ID T1QPH2_CORGM Unreviewed; 1394 AA.
AC T1QPH2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:AGC58977.1};
GN ORFNames=CGUM_CP_p011 {ECO:0000313|EMBL:AGC58977.1};
OS Corymbia gummifera (Red bloodwood) (Eucalyptus gummifera).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AGC58977.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Corymbia.
OX NCBI_TaxID=183803 {ECO:0000313|EMBL:AGC58977.1};
RN [1] {ECO:0000313|EMBL:AGC58977.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23876290;
RA Bayly M.J., Rigault P., Spokevicius A., Ladiges P.Y., Ades P.K.,
RA Anderson C., Bossinger G., Merchant A., Udovicic F., Woodrow I.E.,
RA Tibbits J.;
RT "Chloroplast genome analysis of Australian eucalypts--Eucalyptus, Corymbia,
RT Angophora, Allosyncarpia and Stockwellia (Myrtaceae).";
RL Mol. Phylogenet. Evol. 69:704-716(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; KC180800; AGC58977.1; -; Genomic_DNA.
DR RefSeq; YP_008577568.1; NC_022407.1.
DR GeneID; 17083477; -.
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:AGC58977.1};
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:AGC58977.1};
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..367
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1199..1284
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 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1394 AA; 158518 MW; 761B2C995AE7D032 CRC64;
MEVLMAERVN LVFHNKVIDG TAIKRLISRL IDHFGMAYTS HVLDQVKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEVWYA TSEYLRQEMN
PNFRMTDPFN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIRGV SVSSRNGMMP
ERIFIQTLIG RVLADDIYMG PRCIAIRNQD IGIGLVNRFI TFRTQPISIR TPFTCRSTSW
ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIKFNDDL VHPTRTRHGH PAFLCSIDLY VTIESEDILH KVTIPPKSFL LVQNNQYVES
EQVIAEIRAG TYTFNLKERV RKHIYSESEG EMHWSTDVYH APEFTYSNVH LLPKTSHLWI
LSGGSCRSSG VPFSLYKDQD QMNLRSTERE RRYISSLSVN NDQMRYELCS SDFSGKIKED
RIPDYSELNR IISIVHCNLK YPTTFHENSD LLAKRRRNRF LIPLESIQER KKELMPHSGI
SIELPINGIL RRKSILAYFD DPRYRRKSSG ITKYGTLGVH SVVKKEDLIE YRGIKEFKQK
CQMKLDRFFF IPEEVHIFPE SSSIMVRNNS LIEVDTRIAL NTRSRVGGLV RVERKKKRIE
LKIFSGDIHF PGETDKISRH SGILIPPGTG KTNSKESKKW KNGIYVQRIT PTKKKYFVLV
RPVVTYEVSD GINLATLFPP DLLQERDNMQ LRVVNYIVYR NGKPIRGISD TSIQLVRTCL
ILNWDQDKKS SSIEEAHTSF VEVSTNGLIR DFLRIDLVKF PISYLRKRND PSGSGLISDS
DNVSDHTNNN PFYSKTKIQQ LLSQNQGTIR TLLNKNKECP SLIILSSSNC FRMGPFNAGK
YHNVIKESIS IKKDPIIKIR NSIGPLGTVL QFVNFYSFYY LITHNPILVT KYLQLENLKQ
TFQVINYYLM DENGRILNPD SCSNIVLNSF NLNWYFLHHN YYHNYFEERS TIISLGQFIC
ENVCISKNGP HLKSGQVLIV QVDSVVIRSA KPYLATPGTT VHGHYGEILY EGDTLVTFIY
EKSRSGDITQ GLPKVEQVLE VRSIDSISMN LEKRIEGWNE HIKQILGIPL GFLIGAELTI
VQSRISLVNK IQKVYRSQGV QIHNRHIEII VRQITSKVLV SEDGMSNVFL PGELIGLLRA
ARTGRALEES ICYRAILLGI TRASLNTQSF ISEASFQETA RVLAKAALRG RIDWLKGLKE
NVVIGGMIPV GTGFKGLVHR SRQHKNIPLK TKKKNFFEGE IGDILFHHRE LFDSSISKKF
HDTSEQSFRG FNDS
//
