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RPOC2_TOBAC
ID   RPOC2_TOBAC             Reviewed;        1392 AA.
AC   P38550;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 99.
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   Nicotiana tabacum (Common tobacco).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Bright Yellow 4;
RX   PubMed=16453699; DOI=10.1002/j.1460-2075.1986.tb04464.x;
RA   Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N.,
RA   Matsubayashi T., Zaita N., Chunwongse J., Obokata J.,
RA   Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M.,
RA   Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A.,
RA   Tohdoh N., Shimada H., Sugiura M.;
RT   "The complete nucleotide sequence of the tobacco chloroplast genome: its
RT   gene organization and expression.";
RL   EMBO J. 5:2043-2049(1986).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=8400137; DOI=10.1007/bf00028992;
RA   Olmstead R.G., Sweere J.A., Wolfe K.H.;
RT   "Ninety extra nucleotide in ndhF gene of tobacco chloroplast DNA: a summary
RT   of revisions to the 1986 genome sequence.";
RL   Plant Mol. Biol. 22:1191-1193(1993).
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; Z00044; CAA77410.1; -; Genomic_DNA.
DR   PIR; A05028; A05028.
DR   RefSeq; NP_054486.2; NC_001879.2.
DR   AlphaFoldDB; P38550; -.
DR   GeneID; 800532; -.
DR   KEGG; nta:800532; -.
DR   OrthoDB; 731145at2759; -.
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..1392
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067952"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1392 AA;  157313 MW;  A42BFE7048E0ACE1 CRC64;
     MEVLMAERAN LVFHNKAING TAMKRLISRL IDHFGMAYTS HILDQVKTLG FQQATATSIS
     LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
     PNFRMTDPFN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
     EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTARGI SVSPRNGMMP
     ERIFIQTLIG RVLADDIYMG PRCIATRNQD IGIGLVNRFI TFRAQPISIR TPFTCRSTSW
     ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
     NGKIKFNEDL VHPTRTRHGH PAFLCSIDLY VTIESEDILH NVNIPPKSLL LVQNDQYVES
     EQVIAEIRAG ISTLNFKEKV RKHIYSDSDG EMHWSTDVYH APEFTYGNVH LLPKTSHLWI
     LLGRPCRSSL VYLSIHKDQD QMNAHFLSGK RRYTSNLSVT NDQARQKLFS SDFSGKKEDR
     IPDYSDLNRI ICAGQYNLVY SPILHENSDL LSKRRRNKFI IPLHSIQELE NELMPCSGIS
     IEIPVNGIFR RNSILAYFDD PRYRRKSSGI IKYGTVETHS VIKKEDLLEY RGVKEFRPKY
     QMKVDRFFFI PEEVHILPGS SSIMVRNNSI VGVDTQITLN LRSRVGGLVR VERKKKRIEL
     KIFSGDIHFP GETDKISRHT GVLIPPGTGK RNSKESKKVK NWIYVQRITP SKKKFFVLVR
     PVVTYEITDG INLATLFPPD PLQERDNVQL RIVNYILYGN GKPIRGISDT SIQLVRTCLV
     LNWNQDKKSS SCEEARASFV EIRTNGLIRH FLRINLVKSP ISYIGKRNDP SGSGLLSDNG
     SDCTNINPFS SIYSYSKAKI QQSINQPQGT IHTLLNRNKE CQSLIILSAA NCSRMGPFKD
     VKYHSVIKKS IKKDPLIPIR NSLGPLGTSL PIENFYSSYH LITHNQILVT NYLQLDNLKQ
     TFQVIKFKYY LMDENGKIFN PDPCRNIILN PFNLNWYFLH HNYCEETSKI ISLGQFICEN
     VCIAKNGPPL KSGQVILVQV DSIVIRSAKP YLATPGATVH GHYGETLYEG DTLVTFIYEK
     SRSGDITQGL PKVEQVLEVR SVDSISMNLE KRIEGWNKCI TRILGIPWGF LIGAELTIAQ
     SRISLVNKIQ QVYRSQGVQI HNRHLEIIVR QITSKVLVSE DGMSNVFSPG ELIGLLRAER
     MGRALEEAIC YRVVLLGITR ASLNTQSFIS EASFQETARV LAKAALRGRI DWLKGLKENV
     VLGGVIPVGT GFKGLVHPSK QHNNIPLETK KKNLFEGEMR DILFHHKKLF DSCLSKNFHD
     IPEQSFIGFN DS
 
 
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