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RPOC2_SPIOL
ID   RPOC2_SPIOL             Reviewed;        1361 AA.
AC   P11704;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Spinacia oleracea (Spinach).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3045324; DOI=10.1016/0022-2836(88)90477-9;
RA   Hudson G.S., Holton T.A., Whitfeld P.R., Bottomley W.;
RT   "Spinach chloroplast rpoBC genes encode three subunits of the chloroplast
RT   RNA polymerase.";
RL   J. Mol. Biol. 200:639-654(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX   PubMed=11292076; DOI=10.1023/a:1006478403810;
RA   Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA   Mache R.;
RT   "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT   sequence and gene organization.";
RL   Plant Mol. Biol. 45:307-315(2001).
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; AJ400848; CAB88715.1; -; Genomic_DNA.
DR   PIR; A29959; A29959.
DR   RefSeq; NP_054922.2; NC_002202.1.
DR   AlphaFoldDB; P11704; -.
DR   STRING; 3562.P11704; -.
DR   GeneID; 2715634; -.
DR   KEGG; soe:2715634; -.
DR   OrthoDB; 731145at2759; -.
DR   Proteomes; UP000054095; Chloroplast.
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; Reference proteome; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..1361
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067951"
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   1361 AA;  154769 MW;  19FF8C42BB1B17E8 CRC64;
     MEVLMAERAN LVFHNKAIDG TAMKRLISRL IDHFGMAYTS HILDQLKTLG FQQATATSIS
     LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYS TSEYLRQEMN
     PNFRMTDPYN PVHIMSFSGA RGNVSQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
     EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RRDCGTIRGI SVSPQNSTMP
     ERILIQTLIG RVLADDIYMG SRCIATRNQD IGVGLVNRFI TLRTQLISIR TPFTCRSASW
     ICRLCYGRSP THGGLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
     NGKIQFNEDL VHPTRTRHGH PAFLCYIDLY VTIESDDILH NVNIPPKSFL LVQNDQYVES
     EQVIAEIRAG TSTLNFKERV RKHIYSDSEG EMHWSTDVYH APEFTYGNVH LLPKTSHLWV
     LSGKPYRSSV VPFSLSKDQD QMNTHSLSFE QIYISNPSVT NDQVKDKLSD SFSKKEDRIT
     DYSELNRIGH CNLIYPAKNL DLLAKKRRNR FIIPFQGSQE RKKELMSLSG ISIEIPINGI
     FRKNSIFAYF DDPRYRRKSS GITKYGTIEM HSIVKKEDLI EYRGVKEFRP KYQMKVDRFF
     FIPEEVHILA GSSSIMVRNN SIIGVDTWIT LNTRSRIGGV VRVERKKKKI ELTIFSGDIH
     FPGETDKISR HSGILIPPSR KNSKDSKNLK KWIYVQRITP TKKKYFVLVR PVVPYEITDG
     INLATLFPQD LLQERDNVQL RVVNYILYGN GKVTRGISDT SIQLVRTCLV LNWNQDKKGS
     SIEEARGSFV EVRTNGMIQD FLKVNLVKPA ISYISKRNDP SSEKKEGSDH TNMNPFYSIY
     IYPKTKLQKS FNQNQGTVRT LLGINKECQF FLILSSSNCF RIGPFKGVKY PKELIKKDPL
     IPIRNSFGPL GTALQIANFF SFYYLITHNQ ILVTNYLQLD NLKQTFQPFK FQYYLMDENG
     RIYNPDPCSN IIFNPFKLNW YFLHYHFCEE TSTKIDLGQF VCENVCITKK GTHLKSGQVL
     IVQFDSVVIR SAKPYLATPG ATLHGHYGEI IYEGDTLVTF IYEKSRSGDI TQGLPKVEQV
     LEVRSIDSIS INLEKRIDSW NERITRILGS PWGFLIGAEL TIAQSRISLV NKIQKVYRSQ
     GVQIHNRHIE IIVRQITSKV LVSEDGMSNV FLPGELIGLF RAERTGRALE EAICYRATLL
     GITRASLNTQ SFISEASFQE TARVLAKAAL RGRIDWLKGL KENVVLGGMI PVGTGFKGFV
     HHSSQHKDIP LKTKKQNLFE GEMGDILFYH RELFESCLSK N
 
 
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