIAVTGD NSWPLPVNIQ RLVLNAQKTF KIDFRRRSDM HPMEIVEAVD KLQERLKVVP
GDDYLSMEAQ KNATLFFNIL LRSALASKRV LKEYRLSREA FDWVIGEIES RFLQSLVAPG
EMIGCVAAQS IGEPATQMTL NTFHYAGVSA KNVTLGVPRL REIINVAKKI KTPSLSVYLK
PEVGKTKERA KTVQCALEYT TLRSVTQATE VWYDPDPMST LIEEDVEFVK SYYEMPDEEI
DPDKISPWLL RIELNREMMV DKKLSMADIA EKINLEFDDD LTCIFNDDNA EKLILRIRIM
NDEAPKGELD ESAEDDVFLK KIESNMLTEM ALRGIPDINK VFIKNSKVQK FDDNEGFKAE
TEWMLDTEGV NLLAVMTHED VDARRTTSNH LIEVIEVLGI EAVRRSLLDE LRVVISFDGS
YVNYRHLAIL CDTMTYRGHL MAITRHGINR NDTGPMMRCS FEETVDILLD AAVFAESDYL
RGVTENIMLG QLAPIGTGGC ALYLNEEMLK QAIEIPLPSY MEGGLEFGMT PGRSPISGTP
YHDGMMSPNY LLSPNMRMSP ITDAQFSPYV DKMAFSPTSS PGYSPSSPGY SPSSPGYSPT
SPGYSPTSPG YSPTSPGYSP TSPTYSPSSP GYSPTSPAYS PTSPSYSPTS PSYSPTSPSY
SPTSPSYSPT
//
