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RPOB_CUSRE
ID   RPOB_CUSRE              Reviewed;        1070 AA.
AC   A7M958;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta;
DE            EC=2.7.7.6;
DE   AltName: Full=PEP;
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta;
DE            Short=RNA polymerase subunit beta;
GN   Name=rpoB;
OS   Cuscuta reflexa (Southern Asian 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=4129;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX   PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA   Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT   "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT   plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL   BMC Plant Biol. 7:45-45(2007).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000250}.
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;
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid.
CC   -!- RNA EDITING: Modified_positions=113 {ECO:0000269|PubMed:17714582}, 158
CC       {ECO:0000269|PubMed:17714582}, 184 {ECO:0000269|PubMed:17714582}, 189
CC       {ECO:0000269|PubMed:17714582}, 667 {ECO:0000269|PubMed:17714582};
CC       Note=Editing at positions 113 and 158 is more efficient in
CC       photosynthetically active tissue.;
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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; AM711640; CAM98386.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; YP_001430100.1; NC_009766.1.
DR   AlphaFoldDB; A7M958; -.
DR   SMR; A7M958; -.
DR   GeneID; 5536671; -.
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   2: Evidence at transcript level;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid; RNA editing;
KW   Transcription; Transferase.
FT   CHAIN           1..1070
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000308474"
SQ   SEQUENCE   1070 AA;  120490 MW;  38BB02FAA4C9D643 CRC64;
     MLVDGKGGIT TIPGLNQIQL EGFCRFIDQG LMEELSKFQK IEDIDQEIEF QLFVETYQLV
     EPLIKERDAV YDSLTYSSEL YVSAGLIRKA SKDMQEQTIF IGSLPIMNSL GTFIVNGIYR
     IVINQILQSP GIYYRSELDQ NGISVYTGTI ISDWGGRLEL EIDRKARVWA RVSRKQKISI
     LVLLSAMGLN LREILENVCY PEILLSFLRD KEKKKIGSKE NAILEFYKKF ACVGGDPLFS
     ESLCKELQNK FFQQRCELGR IGRRNMNRRL HLDIPHNNTF LLPRDILEAT DHLIGLKFGM
     GTLDDMNHLQ NKRIRSVADL LQDQFGLALV RLENAVQGTL CGAIRHKRIP TPQNLVTSTL
     LTTTYESFFG LHPLSQVLDG TNPLTQIVHA RKVSSLGPGG LTGRTASFRI RDIHPSHYGR
     ICPIDTSEGI NVGLIGSLAI HVRIGNWGSL ESPFYEISDR LTGVRVLHLS PGRDEYYMVA
     AGNSLALNQD IQEDQVVPAR YRQEFLTIAW EQVNLRSIFP FQYFSIGASL IPFIEHNDAN
     RALMSSNMQR QAVPLTWSEK CIVGTGMERQ AALDSGSLAI AEREGRVIYT DTEKILVSGD
     GKTINIPLVM YQRSNKNTCM YQQPQVRRGQ FIKKGQILAG GAATVEGELA LGKSVLVAYM
     PWEGYNFEDA VLISECLVYE DIFTSFHIKK YEIQIHMTTQ GPEKVTNEIP HLEAHLIRNL
     DKNGIVLQGS WVEPGDVLVG KLTPQVVKES AYAPEDRLLR AILGIPVSAS KETCLKVPIG
     ARGRVIDVRW IQKKGGYGYN PEKIRVYILQ KREIKVGDKV AGRHGNKGII SKILPRQDMP
     YLQDGRSVDL VFNPLGVPSR MNVGQIFECS LGLAGSLLDR HYRIAPFDER YEQEASRKIV
     FSELYEASKQ TANPWAFEPE YPGKSRIFDG RTGKTFEHPV LIGKPYILKL IHQVDDKIHG
     RSIGHYALVT QQPLRGRAKQ GGQRVGEMEV WALEGFGVAH ILQEMLTYKS DHIRARQEVL
     GTTIVGGTIP SPKNAPESFR LLVRELRSLA LELTHFLVSE KNFQVNRKEA
 
 
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