RPOC2_ACOCL
ID RPOC2_ACOCL Reviewed; 1386 AA.
AC Q3V544;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 51.
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 Acorus calamus (Sweet flag).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Acoraceae; Acorus.
OX NCBI_TaxID=4465;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15930156; DOI=10.1093/molbev/msi173;
RA Goremykin V.V., Holland B., Hirsch-Ernst K.I., Hellwig F.H.;
RT "Analysis of Acorus calamus chloroplast genome and its phylogenetic
RT implications.";
RL Mol. Biol. Evol. 22:1813-1822(2005).
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; AJ879453; CAI53784.1; -; Genomic_DNA.
DR RefSeq; YP_319755.2; NC_007407.1.
DR AlphaFoldDB; Q3V544; -.
DR PRIDE; Q3V544; -.
DR GeneID; 3677452; -.
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: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..1386
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000225330"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1386 AA; 156831 MW; E159EF0874D2A737 CRC64;
MEVLMAERAD LVYHNKAIDG TAMKRLISRL IDHFGMAYTS HILDQVKTLG FRQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSFILEKHH SYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
PNFRMTDPSN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIRGI SVQPRNGMTE
RMFFQTLIGR VLADDVYIGL RCIAARNQDI GIGLVNRFIT FRAQPVYIRT PFTCRSTSWI
CQLCYGRSPT HGDLVELGEA VGIIAGQSIG EPGTQLTLRT FHTGGVFTGG TAEHVRAPSN
GKIKFNEELV HPTRTRHGHP AFLCSIDLYV TVEGRDIIHN VNIPPKSLIL VQNDQYVESE
QVIAEIRAGT STFNFKERVQ KHIYSESAGE MHWSTDVYHA PEYTYGNVHL LPKTSHLWIL
SGGPYRSSIV SSSLHKDQDQ TNAHSFSVER RYISDLSMTN GRVRHKLFSS DLSGKRGDRI
LDYSRPDQII SKGHWNFIYP SILHENSDFL AKRRKNRFII PFQYDQEGEK ELIPHSGISI
EIPINGMLRR NSILAYFDDT RYRRSSSGIT KYGTVEIDSI VKKEDFIEYR GTKEFSSKYQ
MKVDRFFFIP EEVHILPGSS SIMVRNNSLI GVDTRITLNI RSRVGGLVRV ERKKKNIELK
IVSGDIHFPG ETDKISRHSG ILIPPGTEKK NSKESKTKLK NWIYVQRITP TKKKYFVLVR
PVATYEIADG INLATLFPQD LLQERDNVQL RVVNYILYGN GKPIRGISHT SIQLVRTCLV
LNWDQEQNGS IEGVRASFVE VRANDLIRDF IRIELCKSAI LYTGKRKDIA GSGLIHDNVS
DRTNINPVYL KDKIPSFIQH QGTVGTLLNR NKECQSLILL SSSNCFRIGP FNGSKYHNVP
KESIKEDPII PIRDSLGLLG TTVPKIANFF YLSYHVITHN HILLTKYLLR DHLKQAFQVL
RYCLMDENRR IYNPDPCSNI IFNAFDLNWR FLHHDYSEET STILSLGQFV CENVCLFKHG
PQIKSGQVII VHVDSFVIRA AKPYLATPGA TVHGHYGEIL YGGDTLITFI YEKSRSGDIT
QGLPKVEQVL EVRSIDSIST NLEKRVEGWN EHITKILGIP WGFLIGAELT IAQSRISLVN
KIQKVYRSQG VQIHNKHIEI IVRQITSKVL VSEDGMSNVF SPGELIGLLR AERTGRALEE
AICYRAILLG ITRASLNTQS FISEASFQET ARVLAKAALR GRVDWLKGLK ENVVLGAMIP
VGTGFKALVH RSRKPNNIHL EIKKNNLFEG QVGDDILFYH RELFGSCGPN NFHDTSEQSF
MKFHDS
