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RPOC2_AMBTC
ID   RPOC2_AMBTC             Reviewed;        1373 AA.
AC   P60289;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Amborella trichopoda.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12832641; DOI=10.1093/molbev/msg159;
RA   Goremykin V.V., Hirsch-Ernst K.I., Wolfl S., Hellwig F.H.;
RT   "Analysis of the Amborella trichopoda chloroplast genome sequence suggests
RT   that Amborella is not a basal angiosperm.";
RL   Mol. Biol. Evol. 20:1499-1505(2003).
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; AJ506156; CAD45097.2; -; Genomic_DNA.
DR   RefSeq; NP_904089.2; NC_005086.1.
DR   AlphaFoldDB; P60289; -.
DR   PRIDE; P60289; -.
DR   GeneID; 2546586; -.
DR   KEGG; atr:2546586; -.
DR   OrthoDB; 731145at2759; -.
DR   Proteomes; UP000017836; 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..1373
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067912"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1373 AA;  156104 MW;  281B7DFFE2F17569 CRC64;
     MEVLMAERAD LVFHNKAIDG TAMKRLISRL IDHFGMAYTS HILDQVKTLG FRQATLTSIS
     LGIDDLLTTP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
     PNFRMTDPFN PVYIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
     EYTISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIRGI SVSPRNGVGV
     TERIFIQTLI GRVLANDVYM GLRCIATRNQ DIGIGLVNRF ITSRAQPIYI RSPFTCRSTS
     WICQLCYGRS TTHGNLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGIAEHVRAP
     SNGKIKFNED LVHPTRTRHG HPAFLCHIDL HVTIESQDII HKVNIPPKSF LLVQNDQYVE
     SEQVIAEIRA GTSTLKERVQ KHIYSDSEGE MHWSTDVYHT PEYTHGNVHL LPKTSHLWVL
     SGSPCRSSIV PFPLHKDQDQ MNVQSLYVEE RYISDLSMNN DRVRHKLFGW DQKRGRVSYY
     SGPDRIISNR NWDSIYPLIL HENSDLLAKR RRNRFIIPFQ YDQEQEKELR PPGIVIKIPI
     KGILRRNSIL AYFDDPRYRR SSSGIAKYGT IEVDSIIKKE DLIEYRKTRE FGPKYQIQIK
     VNRFFFIPEE VHILPRSSSI MVRNNSIIGV DTRITLNIRS QVGGLVRVEK KKKRIELKIS
     SGDIHFPGET DNIARYSGIL IPPGRVKNTE SKFKNWIYVQ RITPIKKKYF VSVRPVVTYE
     IADGINLATF FPQDLLQEKN NLQLRVVNYI LYGDGKPIRG IFHTSIQLVR TCLVLNWDQD
     RAGSIEEEEA YTSLAEVRVN DLIRNFIRID LVKSPISSTG KENDMAGSGL IPNNGSDRIN
     TNPFFSKAKT QSLSQHQGTI RTLLNRNKEG QGESLMVLSS SNCSRIGPLN GSKYHNVTKE
     SIQEDPMISI RNSLGPLGTV PNILNFSSSY HSITHNEILF NKYLLPDNSR ETFLVPKSYF
     MDENRRIYNL DPCSNIILTP FNLNWCFLHH DYWEDTSTII SLGQFLCENI CISKDGPCVK
     SGQIIIVHVD SLVIRLAKYH LATRGATVHG HYGEILYEGD TLVTFIYEKS RSGDITQGLP
     KVEQVLEVRS IDSISMNLEK RVEGWNERIT GFLGIPWEFF ISAQLTIVQS RISLVNKIQK
     VYRSQGVQIH NRHIETIVRQ ITSKVLVSED GMSNVFSPRE LIGLLRAERI GRALEDDICY
     RAILLGITRA SLNTQSFISE ASFQETTRVL AKAALRSRID WLKGLKENVV LGGMIPVGTG
     FKGFVHHSRE HNNISLEIKK KNLFDGKMRD ILFYHREFCG SCIPKNFHDT SEQ
 
 
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