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RPOC1_TUPAK
ID   RPOC1_TUPAK             Reviewed;        1578 AA.
AC   Q3ZJ92;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN   Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
OS   Tupiella akineta (Green alga) (Pseudendoclonium akinetum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade;
OC   Ulotrichales; Tupiellaceae; Tupiella.
OX   NCBI_TaxID=160070;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1912;
RX   PubMed=15930151; DOI=10.1093/molbev/msi182;
RA   Pombert J.-F., Otis C., Lemieux C., Turmel M.;
RT   "The chloroplast genome sequence of the green alga Pseudendoclonium
RT   akinetum (Ulvophyceae) reveals unusual structural features and new insights
RT   into the branching order of chlorophyte lineages.";
RL   Mol. Biol. Evol. 22:1903-1918(2005).
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_01323}.
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_01323};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01323}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR   EMBL; AY835431; AAV80599.1; -; Genomic_DNA.
DR   RefSeq; YP_636175.1; NC_008114.1.
DR   AlphaFoldDB; Q3ZJ92; -.
DR   SMR; Q3ZJ92; -.
DR   GeneID; 4108779; -.
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:0000287; F:magnesium ion binding; 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; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR034678; RNApol_RpoC1.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 2.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   SMART; SM00663; RPOLA_N; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..1578
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353513"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         1286
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         1288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         1290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ   SEQUENCE   1578 AA;  183291 MW;  8F6EBD8C1A92488B CRC64;
     MSSDLKYSLS SEPPQPQVQS PLLKILKGEV SETTELKKLH SFRLCLSSPK IIKQWAQRTL
     PNGEIVGSIT NAQTVNYKTL KPEKGGLFCE RVFGPVKDFY CSCGKQKTKQ HPKVCPTCGV
     QYISSQSRRY KMGYIELVSP VTHIWYLKSS PSYISLLLNL KKKNLEALTY CSENLSLNIK
     SFQNELLFQN VLHLLKANPF ALEKGLKKRK KRFLVNSNWF SFIFDNSYLI KANSGFQLKV
     KDFPFFLITK NQNLQNFMGV CSQSANGNEQ ILPEMEKQGK NTFQFSPFLT TVQKHGSSEN
     GSFPELKREK DELELFKLID SFSSKSPSKK KDFFRSEILT AFYKKYSKFH FSRFRSNKKS
     FLISLFSSSN NWYFNKNQNI GYFSIFNKNF KIFFSLLNYQ ILLKTIDKNS LANLLSPLFD
     NYLNDDSQVL FDDSIKKLNL TKNFRSNEDQ ELSTLLNSCF FLNKIGAIAQ SPFSLAFYTQ
     KSEKFYCFSP SFLNPFEKDS LSGKIFSLKK KKILPSQKMF ELKPLTLFCS KKTKRNEVES
     ENPNSNHMLP FIAFSKKQRC EEKADFFKQL RMIELESEKS RSPKDLLFLN KFPFKNEKKL
     KYNLQKRNKL HTLKNPIGNF KFRKYFSLRL DSSLKRSLLI YQIKNFKNGF EHSDFYSENQ
     TSTNFTKFLV SRELEKSSKF SNSLFSFENF AQLLIFIFDF PAALERQRQS FSLRSYSKSA
     NFRSQTSARG EVGGNFNLEV KQSQNYFLDW KLTNNYRNFY QSSEIQNLNC FFISNFLVKN
     AIPVSPLSLE QFVFNNETQK NLHLGNEDSR FFANLKKPIK KLGLLKNSFL AETLANAKAN
     AHNLKENRTP VIQDKENESQ TFSQLFFDQI DQKEGSSLKS KDLNFTNWNN KKITRFIELL
     EKTLFLKKPG LVNNYYTISQ SLQWPCQKDW ARFLNYMTNT ADKTDSLIPS YLERGISFDL
     VLTGAGSIKK LLSLFTPMGK KASIEIVAKQ INGTLLKLNR DIKRLEDFFK FEIFFIDDQE
     IIEKVFMKLV ILRSLRSKAL RRLKVLRPFK GSHVLPEWMV LSVLPILPPA LRPIIPLDSQ
     QVAVSDLNKL YQTVLFRNKR VQRFYNDYYS LNFSEEMRYA QRLLQEAVDA LIENGKGDSA
     AITASNNRPL KSLSDMIKGK KGRFRQNLLG KRVDYSGRSV IVVGPKLRLH ECGLPKEMAI
     ELFQPFLIRR LIFKEVATNF ISAKKLIKSN PESILDILRE VMENRPVLLN RAPTLHRLGI
     QAFQPKLISG RAILLHPLVC AAFNADFDGD QMAVHIPLSF QACAEAWKLM GSRNNLLSPA
     TGEPIILPSQ DMVLGCYYLT TLDRVKIKQK LSQSSFLFPF LISKQGVHEN LSTISSNSKG
     IENWILKKPS QKSEIRTLSS FYEINESERA TFESKTNDTS ILKLQDKKRR ETLTFKRNRL
     SPVDTKLHLM DLSKNKNQNL FLNRFEKRAN CKVWSDSNKY YSNWDQVLQS LNQQLIDLHS
     PIWLRWNFYF EFVLKKESFL EIRLDKYGNS VYINPNYQSY SNSKLEKIVF YIRTTPGRVL
     MNKLIFEALN KPSLKKSF
 
 
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