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Database: UniProt
Entry: Q1L5Y7_ANTMA
LinkDB: Q1L5Y7_ANTMA
Original site: Q1L5Y7_ANTMA 
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};
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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
//
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