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Database: UniProt
Entry: B7ZIN6_KETDA
LinkDB: B7ZIN6_KETDA
Original site: B7ZIN6_KETDA 
ID   B7ZIN6_KETDA            Unreviewed;      1222 AA.
AC   B7ZIN6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE   AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE            Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN   ECO:0000313|EMBL:BAH11403.1};
OS   Keteleeria davidiana (David's keteleeria) (Pseudotsuga davidiana).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:BAH11403.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Keteleeria.
OX   NCBI_TaxID=3324 {ECO:0000313|EMBL:BAH11403.1};
RN   [1] {ECO:0000313|EMBL:BAH11403.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu C., Chaw S.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH11403.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19166950; DOI=10.1016/j.ympev.2008.12.026;
RA   Wu C.-S., Lai Y.-T., Lin C.-P., Wang Y.-N., Chaw S.-M.;
RT   "Evolution of reduced and compact chloroplast genomes (cpDNAs) in
RT   gnetophytes: Selection toward a lower-cost strategy.";
RL   Mol. Phylogenet. Evol. 52:115-124(2009).
RN   [3] {ECO:0000313|EMBL:BCK60587.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Chaw 1470 {ECO:0000313|EMBL:BCK60587.1};
RA   Wu C.S., Sudianto E., Chaw S.M.;
RT   "Tight association of genome rearrangements with gene expression in conifer
RT   plastomes.";
RL   BMC Plant 21:33-33(2021).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000256|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:0000256|ARBA:ARBA00024550,
CC         ECO:0000256|HAMAP-Rule:MF_01324};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01324}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_01324}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR   EMBL; AP010820; BAH11403.1; -; Genomic_DNA.
DR   EMBL; LC571883; BCK60587.1; -; Genomic_DNA.
DR   RefSeq; YP_002519538.1; NC_011930.1.
DR   AlphaFoldDB; B7ZIN6; -.
DR   GeneID; 7367941; -.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd02655; RNAP_beta'_C; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.1790.20; -; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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   NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:BAH11403.1};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01324};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01324}; Plastid {ECO:0000313|EMBL:BAH11403.1};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01324};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}.
FT   DOMAIN          106..183
FT                   /note="RNA polymerase Rpb1"
FT                   /evidence="ECO:0000259|Pfam:PF05000"
FT   DOMAIN          185..410
FT                   /note="RNA polymerase Rpb1"
FT                   /evidence="ECO:0000259|Pfam:PF04998"
FT   DOMAIN          1032..1119
FT                   /note="RNA polymerase Rpb1"
FT                   /evidence="ECO:0000259|Pfam:PF04998"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1222 AA;  138475 MW;  FE988172A6E524CF CRC64;
     MKIWRFFLMK ERTRLPFDNL PFYNKVMDKT AIKKLISRLI DHFGMTYTSH ILDQLKTSGF
     QQATDTAISL GIDDLLTAPS KGWLVQDAEQ QGSISEKHNH YGNVHAVEKL RQSIEIWYAT
     SEYLRKEMNP NFSMTDPLNP VHVMSFSGAR GNTSQVHQLV GMRGLMSDPQ GQIIDLPIRR
     NLREGLSLTE YIISCYGARK GVVDTAVRTA DAGYLTRRLV EVVQHIVVRI KDCGTIKGIF
     VSPIRGRERD RNEIVVRTQI LIGRVLADDV YINRRCIATR NQDIGVGLAN QLINLRTQSI
     YIRTPFTCKS ISRICQLCYG RSTTHNHLIE LGEAVGIIAG QSIGEPGTQL TLRTFHTGGV
     FTGDIAEHVR APFNGKIEFN ENLVYPTRTC NGHPAYLCHN NLSITIDGKD QVQNLTIPPQ
     SLLLVQNDQY VESEQIIAEV RARTSSFKEK VRKNIYSDLE GEMHWSTNVC HAPEYVHGNV
     HSILRTGYLW ILSGGIYGSG VVPFPFNKHQ DQVDVQLFVA KHQSLSDSYV DQMEHRSGDS
     NCYGKEEKIF SYSETDRTIS NEHQDSIYVT FSPKNYNIKG KKQMNRFIVP LQFDKEWGKR
     RIPCPDAILR IPKSGILQRN SIFGYSNVEY GIPDGPDMTT PFSLSLDLSR EGDNLQIQVS
     NSISYEEDGE RIQVMSDTSI PLVQTCLGFD WEQIDSIESG AYASLTSVKT NKIVSNMIQI
     SLMKYPLFFM GRRDNQASSN LMFHNKLYHT NLFSSNGESQ LISKHQGTIC SLSNGGEDSG
     SFMVLSPSDC FRIVLFNDFK CYDTVNKSNR EDPMRKKIIE FSGLLGHLHS ITNRFPSSHF
     LTYKKVLSKK HSIFHNSLNT FQVPKYYFMD ENTRISHFDP CRNIISNLLG PNWCYSPSEF
     CERTFPVVSP GQFMPESVCI SEHEPLPESG QIIAVDEESL VIRSAKPYLA TRKATVHGHY
     GEILDKGDTL ITLIYERFKS SDIIQGLPKV EQLSEARLNN SISMNLKESF ENWTGDMTRF
     LGSLWGLFIS ARITMEQSQT HLVNQIQKVY RSQGVRICDK HIEIIVRQMT SKVLISEDGT
     ANVFSPGELI GLSRAQRMNR ALEEAIYYQT MLLGITRASL NTQSFISEAS FQETARVLAK
     AALQGRIDWL KGLKENVILG GIIPAGTGQH IRRSGKRNGM DPRMGNRNLF SNKVKDILFH
     HDKVSFFSIQ ENSHNILKQP LK
//
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