ID J3RPY0_ORYSI Unreviewed; 1513 AA.
AC J3RPY0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:AER12974.1};
OS Oryza sativa subsp. indica (Rice).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AER12974.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:AER12974.1};
RN [1] {ECO:0000313|EMBL:AER12974.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22870184; DOI=10.1371/journal.pone.0042041;
RA Zhang T., Hu S., Zhang G., Pan L., Zhang X., Al-Mssallem I.S., Yu J.;
RT "The Organelle Genomes of Hassawi Rice (Oryza sativa L.) and Its Hybrid in
RT Saudi Arabia: Genome Variation, Rearrangement, and Origins.";
RL PLoS ONE 7:E42041-E42041(2012).
RN [2] {ECO:0000313|EMBL:ANG44646.1}
RP NUCLEOTIDE SEQUENCE.
RA Ulaganathan K., Mettu M.R.;
RT "Sequencing of chloroplast genome of Oryza sativa indica cultivar RP Bio-
RT 226.";
RL Submitted (FEB-2016) 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; JN861109; AER12887.1; -; Genomic_DNA.
DR EMBL; JN861110; AER12974.1; -; Genomic_DNA.
DR EMBL; KU705873; ANG44646.1; -; Genomic_DNA.
DR RefSeq; YP_654208.1; NC_008155.1.
DR GeneID; 4126924; -.
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:AER12974.1};
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:AER12974.1};
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..355
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1317..1364
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 644..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..704
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..763
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1513 AA; 173707 MW; 559EE8F4C89327AC CRC64;
MAERANLVFQ NKEIDGTAMK RLISRLIDHF GMGYTSHILD QIKTLGFHQA TTTSISLGIE
DLLTIPSKGW LVQDAEQQSF LLEKHYYYGA VHAVEKLRQS VEIWYATSEY LKHEMNSNFR
ITDPSNPVYL MSFSGARGNA SQVHQLVGMR GLMADPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTADAG YLTRRLVEVV QHIIVRRRDC GTIQAISVSP QNGMTEKLFV
QTLIGRVLAN DIYIGSRCIA TRNQDIGIGL VNRFITTFRA QPFRAQPIYI RTPFTCRSTS
WICQLCYGRS STHGDLVELG EAVGVIAGQS IGEPGTQLTL RTFHTGGVFT GGTADLVRSP
SNGKIQFNGD LVHPTRTRHG QPAFLCYIDL HITIQSQDIL HSVTIPSKSL ILVQNDQYVE
SEQVIAEIRA GTSALHFKEK VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW
ILSVSMCRSS IASFSLHKDQ DQMNTYSFSV DGRYIFGLSM ADDEVRHRLL DTFGKKDREI
LDYSTPDRIM SNGHWNFVYP SILQNNFDLL AKKRRNRFAI PLQYHQEQEK EPISCFGISI
EIPFMGVLRR NTIVAYFDDP RYKKDKKGSG IVKFRYRTLE DEYRTREKDS ENEYGSPENE
YRTREEECKT LEDEYRTREE EYETLEDEYG IPENEYETLE DEYGILEDEY RTREEESEDE
YGSPENKYRP REDKYGTLEE DSEDEHGTLE EDSEEDSEDE YGNPEEDSVL KKGVLIEHRG
TKEFSLKYQK EVDRFFFILQ ELHILPRSSS LKVLDNSIIG VDTQLTKNTR SRLGGLVRVK
RKKSHTELKI FSGDIHFPEE ADKILGGSLI PLEREKKDSK ESKKRENWVY VQWKKILKSK
EKYFVLVRPA VAYEMNEGRN LATLFPQDLL QEEGNLQLRL VNFISHENSK LTQRIYHTNS
QFVRTCLVLN WEQEEKEEAR ASLVEIRANG LIRDFLRIGL IKSTISYTRK RYDSRSAGLI
LHNRLDRTNT NSFYSKAKIQ SLSQHQEAIG TLLNRNKEYQ SLMVLSASNC SRIGFFKNSK
NPNGVKESNP RIPIPKFLGL FRNFSGLLGT IAPSISNFSS SYYLLTYNQI LLKKHLLLDN
LKQNFKVLQG LKHSLINENQ RTSNFDSNIM LDPFQLNWHF LPHDSWEETS AKIHLGQFIC
ENVCLFKSHI KKSGQIFIVN IDSFVIRAAK PYLATTGATV HGHYGEILYK GDRLVTFIYE
KARSSDITQG LPKVEQIFEA RSIDSLSPNL ERRIEDWNER IPRILGGPWG FLIGAELTIA
QSRISLVNKI QKVYRSQGVQ IHNRHIEIII RQVTSKVRVS EDGMSNVFSP GELIGLLRAE
RAGRALDESI YYRAILLGIT RVSLNTQSFI SEASFQETAR VLAKAALRGR IDWLKGLKEN
VVLGGIIPVG TGFQKFVHRY PQDKNLYFEI QKKKLFASEM RDILFLHTEL VSSDSDVTNN
FYETSESPFT PFI
//
