ID   A0A8K1HNH0_9MAGN        Unreviewed;      1073 AA.
AC   A0A8K1HNH0;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   27-NOV-2024, entry version 7.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01321};
DE   AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01321};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE            Short=RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000256|HAMAP-Rule:MF_01321,
GN   ECO:0000313|EMBL:UBN07738.1};
GN   ORFNames=Lod_N6912Cp012 {ECO:0000313|EMBL:UBN07738.1},
GN   LorDel_N4678Cp012 {ECO:0000313|EMBL:UBN07673.1};
OS   Loranthus delavayi.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:UBN07738.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Santalales; Loranthaceae; Lorantheae; Loranthinae; Loranthus.
OX   NCBI_TaxID=227897 {ECO:0000313|EMBL:UBN07738.1};
RN   [1] {ECO:0000313|EMBL:UBN07738.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nickrent D.L., Su H.-J., Lin R.-Z., Devkota M.P., Hu J.-M., Glatzel G.;
RT   "Examining the Needle in the Haystack: Evolutionary Relationships in the
RT   Mistletoe Genus Loranthus (Loranthaceae).";
RL   Syst. Bot. 46:403-415(2021).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000256|ARBA:ARBA00004026, ECO:0000256|HAMAP-Rule:MF_01321,
CC       ECO:0000256|RuleBase:RU363031}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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         ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031};
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:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|HAMAP-Rule:MF_01321,
CC       ECO:0000256|RuleBase:RU000434}.
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DR   EMBL; MT987625; UBN07673.1; -; Genomic_DNA.
DR   EMBL; MT987626; UBN07738.1; -; Genomic_DNA.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1100.10; -; 1.
DR   Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1.
DR   Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 2.
DR   Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR   Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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; 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; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR   PANTHER; PTHR20856:SF20; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:UBN07738.1};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01321};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01321}; Plastid {ECO:0000313|EMBL:UBN07738.1};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01321};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01321}.
FT   DOMAIN          128..317
FT                   /note="RNA polymerase Rpb2"
FT                   /evidence="ECO:0000259|Pfam:PF04561"
FT   DOMAIN          378..447
FT                   /note="RNA polymerase Rpb2"
FT                   /evidence="ECO:0000259|Pfam:PF04565"
FT   DOMAIN          586..982
FT                   /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00562"
FT   DOMAIN          984..1059
FT                   /note="RNA polymerase Rpb2"
FT                   /evidence="ECO:0000259|Pfam:PF04560"
SQ   SEQUENCE   1073 AA;  122308 MW;  4CF82B65398FEECE CRC64;
     MLWDGNEGMY TIPGLNQIQF EGFCRFIDRG LMEKLYKFPK IKDADQEIEF QLFVETYQLV
     EPLIKERDAV YESLTYSSEL YVYSGLIWKT SRDMEEQTIF IGNIPLMNSL GTSIVNGIYR
     IVINQILQSP GIYYRSELDH NGISAYTATI ISDWGGRLEL EIDKKERMWA RVSRKQKISI
     LVLSSAMGSH LRQILENVCY PEIFLSFLNL NEKEKRRIGA KENATLEFYR QFFCISGDPG
     FSESLCKELQ QKFFQQKCEL GSIGRRNMNQ RLKLDIPQNN LFLLPRDILA AADHLIRMKL
     EMCTLDNMNH LKNKRIRSVA DLLQDQLGLA LVRLENFVQG TICRAIRHKW TPTPHNLVTS
     TPLTITYEYF FGLHPLSQVL DRTNPLTQIV HGRKSSHLGP GGLTERAASC FPIRDIHPSH
     YGRICPIDTS EGINVGLIGS LAIYARIGRW GSLESLFYVY EISAKKMRML YLSSSMDESY
     MVAAVNSLVL NLSIQEEQLV PARYRQEFLT IAWEQVHLRS IFPFQYFSIG ASLIPFIEHN
     DANRALMSSN MQRQAVPLSR SERCIVGTGL ERQAALDSGV PVMAERGGKI ISTDTDKILL
     SDSVETLSIS LIMYQRSNKN TCMYQKPKVW KDKCIKRGHI LADGTATVGG ELALGKNVLV
     AYMPWGGYNF EDAVLISERL VYKDIYTSFN IQKYEIKTHV TRQGPEKITT KIPHLESHLL
     RNLDKKGVVM LGSWVEAGDI LVGKLTPQMV KKLSYAPEDK LVRTILGIQV STSKETCLKL
     PTGGRGKVID VRWYCRKGGY NYNPETICVY ILQKREIKVG DKVAGRHGNK GIISKILPIQ
     DMLYLQDGRP VDMVFNPLGV PSRMNVGQIF ECSLGLAGSL LDRHYRIGAF DERYEQEASR
     KLVFSELYEA SRQRVNPWVF EPEYPGKSRI FDGRTGDSFD QPVIIGNPYI FKLIHQVDDK
     IHGRSSGHYA LVTQQPLRGR AKRGGQRVGE MEVWALEGLG VAHILQEMLT YKSDHIRARQ
     EVLGTTIVGR TISNPEDAPE SFRLLVRELR SLALEMNHFL VSEKNFRINR KEV
//