ID I6LRJ3_GOSST Unreviewed; 1393 AA.
AC I6LRJ3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, 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:ADZ74725.1};
OS Gossypium sturtianum (Sturt's desert rose) (Gossypium sturtii).
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADZ74725.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=34278 {ECO:0000313|EMBL:ADZ74725.1};
RN [1] {ECO:0000313|EMBL:ADZ74725.1}
RP NUCLEOTIDE SEQUENCE.
RA Shang Mingzhao., Wang Kunbo., Hua Jinping., Liu Fang., Wang Chunying.,
RA Zhang Xiangdi., Wang Yuhong., Li Shaohui.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; JF317356; ADZ74725.1; -; Genomic_DNA.
DR RefSeq; YP_008992885.1; NC_023218.1.
DR GeneID; 18127302; -.
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:ADZ74725.1};
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:ADZ74725.1};
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..365
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1196..1281
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 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 298
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"
SQ SEQUENCE 1393 AA; 158846 MW; E2A86C0AA9D4F0D2 CRC64;
MAERANLVFH NKVIDGTAIK RLISRLIDHF GMAYTSHILD QVKALGFQQA TATSISLGID
DLLTIPSKGW LVQDAEQQSL ILEKHHHFGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
MTDPFNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTTRGISVSP QKRTLPERIF
IQTLIGRVLA DDIYMGPRCI AIRNQDIGLG LVDRFRAFRT QPISIRTPFT CRSTSWICRL
CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE HVRAPFNGKI
KFNEDLVHPT RTRHGHPAFL CYRDLYVIIE SEDIIHKVTI PPKSFLLVQN DQYVESEQVI
AEIRAGTYTL NLKERVRKHI YSDSEGEMHW STDVYHSPEF TYSNVHLLPK TSHLWILSGG
SYKFSVVPFS LHKDQDQINI HYLSAERRYI SRFSANNDQV RHNLFSSDFS DKKEDRIYDY
SELNRIIGTG HCDFIYSAIL HENADLLAKR RRNRFIIPFQ LIQDQEKELM LHSHSGISME
IPINGIFRRK SILAFFDDPR YRRKSSGITK YGTLGAHSIV KREDVIEYRG VKKVKPKYQM
KVDRFFFIPE EVHILSESSS IMVRNNSIIG VDTQITLNTR SRVGGLVRVE RKKKRIELKI
FSGNIYFPGE RDKISRHSGI LIPPGTGKTN SKESKKLKNW IYVQRITPTK KKYFVLVRPV
TPYEIPDGLN LATLFPQDPF REKDNMQLRA VNYILYGNGK PTRRIYDTSI QLVRTCLVLS
WDQDNKSSFA EEVCASFVEV RTNGLIRDFL RIDLVKSHIF YMRKRNDPSA SELISDNRSD
RTNKNPFYSI YSNARIQQSF SQNHGTIHTL LNRNKESQSL LILSSSNCFR MGPFNDVKYH
NVIKQSIKKD PLIPIKNLLG PLGTAPKIAN FYSSFYPLIT HNQTSVAKYL ELDNLKQAFQ
VLNYYLIAEN GRIYNFDPCR NIFLNAVNLN WYFPHHHYHH NYCEETSTII SLGQFICENV
CIAKSGPRLK SGQVFIVQAD SIVIRSAKTY LATPGATVHG HYGEILYEGD TLVTFIYEKS
RSGDITQGLP KVEQVLEVRS IDSISMNLEK RIEGWNECIT RILGIPWGFV IGAELTIVQS
RLSLVNKIQK VYRSQGVQIH NRHIEIIVRQ ITSKVLVSED GMSNVFLPGE LIGLLRAERT
GRALEEAICY RAVLLGITRA SLNTQSFISE ASFQETARVL AKAALRGRID WLKGLKENVV
LGGMIPAGTG FKGLVHRSRQ HNNILLETKK KNFFGGEMRD IFFHHRELFD SCISNNLHDT
SGRSFIGIEF NDS
//
