RPOC2_ORYSA
ID RPOC2_ORYSA Reviewed; 1513 AA.
AC P0C507; P12093; Q6QY81;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 sativa (Rice).
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=4530;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PA64s;
RX PubMed=15122023; DOI=10.1104/pp.103.031245;
RA Tang J., Xia H., Cao M., Zhang X., Zeng W., Hu S., Tong W., Wang J.,
RA Wang J., Yu J., Yang H., Zhu L.;
RT "A comparison of rice chloroplast genomes.";
RL Plant Physiol. 135:412-420(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; AY522331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C507; -.
DR SMR; P0C507; -.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..1513
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067937"
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; 173779 MW; 5C7B00A636757A09 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 RIPIPKFWGL 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 PQNKNLYFEI QKKKLFASEM RDILFLHTEL VSSDSDVTNN
FYETSESPFT PFI
