ID Q1L5Y7_ANTMA Unreviewed; 780 AA.
AC Q1L5Y7;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012418};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
DE Flags: Fragment;
GN Name=RPB1 {ECO:0000313|EMBL:AAY89349.1};
OS Antirrhinum majus (Garden snapdragon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX NCBI_TaxID=4151 {ECO:0000313|EMBL:AAY89349.1};
RN [1] {ECO:0000313|EMBL:AAY89349.1}
RP NUCLEOTIDE SEQUENCE.
RA Luo J., Yoshikawa N., Hall B.D.;
RT "Paralog Sorting and Differential Expression of RPB2 Genes in Core
RT Eudicots.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; DQ020643; AAY89349.1; -; mRNA.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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; cd02733; RNAP_II_RPB1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 2.40.40.20; -; 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; 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; IPR006592; RNA_pol_N.
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; 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; 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 SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..225
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT COILED 371..398
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY89349.1"
FT NON_TER 780
FT /evidence="ECO:0000313|EMBL:AAY89349.1"
SQ SEQUENCE 780 AA; 88490 MW; 79880DD6B021A878 CRC64;
ATQRSGRXIK SICSRLKAKE GRIRGNLMGK RVDFSARTVI TPDPTINIDE LGVPWSIALN
LTYPETVTPY NIERLKELVE YGPHPPPGKT GARYIIRDDG QRLDLRYLKK SSDMHLELGY
KVERHLNDGD FVLFNRQPSL HKMSIMGHRI KIMPYSTFRL NLSVTSPYNA DFDGDEMNMH
VPQSFETRAE VLELMMVPKC IVSPQANRPV MGIVQDTLLG CRKITKRDTF IEKDVFMNIL
MWWEDFDGKV PAPVILKPRP LWTGKQVFNL IIPKQINLLR YSAWHQEKEK GFITPGDTQV
RIEKGELLTG TLCKKTLGTG TGSLIHVIWE EVGPDAARKF LGHTQWLVNY WLLQNAFSIG
IGDTIADAAT MEKINETIQN AKNEVKELIR AAQEKQLEAE PGRTMMESFE NRVNQVLNKA
RDDAGSSAQK SLSEHNNLKA MVTAGSKGSF INISQMTACV GQQNVEGKRI PFGFIDRTLP
HFTKDDYGPE SRGFVENSYL RGLTPQEFFF HAMGGREGLI DTAVKTSETG YIQRRLVKAM
EDIMVKYDGT VRNSLGDVIQ FLYGEDGMDA VWIESQPLES LKLKKSDFND MYRYEIDSSN
WNPSYMLSEA VEDLKTIREI RSVFDAEVQK LEADRFQLGT GIATTGDNSW PLPVNIRRLV
LNAQKTFKVD FRRPSDMHPM EIVEAVDKLQ ERLKVVVGDD YLSMEAQKNA TLFFNILLRS
ALASKRVLKE YRLTREAFEW VIGEIESRFL QSLVAAGEMI GCVAAQSIGE PATQMTLNTF
//