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RPOC2_SYNY3
ID   RPOC2_SYNY3             Reviewed;        1317 AA.
AC   P73334;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN   Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324}; OrderedLocusNames=sll1789;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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 cyanobacteria the RNAP catalytic core is composed of 2
CC       alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC       factor is associated with the core the holoenzyme is formed, which can
CC       initiate transcription. {ECO:0000255|HAMAP-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; BA000022; BAA17364.1; -; Genomic_DNA.
DR   PIR; S77517; S77517.
DR   AlphaFoldDB; P73334; -.
DR   SMR; P73334; -.
DR   IntAct; P73334; 2.
DR   STRING; 1148.1652442; -.
DR   PaxDb; P73334; -.
DR   EnsemblBacteria; BAA17364; BAA17364; BAA17364.
DR   KEGG; syn:sll1789; -.
DR   eggNOG; COG0086; Bacteria.
DR   InParanoid; P73334; -.
DR   OMA; IEGKSDW; -.
DR   Proteomes; UP000001425; Chromosome.
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; IPR007066; RNA_pol_Rpb1_3.
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; 4.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 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   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase; Zinc.
FT   CHAIN           1..1317
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067910"
FT   REGION          1279..1317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1288..1317
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         293
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"
SQ   SEQUENCE   1317 AA;  144777 MW;  27B6970469E7E551 CRC64;
     MTFYNYTIDK GRLKKLIALA YRRYGSARCS QLADELKELG FRFATKAGVS ISVDDLTIPP
     EKKQMLEAAE KEIRTTEERY ARGEITEVER FQKVIDTWNG TSEELKDQVV VNFRKTDPLN
     SVYMMAFSGA RGNMSQVRQL VGMRGLMADP QGEIIDLPIK TNFREGLTVT EYVISSYGAR
     KGLVDTALRT ADSGYLTRRL VDVSQDVIVR EQDCGTERSL RVTAMTDGDQ VKISLADRLF
     GRLLAKDVVG PDGEIIAKRN DEIDEALANR IAAVTDEVYV RSPLTCEAAR SVCQNCYGWS
     LAHGHKVDLG EAVGIIAAQS IGEPGTQLTM RTFHTGGVFT GEVARQEKAP EDGTVKWGKG
     LSTRKVRTRH GEDAEQVEIA GDLIWKGEGK KAATQTYSLT PGSLLFVQDG QTVTAGQLMT
     EISLSKTQRS TERATKDVAG DLAGEVLFDR LVPEEKTDRQ GNTTRIAQRG GLVWILSGEV
     YNLPPGAEPV VKNDEQVEVG SIMAETKLVT NDGGVVRLVS NREIEIITAS VLLDQAQVKL
     ESSGGREQYV IYTADKQRFL LKAAPGTKVQ NHSIVAELID DRYRTTTGGM IRYAGVEVAK
     GGRKQGYEVT KGGTLLWIPE ETHEINKDIS LLIVEDGQYV EAGTEVVKDI FCQSSGIVEV
     VQKNDILREI IIKPGDFYQD VDPGSVKIES GQLLQPGQDV FPGVTVSTLS QAEWIESPEG
     NGLLLRPVEE YKVFDEPAAP SQGSQNEEGG RQIELRSVQR LFYKDGDRVK SVEGAPLLST
     QLVLEIYGSG NEGISHLSAD IELQDDEEED CQRLQLVILE SLVLRRDQES DPLGGASKTR
     LLVQDGDQIP PGAVVARTEI QCKEAGTVRG IKEGQESIRR VLLERAADRL VVDLPSAPEV
     KPGQLLVAGQ ELVPGVKLEE SGKVLEINGK GDNYQLVLRR ARPYRVSPGA VLHIEDGDLV
     QRGDNLVLLV FERAKTGDIV QGLPRIEELL EARKPKEACV LARAPGVCQV EYLEDESVDI
     KVVEDDGTVS EYPLLPGQNA MVTDGQRIDV GHALTDGYNN PHEILDVFFS YYVDKDGCYQ
     AALRGLQAAQ KFLVNEVQTV YQSQGVDISD KHIEVIVRQM TAKVRIDDGG DTTMLPGELV
     ELRQVEQVNE AMGITGSAPA RYTPVLLGIT KASLNTDSFI SAASFQETTR VLTEAAIEGK
     SDWLRGLKEN VIIGRLIPAG TGFSSHEEVL GLIETQDDIQ GYMIEPIELP TTKKKASATK
     VKTKKVEADD DLLDDTRARA YAGTQLSQDD EEFEETYDTD EDDFDMDDDD DFGDDED
 
 
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