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RPOC2_EUGGR
ID   RPOC2_EUGGR             Reviewed;         830 AA.
AC   P23581;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'';
DE            EC=2.7.7.6;
DE   AltName: Full=PEP;
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'';
DE            Short=RNA polymerase subunit beta'';
GN   Name=rpoC2;
OS   Euglena gracilis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Z / UTEX 753;
RX   PubMed=2110656; DOI=10.1093/nar/18.7.1869;
RA   Yepiz-Plascencia G.M., Radebaugh C.A., Hallick R.B.;
RT   "The Euglena gracilis chloroplast rpoB gene. Novel gene organization and
RT   transcription of the RNA polymerase subunit operon.";
RL   Nucleic Acids Res. 18:1869-1878(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z / UTEX 753;
RX   PubMed=8346031; DOI=10.1093/nar/21.15.3537;
RA   Hallick R.B., Hong L., Drager R.G., Favreau M.R., Monfort A., Orsat B.,
RA   Spielmann A., Stutz E.;
RT   "Complete sequence of Euglena gracilis chloroplast DNA.";
RL   Nucleic Acids Res. 21:3537-3544(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-830.
RC   STRAIN=Z / UTEX 753;
RX   PubMed=6277930; DOI=10.1016/s0021-9258(19)81105-5;
RA   Orozco E.M., Hallick R.B.;
RT   "Euglena gracilis chloroplast transfer RNA transcription units. II.
RT   Nucleotide sequence analysis of a tRNAVal-tRNAAsn-tRNAArg-tRNALeu gene
RT   cluster.";
RL   J. Biol. Chem. 257:3265-3275(1982).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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:0000250|UniProtKB:P0A8T7};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X17191; CAA35054.1; -; Genomic_DNA.
DR   EMBL; X70810; CAA50136.1; -; Genomic_DNA.
DR   EMBL; M22010; AAA84228.1; -; Genomic_DNA.
DR   PIR; S19259; RNEGB2.
DR   RefSeq; NP_041949.1; NC_001603.2.
DR   AlphaFoldDB; P23581; -.
DR   GeneID; 807500; -.
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:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
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; 4.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..830
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067923"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   CONFLICT        593
FT                   /note="I -> II (in Ref. 3; AAA84228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        688
FT                   /note="L -> R (in Ref. 3; AAA84228)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   830 AA;  94757 MW;  BEF9A964B70F68B8 CRC64;
     MNFGNIVCFN RVFDKNEIRN LISWFLSNYG SIRTKELLDK MKNFGFTYAT TTGLSLGLGD
     LKIPSSKANL VKSSEKILFK TRNRYKNGMI NFINVLDEER DIWNVVNENL KKESINNLRQ
     SDFLNPLYSM TLSGARGSIT QVKQLIGMRG LMSDSQGNVI PFPIKTNFKE GLNITEYFVS
     CYGARKGLID TALKTANAGY LTRRMIYTAQ NLIVKRSDCF TKYNTCVLLQ NQDKEELKFL
     KEKLIGRVLA KTIVNAKTGD ILVSAGQDIC NYTFKKIINF PEVYIRTPFN CVLMEGICQI
     CYGWNLACGK MVELGECVGI LAAQSIGEPG TQLTMRTFHT GGVFSAKAKE VITSPLNGKI
     WYDLNTGLRR VYNKFKEKAF LTLQEKKIVI YENDVSKSIM FLPSSTLLYV KPGRKIFDKQ
     IIGESVNSNL KNDVFGIEEI RDVKAKISGQ IFFPQINSKQ FGKIFWIISS IIMSFTSLFF
     HLTKKFSFKN KLICPTTNVH KKELFVNRKK ELFPRKFGKL FINIRNVNSL VDKSKVLKKR
     SSHIITCILD QDKVIMLRNL KKQKRIFGNF KIGCFLKTGQ IISNFKLLHS SQIIQERKEF
     SIFRKVMPFS TNDDTLMRIE DKPFIRKNQL LYRVNFVREK TYDIVQGLPK VEKLLEARMT
     SSLKEIINNP HDILTESFFT FLDDYENLVA ARKSFEVIQK YLIDGVQTVY KSQGVKIADK
     HIELIVKQIT SKVIVTNPGD SSFMVGDFLD LNLVEVLNKR LVNSIVYEPI IMGLTRFSLS
     SQSFIAQASF QETTRVLTKA ALQGRADWLS GLKENLVLGN IIPAGTGFKN
 
 
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