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RPOB_CUSEX
ID   RPOB_CUSEX              Reviewed;        1070 AA.
AC   A8W3B6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321};
OS   Cuscuta exaltata (Tall dodder).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Monogynella.
OX   NCBI_TaxID=476139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA   McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT   "Complete plastid genome sequences suggest strong selection for retention
RT   of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL   BMC Plant Biol. 7:57-57(2007).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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:0000255|HAMAP-Rule:MF_01321};
CC   -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC       composed of four subunits: alpha, beta, beta', and beta''. When a
CC       (nuclear-encoded) sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SUBCELLULAR LOCATION: Plastid.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC       some thylakoids, although the photosynthetic activity does not exceed
CC       the light compensation point. {ECO:0000305}.
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DR   EMBL; EU189132; ABW83687.1; -; Genomic_DNA.
DR   RefSeq; YP_001542523.1; NC_009963.1.
DR   AlphaFoldDB; A8W3B6; -.
DR   SMR; A8W3B6; -.
DR   GeneID; 5729608; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.30.150.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR   InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR010243; RNA_pol_bsu_bac.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 3.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..1070
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000329199"
SQ   SEQUENCE   1070 AA;  120464 MW;  F3D69C09A8D45EA8 CRC64;
     MLEDGKGGIT TIPGLNQIQF EGFCRFIDQG LTEELYKFQK IEDIDQEIEF QLFAETYQLV
     EPLIKERDAV YDSLTYSSEL YVSAGLIRKA SKDMQEQKIF IGSIPIMNSL GTSIVNGIYR
     IVINQILQSP GIYYRSELDQ NGISVYTGTI ISDWGGRSEL EIDRKARIWA RVSRKQKISI
     LVLSSAMGSN LREIIENVCY PEILLSFLRD KEKKKIGSKE NAILEFYKKF ACVGGDPLFS
     ESLCKELQNK FFQQRCELGR IGRRNMNRRL HLDIPQNNTF LLPRDILEAT DLLIGLKFGM
     GTLDDMNHLQ NKRIRSVADL LQDKFGLALV RLENAVQGTI CGAIHHKKIP TPQNLVTSTL
     LTTTYESFFG LHPLSQVLDR TNPLTQIVHA RKVSSLGPGG LTGRTASFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLAI HVRIGNWGSL ESPFFKISDR LTGVRVLHLS PGRDEYYMVA
     AGNSLALNQD IQEDLVVPAR FRQEFLTIAW EQVNLRSIFP FQYFSIGTSL IPFIEHNDAN
     RALMSSNMQR QAVPLAWSEK CIVGTGVERQ AALDSGSLAI AEREGRVIYT DTEKILVSGD
     GKTISIPLVM YQRSNKNTCM YQQPQVRRGQ FIKKGQILAD GAATVEGELA LGKSVLVAYM
     PWEGYNYEDA VLISECLVYE DIFTSFHIRK YEIQTHVTTQ GPEKVTNEIP HLEAHLIRNL
     DKNGIVLQGS WVEPGDVLVG KLTPQVVKES SYAPEDRLLR AILGIQVSAS KETCLKVPIG
     GRGRVIDVRW IQKKGGYGYN PEKIRVYILQ KREIKVGDKV AGRHGNKGII SKILPRQDMP
     YLQDGRSVDL VFNPLGVPSR MNVGQIFECS LGLAGSLLDR HYRIAPFDER YEQEASRKIV
     FSELYEASKQ TANPWAFEPE YPGKSRIFDG RTGNTFEHPV LIGKPYILKL IHQVDDKIHG
     RSSGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
     GTTIVGGTIP NPKNAPESFR LLVRELRSLA LELTHFLVSE KNFQVNKREA
 
 
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