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RPOB_MARPO
ID   RPOB_MARPO              Reviewed;        1065 AA.
AC   P06272;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 125.
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   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2974085; DOI=10.1016/0022-2836(88)90002-2;
RA   Umesono K., Inokuchi H., Shiki Y., Takeuchi M., Chang Z., Fukuzawa H.,
RA   Kohchi T., Shirai H., Ohyama K., Ozeki H.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   II. Gene organization of the large single copy region from rps'12 to
RT   atpB.";
RL   J. Mol. Biol. 203:299-331(1988).
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, chloroplast.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; X04465; CAA28061.1; -; Genomic_DNA.
DR   PIR; A00691; RNLVB.
DR   RefSeq; NP_039275.1; NC_001319.1.
DR   AlphaFoldDB; P06272; -.
DR   SMR; P06272; -.
DR   GeneID; 2702533; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IEA:EnsemblPlants.
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:0035196; P:miRNA processing; IEA:EnsemblPlants.
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; -; 1.
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   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..1065
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048030"
SQ   SEQUENCE   1065 AA;  120447 MW;  0BB0AF013A9D3FC3 CRC64;
     MEIFILPEFG KIQFEGFNRF INQGLSEELS NFPIIEDIDQ EFEFQIFGEQ YKLAEPLLKE
     RDAVYQSITY SSDVYVPAQL TQKKKGKIQK QIVFLGSIPL MNSQGTFVVN GVARVIINQI
     LRSPGIYYNS ELDHNGIPIY TGTLISNWGG RLKLEIDGKT RIWARISKKR KVSILVLLLA
     MGLNLQNILD SVCYPKIFLE FIKKNTKKEY PNSTEDAIVE LYKHLYCIGG DLFFSESIRK
     ELQKKFFQQR CELGKIGRLN LNKKLNLNVP ENEIFVLPQD ILAAVDYLIK LKFGIGTIDD
     IDHLKNRRVC SVADLLQDQL KLALNRLENS VLFFFRGATK RKRLPTPKSL VTSTPLIMTF
     KEFFGSHPLS QFLDQTNPLT EIVHKRRLSS LGPGGLTRRT ASFQVRDIHA SHYGRICPIE
     TSEGMNAGLI ASLAIHAKIS ILGCLESPFY KISKLSNLEE IINLSAAEDE YYRIATGNCL
     ALDQNSQEEQ ITPARYRQDF VAIAWEQVHL RSIFPLQYFS VGASLIPFLE HNDANRALMG
     SNMQRQAVPL LKPEKCIVGT GIESQTALDS GSVTVSSHGG KIEYLDGNQI ILSLKKKKID
     KNLIIYQRSN NSTCMHQKPK VEKQKYIKKG QILADGAATA NGELALGKNI LVAYMPWEGY
     NFEDAILINE RLIYEDIYTS IHIERYEIEA RVTSQGPEKF TNEIPHLDDY LLRHLDQNGI
     VLTGSWVETG DVLVGKLTPQ ETEENLRAPE GKLLQAIFGI QVATSKETCL KVPPGGRGRV
     IDIRLISQED NSANTAQIIH IYILQKRKIQ IGDKVAGRHG NKGIISKILP RQDMPFLQDG
     TPIDMILSPL GVPSRMNVGQ IFECLLGLAG SFLHKNYRII PFDERYEREA SRKLVFSELY
     KASKKTTNPW LFEPDNPGKN RLIDGRTGEI FEQPITIGKA YMLKLIHQVD DKIHARSSGP
     YALVTQQPLR GRSRRGGQRV GEMEVWALEG FGVAYILQEM LTIKSDHIRA RYEVLGAIVT
     GEPIPKPNTA PESFKLLVRE LRSLALEINH VIICEKNLKL KLKEI
 
 
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