ID U5KCR4_LILLO Unreviewed; 1374 AA.
AC U5KCR4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:AGQ55749.1};
OS Lilium longiflorum (Trumpet lily).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AGQ55749.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX NCBI_TaxID=4690 {ECO:0000313|EMBL:AGQ55749.1};
RN [1] {ECO:0000313|EMBL:AGQ55749.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23950788;
RA Kim J.S., Kim J.H.;
RT "Comparative Genome Analysis and Phylogenetic Relationship of Order
RT Liliales Insight from the Complete Plastid Genome Sequences of Two Lilies
RT (Lilium longiflorum and Alstroemeria aurea).";
RL PLoS ONE 8:E68180-E68180(2013).
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|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; KC968977; AGQ55749.1; -; 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; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR PANTHER; PTHR48355: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:AGQ55749.1};
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:AGQ55749.1};
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 93..157
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 172..382
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1183..1268
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1374 AA; 156636 MW; FD68B7B322B17ED2 CRC64;
MAERVDLVFH NKVIDRTAMK RLISRLIDHF GMAYTSHILD QMKTLGFQQA TVTSISLGID
DLLTIPSKGW LVRDAEQQSF FLEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
MTDPSNPVHL MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIIIRRIDC GTIQGISVSP RNEMTERIFV
QTLIGRVLAD DIYIGLRCIA TRNQDIGIGL INRFITFRAR PIYIRTPFTC RSTSWICQLC
YGRSPTHGDL AELGEAVGII AGQSIGEPGT QLTLRTFHTG GVFTGGTAEH VRAPSNGKIK
FNEDFVHPTR TRHGHPAFLC SIDLYVIIES RSVIHNVNIP PKSLILVQNN QYVESEQVIA
EIRAGTSTFH FKEKVRKHIY SESEGEMHWS TGVYHAPEYT YGNVHLLPKT SHLWILAGGP
RGSSIMSFSI HKDQDQINAH SFSVEDKYIS DLSMTNDRVR HKLLDTSSKK DMEIIDYSIS
NRIISNGKWN LIYPSILQDN SDLLAKRRKN GFIIPLKYDQ EWQKELISCF GISIEIPING
ILRRNSILAY FDDPRYRRSS SGITKYGTAE VDSIIKKEDL IEYRGTKELS LKYQMKVDRF
FFIPEEVHIL PGSSSIMVRN NSIIRVYTRL ALNKRSRIGG LVRVERKKKS IELRIFYGDI
HFPGETDKIF RHCGILIPPV TGKKKNSKES KKLKDWIYVQ RITPTKKKYF VSVRPVVTYE
IADGINLATL FPQDLLREKD DVQLRIVNYI LYEYGKSIRR IYNTSIQLVR TCLVLNWDQK
QNGSKKEVYA SFVEVRANDL IRDFIRIELV KVKSTLSYSG KRYNITDSGL IPNKGLDRAN
INPFHSKGKF QLLTQQQETI GTLLNQHKEC QSFIILSSSN CFRISPFKGS KYNNAILDPL
IPIRYLLGPL GTIVSKITNF YSSYHLLTHN QISLKKYLLL NNFKQTFKVL QVLKYCLMDE
NRRIYNPNSC SNIILNPFHL NCCFLHHDSG EETSTIICLG QFICENACLF KYGPHIKKSG
QILIVHVDSL VIRSAKPYLA TPGATVHGHY GEILYEGKTL VTFIYEKSRS GDITQGLPKV
EQVLEVRSID SISMNLEKRV ESWNERIPRI LGIPWGFLIG AELTIAQSRI SLVNKIQKVY
RSQGVQIHNR HIEIIVRQIT SKVLVSEDGM SNVFSPGELI GLLRAERAGR ALDEAINYRA
ILLGITRTSL NTQSFISEAS FQETARVLAK AALRGRIDWL KGLKENVVLG GLIPVGTGFK
KLVHHSRENK NIYLEIKRKN LFELEMGDIL LYHRELCAPN NFHGTSQQPF TRFS
//
