ID H2F829_EUCGA Unreviewed; 1343 AA.
AC H2F829;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:AEX94812.1};
OS Eucharis grandiflora (Amazon lily).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEX94812.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Amaryllidoideae; Eucharis.
OX NCBI_TaxID=44989 {ECO:0000313|EMBL:AEX94812.1};
RN [1] {ECO:0000313|EMBL:AEX94812.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22291168; DOI=10.3732/ajb.1100491;
RA Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
RA Pires J.C.;
RT "Quality and quantity of data recovered from massively parallel sequencing:
RT Examples in Asparagales and Poaceae.";
RL Am. J. Bot. 99:330-348(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|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; JQ274974; AEX94812.1; -; 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:SF2; 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:AEX94812.1};
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:AEX94812.1};
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..372
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1147..1233
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 1343 AA; 152265 MW; BEA43DE306720121 CRC64;
MAERADLVFH NKVIDGTAMK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID
DLLTIPSKGW LVQDAEQQSF ILEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
MTDPSNPVHL MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIIVRRTDC GTIRGISVSP RNGMTEKIFV
QTLIGRVLAD DIYMGIRCIA TRNQDIGIGL ANRFITFRAQ PIYIRTPFTC RNTSWICQLC
YGRSPTHGDL VELGEAIGII AGQSIGEPGT QLTLRTFHTG GVFTGGTAEH VRAPSNGKIK
FNEYLVHPTR TRHGHPAFLC SIDLYVTIES RDILHSVNIP PKSLILVQND QYVESEQVIA
EIRAGTSTFH FKERVRKHIY SESEGEMHWS TDVYHAPEYT YSNVHLLPKT SHLWILAGGP
CRSSIVSFSL HKDQDQMNAH SFFVDERYIS DRLITNDRVR HKLLDPSGKK DREILDYSRL
DRIISNGYWN FIYPSILQEN SDFLAKRRRN RFLIPLQYDQ EREKELIPSF GISIEIPING
ILRRNSILAY FDDPRYRRKS SGITKYGIVE VDSIVKKEDL IEYRGAKEFS PKYQMKVDRF
FFFPEEVHIL PGSSSIMVRN NSIIGVDTQL ALNTNTRSRV GGLVRVERKK KSIELKIFSG
DIHFPGETDK ISKHSGILIP PGTEKKNSKE SKKKLKNWIY VQRITPTKKK YFVLVRPVVT
YEIADGINLA KLFPQDLLQE KDNVELKVVN YILYGNGKSI RGISHTSIQL VRTCLVLNWD
QEKKGSIEEV RASFVEVRAN DLIRDFIRIE LVKSTISYVG KRYDTAGSGL IPDNGLDRTN
INPFYSKAKI PLVTQHQGTI GTLLNRNKEG QSLRILSSFN CSRVGPCPFN SSKYNNVAKE
SNPITPIRDL LGPLGTIVPK IVNFYSSYHN PGPCNNIILN PFHLNWCFLH HNYCEETSTI
ISIGQFLYEN ICLVKYGPHI KKSGQILIVH VDSLVIRSAK PYLATPGATV HGHYGEPLSE
GDTLVTFIYE KSRSGDITQG LPKVEQILEV RSIGSISMNL ERRVEGWNER IPRILGIPWG
FLIGAELTIA QSRISLVNKI QKVYRSQGVQ IHNRHIEIIV RQVTSKVLVS EDGMSNVFLP
GELIGLLRAE RAGRALDEAI CYRAILLGIT RASLNTQSFI SEASFQETAR VLAKAALRGR
IDWLKGLKEN VVLGGIIPVG TGFKKLVHRS RQDKNIHLEI KKKNLFELEM RDILLHHREF
FCSCAQNNFH DTPEKSFTRF HNS
//
