RPOC2_CYCTA
ID RPOC2_CYCTA Reviewed; 1339 AA.
AC A6H5F7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
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 Cycas taitungensis (Prince sago) (Cycas taiwaniana).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Cycadidae; Cycadales; Cycadaceae; Cycas.
OX NCBI_TaxID=54799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17383970; DOI=10.1093/molbev/msm059;
RA Wu C.-S., Wang Y.-N., Liu S.-M., Chaw S.-M.;
RT "Chloroplast genome (cpDNA) of Cycas taitungensis and 56 cp protein-coding
RT genes of Gnetum parvifolium: insights into cpDNA evolution and phylogeny of
RT extant seed plants.";
RL Mol. Biol. Evol. 24:1366-1379(2007).
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; AP009339; BAF64923.1; -; Genomic_DNA.
DR RefSeq; YP_001312182.1; NC_009618.1.
DR PRIDE; A6H5F7; -.
DR GeneID; 5309622; -.
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..1339
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353558"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 299
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"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1339 AA; 151203 MW; 4DB6EF310C98F8F3 CRC64;
MRRFFPMAER AKLLFHNEAM DKTAMKQLIS RLINHFGMTY TSNISDQLKT SGFQRATDAA
ISLGIDDLLT APSKGWLVQD AEQQGSISEK HHHYGNVHAV EKLRQSIETW YATSEYLRQE
MNPNFRMTDP FNPVHMMSFS GSRGSTSQVH QLVGMRGLVS DPQGQIVDLP IQSNFREGLS
LTEYIISCYG ARKGVVDTAV RTSDAGYLTR RLVEVVQHIV VRKTDCGTIQ GIFVNLIQGR
ERIKNRIVLQ TLIGRVLADD VYIDMRCIAT RNQDIGVGLA HQLITLRAQP IYIRTPSTCK
SLSRICRLCY GRSPTHGNLI ELGEAVGIIA GQSIGEPGTQ LTLRTFHTGG IFTGDIAEHV
RAPFNGKIEF DENLVYPTRT RHGHPAFMCH NNLSITLDGQ DQVHDLTISP QSLLLVQNNQ
YVESEQIIAE VHARTSPSKE KVRKHIYSNL EGEMHWSTNV CHAPEYVQGN VHLILRTSHL
WVLSGGIHGS SAVSFPFHKD QDQVNVQLPL AKHELLPDYS VNQDRMKHKS VDSNFYGKEE
QISSYSEIDR VISNEHWDSI YSTISSDNFN ISGKKQRNRF FVPLRYDKER GNKGISRPNL
IIKISRNGIS QRNDIFAVLD DPRYRINSSG IIKYGTIKVD SIGNKENYLG DQRARGFRSK
DKMKGGRFLF IPEEVHILYE SSSIMVQNNS IIRAGTQITC DIESQVGGLV RIVRIKKKIE
MRILPGDIYF PGEIHGISRH NGTLIPPGKI LFDEFQSENW IYLQWIIPPK EKPFVPVRPV
VEYGIPDGPD ITAPLSLDLL REGDNLQVRV GNFLLYGDGE RIQVINDISI QLVRTYLVLD
WEQKDSMEEA YAYLTEVRTN GIVRNXLQIS LAKYPILYMG KRKNTAGSKS MFHNKLDHAN
PISSNEESQL LSQHQGTIRA LPNEREEGGS LMVLSPSDCS RIVLSKGSKH YDMVNRSIQD
DSMMQIIELS GFLGNLHSIA NRSPSSHSIT YNKYYNISLK EQPIFGNSEN TLRVPKWYFM
DENTVVSNFG PCRNIISDLF NSNRCFPLSK FCENPFPVVS LGQLIRESVR ISEDEPLPGS
GQIIAVHEES LVIRLAELYL ATRRATVHGH YGEIINEGDT LITLIYERFK SGDIIQGLPK
VEQLSEARSI NSISMNLEKS FEDWNRDMTR SLGSPWGSFI SSKITMEQSR IHLVNQIQRV
YRSQGVQISD KHIEIIVRQM TSKVLISGDG MADVFLPGEL IELSRAQRMD RALKEATYYR
TMLLGATRAS LDTQSFISEA GFQETARVLA RAALQGRIDW LKGLKENVIL GGIVPAGTGF
KQSIYHSGER NEIDPRTGK
