RPOC2_NEOYE
ID RPOC2_NEOYE Reviewed; 1226 AA.
AC Q1XDN7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 55.
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 Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX NCBI_TaxID=2788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-51;
RA Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL Submitted (NOV-2003) 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: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; AP006715; BAE92374.1; -; Genomic_DNA.
DR RefSeq; YP_536931.1; NC_007932.1.
DR AlphaFoldDB; Q1XDN7; -.
DR GeneID; 3978931; -.
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; IPR007066; RNA_pol_Rpb1_3.
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; 4.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 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..1226
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000277200"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 297
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"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1226 AA; 136878 MW; 17904518EBD7EBBA CRC64;
MDNRRSLAQP SFSNKVIDTN ELKNLIVWAF RNYGIARAAN MADKLKDLGF HYATQAGISL
SLEDLRIPPS KQSLLLGTIE DIKATENKYR RGEITAVERF QKVIDTWNNA SESLKQEVIK
YFKETDPLNA VSMMAFSGAR GNISQVRQLV GMRGLMADPQ GQIIDLPISS NFREGLTVTD
YFISSYGARK GLVDTALRTA DSGYLTRRLV DVSQDVIIRE VDCKTNKGII LEDLVDTQKI
LINLEQALSG RVLAENVFHP ETNCLIAHTN QDVSPKLAKE ITKAGIKKVL VRSPVTCNSR
SSVCQYCYGW NLAHGRLVDL GEAVGIIAAQ SIGEPGTQLT MRTFHTGGVF TGELAEQIYA
PIDGQLIDLD IESYTDVRTR HGEQALITKK PTQVTIRSKK NQKSIINLSK GTTLLICDGE
LVSKDQVIAE SPRRNRLMTE RAQKHVVSDL SGKICFSNLT VEETDNNQYT TRITKTGGLI
WVLSGEVYSI SDSANVIVHK EDKTKAGTIL AQTELINHYA GEVRIHQNTN SSITNIQVIT
ESIVIPGCYI YTDVIHKKES YILETEKKQK FLFKAIPNQK IQDGYTVAEL ISDTYKTTSG
GIIKYLDLNV SKKKTGLDKD AYEILSPGYI LWISEETHEI NKDSSLILVH NGDVIESGTE
LVKNIFSKSS GIAEIIEKDG IVREIIIKPG SIYKLSEVYS NNDKSRGFLR PGERLHNNIS
TDKLVYWEYI ENEQMPYILI RPVIVYSIPE TKSSLIENLV SQKPSQTKLK LVKRTPFRDG
ERVKSIEGVH LVTTNLVAEI EHRDDNLISS IEFSAKESGN NYFDLRLSTF ETLSIKSIDV
NKSEKQQSQT RIIVKNGEYI KPFTVVASTE IIAMSEGTVE EIYSEKNTSR RILIATSSDK
KTFNIGKSTV KVSVGDWIRC GDFITENMTS LDSGQIIEIS SRSVTLRIAR PYLVSNGAIL
HVDNNALIRR GETLAILVFD RAKTGDIIQG LPRIEEILEA RKKTDVLLNP HDILDASFDL
YIECGLALYE AARLSFQEIQ LLLVKEVQLV YQSQGVNISD KHVEVIVRQM TSKVKIENGE
ETGYLPGELV ELQKIEQTNK AITLRNKINA SYRPVLLGIT QASLNTESFI SAASFQETTK
VLTEAAISGK LDWLRGLKEN VIIGRLIPAG TGFNMYDNCN GSSLEKKNLT ANTNDESTIS
SVRDDLDDII LDDRTARNYF SNKSVE
