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RPOC2_ORYNI
ID   RPOC2_ORYNI             Reviewed;        1513 AA.
AC   Q6ENI2;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SL10 {ECO:0000312|Proteomes:UP000006591};
RX   PubMed=15556301; DOI=10.1016/j.gene.2004.06.008;
RA   Masood M.S., Nishikawa T., Fukuoka S., Njenga P.K., Tsudzuki T.,
RA   Kadowaki K.;
RT   "The complete nucleotide sequence of wild rice (Oryza nivara) chloroplast
RT   genome: first genome wide comparative sequence analysis of wild and
RT   cultivated rice.";
RL   Gene 340:133-139(2004).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01324}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR   EMBL; AP006728; BAD26770.1; -; Genomic_DNA.
DR   RefSeq; YP_052741.1; NC_005973.1.
DR   AlphaFoldDB; Q6ENI2; -.
DR   STRING; 4536.ONIVA03G24830.1; -.
DR   GeneID; 2885930; -.
DR   eggNOG; ENOG502QPYA; Eukaryota.
DR   Proteomes; UP000006591; Chloroplast.
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:0009536; C:plastid; IC:Gramene.
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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR   InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR   TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..1513
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067936"
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:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1513 AA;  173741 MW;  53DD1DDF1F1BEF02 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 RIPIPKFFGL 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
 
 
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