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RPOC2_COFAR
ID   RPOC2_COFAR             Reviewed;        1391 AA.
AC   A0A325;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 45.
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   Coffea arabica (Arabian coffee).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX   NCBI_TaxID=13443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17309688; DOI=10.1111/j.1467-7652.2007.00245.x;
RA   Samson N., Bausher M.G., Lee S.-B., Jansen R.K., Daniell H.;
RT   "The complete nucleotide sequence of the coffee (Coffea arabica L.)
RT   chloroplast genome: organization and implications for biotechnology and
RT   phylogenetic relationships amongst angiosperms.";
RL   Plant Biotechnol. J. 5:339-353(2007).
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; EF044213; ABJ89669.1; -; Genomic_DNA.
DR   RefSeq; YP_817472.1; NC_008535.1.
DR   AlphaFoldDB; A0A325; -.
DR   GeneID; 4421789; -.
DR   Proteomes; UP000515148; Chloroplast Pltd.
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..1391
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000277187"
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   1391 AA;  157609 MW;  DD51693CE052A484 CRC64;
     MEVLMAERAN LVFHNKSIDG TAMKRLISRL IDHFGMAYTS HILDQVKTLG FKQATATSIS
     LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
     PNFRMTDPFN PVHIMSFSGA RGNVSQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
     EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTVRGI SVSPPNGMMP
     EKFFIQTLVG RVLADDIYMG PRCIATRNQD IGIELVNRFI TFRAQPISIR TPFTCRSTSW
     ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFAG GIAEHVRAPS
     NGKIKFNEDL VHPTRTRHGH PAFLCFIDLY VTIKSENILH NVNIPPKSFL LVQNDQYVEA
     EQVIAEIRAG TSTLSFKEKV RKHIYSDSDG EIHWSTDVYH APQFTYGNVH LLPKTSHLWI
     LLGGPCRSSL VSLSLHKDQD QMNTHSLSVK RRYTYKLSVT NDRVRYKFFS SDFYGKKKNR
     IPDYLDLNRI ICTGYCNRIY PAILHENSDL LSKRRRNRFI MPLQSIQERE NESPGISIEI
     PINGIFRRNS ILSYFDDPRY RRKSSGITKY GTIEMHSLVK KEDLIEYRGV KEFRPKYQMK
     VDRFFFIPEE VHILPGSSSI MVQNNSIIGI DTQITLNIRS RVGGLVRVER KKKGIELKIF
     SGDIHFPGET DKISRHSGVL IPLPPGTGKI NSKESKKLKN WIYVQRITPS KKGYFALVRP
     VITYEKRDGL NLATLFPPDL LQERDNVRLQ VVNYILYGNG KPIRGISDTS IQLVRTCLVL
     NWDQDKKSSS SEEAPASFVE IRTNGLIRHF LRIDLVKSPI SYIVKRNDPS GSGLLSDNGS
     DCTNINPFSS IYSYSKARIQ QFLNPNQGTI HTLLNKNREF QSLIILLSSN CSRMGPFAGV
     KYHNVIKESI KNKKDPRISI RNSLGPLGSA PPIANFFSFS HLLTHNQILV TNYLQLDNIK
     ETFQVIKYYS MDENGKIYNP DPCNNIILNP LNLNWYFRHH NYCEETSTII SLGQFICENV
     CIAKNRPHLK PGQVIFVQVD SVVIRSAKPY LATPGATVHG HYGETLYEGD ILVTFIYEKS
     RSGDITQGLP KVEQILEVRS IDSISMNLQK RIEGWNKCIT RILGTPWGFL ISAELTIVQS
     QISLVNKIQK VYRSQGVQIH NKHIEIIVRQ ITSKVLISED GMSNVFSPGE LIGLLRAERM
     GRALEEAICY RAVLLGITRA SLNTQSFISE ASFQETARVL AKAALRGRID WLKGLKENVV
     LGGMIPVGTG FKGLVKPSKQ HNKALLETKK KNLFEGEMRD ILFHHRNFFD SFLLKKFHDP
     SEQSFIGFND S
 
 
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