ID H6WBU7_9LILI Unreviewed; 1378 AA.
AC H6WBU7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN ECO:0000313|EMBL:AEZ01417.1};
OS Japonolirion osense.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEZ01417.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Petrosaviaceae; Japonolirion.
OX NCBI_TaxID=112799 {ECO:0000313|EMBL:AEZ01417.1};
RN [1] {ECO:0000313|EMBL:AEZ01417.1}
RP NUCLEOTIDE SEQUENCE.
RA Davis J.I., McNeal J.R., Barrett C.F., Chase M.W., Cohen J.I., Duvall M.R.,
RA Givnish T.J., Graham S.W., Petersen G., Pires J.C., Seberg O.,
RA Stevenson D.W., Leebens-Mack J.;
RT "Contrasting Patterns of Support among Plastid Genes and Genomes for Major
RT Clades of the Monocotyledons.";
RL Bot. J. Linn. Soc. 0:0-0(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|HAMAP-Rule:MF_01324}.
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,
CC ECO:0000256|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01324};
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_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR EMBL; JQ068961; AEZ01417.1; -; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR PANTHER; PTHR34995; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR PANTHER; PTHR34995:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AEZ01417.1};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01324};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Plastid {ECO:0000313|EMBL:AEZ01417.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}.
FT DOMAIN 97..161
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 176..368
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1182..1267
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1378 AA; 156410 MW; 444053E859A2AEFD CRC64;
MEVLMAERAD LVFHNKVIDG TAMKRLISRL IDHFGMAYTS HILDQVKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSFLLEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
PNFRMTDPSN PVHLMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIIVR RTDCGTIRGI SVSPLNGMTE
NIFIQTLIGR VLADDIYIGP RCIATRNQDI GIGLVNRFIT FRAQPIYIRT PFTCRSTSWI
CQLCYGRSST HGDLVELGEA VGIIAGQSIG EPGTQLTLRT FHTGGVFTGG TAEHVRAPSN
GKIKFNEDLL HPTRTRHGHP AFLCSIDLYV TIESQDIIHN VNIPPKSLIL VQNDQYVESE
QVIAEIRAGA PTLNFKERVR KHIYSESEGE MHWSTDVYHA PEYTYGNVHL LPKTSHLWIL
AGGPCRSSIV SFSLHKDQDQ MNVHSFFSLE ERYISDLSMT NDRVRHKLSD TSGKRERETL
DYSRPDRIIS NGHWNFIYPS IFQENSDFLA KRRRNRFIIP LQYDQEREKE LIPRFGISIE
IPINGILRRN SILAYFDDPR YRRSSSGITK YGTVEVDSIV KKEDLIEYRG AKEFSPKYQM
KVDRFFFIPE EVYILPGSSS IMVRNNSIIG VDTRITLNTR SRVGGLVRVE RKKKSIELKI
FSGDIHFPGE TDKISRHSGI LIPPGTGKKN PKESKKLKNG IYVQRITPTK KKYFVSVRPV
VTYEIADGIN LATLFPQDLL QEKDNVQLRV VNYILYGNGK SIRGIYHTSI QLVRTCLVLN
WDQEQNGSIE EVHASFVEVR ANDLIRDFIK MELAKPTISY TGKRNDIAGS VWIPNNGLDR
TNINPFYSKA KIQPLTQHQG TIGIGTLLNR NKECQSLIIL SSSNCSRIGP FNGSKYNKSD
PIIPIRDLLG PLGTIVPKIA NFYSSYHLIT HNQILLKKYL LLDNFKRTSQ VLKYCLMDEN
GRIYNPDPCS NIILNPFNLN WRFLHHYYCE ETYTIISLGQ FICENVCLFK YGPHIKKSGQ
ILIVHVDSLV IRSAKPYLAT PGATVHGHYG EILYEGDTLV TFIYEKSRSG DITQGLPKVE
QVLEVRSVDS ISMNLEKRVE GWNERIPRIL GIPWGFLIGA ELTIAQSRIS LVNKIQKVYR
SQGVQIHNRH IEIIVRQVTS KVLVSEDGMS NVFSPGELIG LLRAERAGRV LDEAICYRAI
LLGITRASLN TQSFISEASF QETARVLAKA ALRGRIDWLK GLKENVVLGG IIPVGTGFIK
LVHRSRQDKN IHLEIKKKNL FEVEMRDILF HHRELFCSCI PNNFHEPSEQ SFTRFNDS
//