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RPOC2_LACSA
ID   RPOC2_LACSA             Reviewed;        1381 AA.
AC   Q56P11; Q1KXP1; Q332Y9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 63.
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}; ORFNames=PSC014;
OS   Lactuca sativa (Garden lettuce).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15917497; DOI=10.1093/molbev/msi174;
RA   Kim K.-J., Choi K.-S., Jansen R.K.;
RT   "Two chloroplast DNA inversions originated simultaneously during the early
RT   evolution of the sunflower family (Asteraceae).";
RL   Mol. Biol. Evol. 22:1783-1792(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Cisco;
RX   PubMed=16604461; DOI=10.1007/s11248-005-3997-2;
RA   Kanamoto H., Yamashita A., Asao H., Okumura S., Takase H., Hattori M.,
RA   Yokota A., Tomizawa K.;
RT   "Efficient and stable transformation of Lactuca sativa L. cv. Cisco
RT   (lettuce) plastids.";
RL   Transgenic Res. 15:205-217(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Salinas;
RA   Timme R.E., Kuehl J.V., Boore J.L., Jansen R.K.;
RT   "A comparison of the first two published chloroplast genomes in Asteraceae:
RT   Lactuca and Helianthus.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; AY865171; AAX58144.1; -; Genomic_DNA.
DR   EMBL; AP007232; BAE47583.1; -; Genomic_DNA.
DR   EMBL; DQ383816; ABD47222.1; -; Genomic_DNA.
DR   RefSeq; YP_398318.1; NC_007578.1.
DR   AlphaFoldDB; Q56P11; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_9X5941_mrna; cds-PLY79379.1; gene-LSAT_9X5941.
DR   GeneID; 3772824; -.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_9X5941_mrna; cds-PLY79379.1; gene-LSAT_9X5941.
DR   KEGG; lsv:3772824; -.
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..1381
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067927"
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"
FT   CONFLICT        1369..1381
FT                   /note="SNNFHDTQEQSFF -> QIISMIHKNNHFL (in Ref. 1;
FT                   AAX58144)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1381 AA;  156921 MW;  EC55859E6B2659D8 CRC64;
     MEVLMAERPT QVFHNKVIDG TAMKRLISRF IDHYGIGYTS HILDQVKTLG FRQATAASIS
     LGIDDLLTIP SKRWLVQDAE QQSFILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
     PNFRMTDPFN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
     EYIISCYGAR KGVVDTAIRT SDAGYLTRRL VEVVQHIVVR RTDCGTVRGI SVSPRNGMMT
     DRIFIQTLIG RVLADDIYIG SRCIATRNQD IGVGLVSRFI TFRAQPISIR TPFTCRSTSW
     ICQLCYGRSP AHDDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
     NGKIKFNEDL VHPTRTRHGH PAFLCSRDLY VTIESEDIIH NVCIPPKSFL LVQNDQYVES
     EQVIAEIRAR TSTLNLKEKV RKHIYSDSEG EMHWNTDVYH APEFTYGNIH LLPKTSHLWI
     LLGEPWRYSL GPCSIHKDQD QMNAYSLSVK PRYIANPSVT NNQVRHKFFS SYFSGKNQKG
     DRIPDCSELN RMTCTDHSNL RYPAILDGNS DLLAKRRRNR FIIPLESIQE GENQLIPSSG
     ISMEIPRNGI LRRNSILAYF DDPRYIRKSS GLTKYETREL NSIVNEENLI EYRGVKVFWP
     KYQKEVNPFF FIPVEVHILS ESSSIMVRHN SIIGADTQIT FNRRSRVGGL VRVKKKAEKM
     KLIIFSGDIH FPGKTNKAFR LIPPGGGKPN SKEYKKLKNW LYIQRMKLSR YEKKYFVLVQ
     PVVPYKKTDG INLGRLFPPD LLQESDNLQL RVVNYILYYD PILEIWDTSI QLVRTSLVLN
     WDQDKKIEKA CASFVEIRTN GLLRYFLRID LAKSPISYTG KRNDLSGSGL ISENGSDRAN
     VNPFSSIYSY SKSRIKESLN PNQGTIHTLL NRNKESQSLI ILSSSNCFRI GPFNDVKSPN
     VIKESIKKNP LIPIRNSLGP LGTGFPIYNF DLFSHLITHN QILVTNYLQL DNFKQIFQIL
     KYYLLDENGQ IYNPYSCSNI ILNPFHLNWY FLHYNYCEET SPIVSLGQFL CENVCIAKKG
     PHLKSGQVLI VQVDSVVIRS AKPYLATPGA TVHGHYGEIL YEGDTLVTFI YEKSRSGDIT
     QGLPKVEQVL EVRSIDSISM NLEKRIEGWN KSITRILGIP WAFLIGAELT IVQSRISLVN
     KVQKVYRSQG VQIHNRHIEI IVRQITSKVL VSEDEMSNVF SPGELIGLLR AERMGRALEE
     AICYQAVLLG ITRASMNTQS FISEASFQET ARVLAKAALL GRIDWLKGLK ENVVLGGMIP
     VGSGFKTPSS EPNNIPNNIA FELQKKNLLE GEMKDILFYH RKLFDSCLSN NFHDTQEQSF
     F
 
 
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