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RPOC2_THEVB
ID   RPOC2_THEVB             Reviewed;        1324 AA.
AC   Q8DL57;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=tll0640;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC08191.1; -; Genomic_DNA.
DR   RefSeq; NP_681429.1; NC_004113.1.
DR   RefSeq; WP_011056487.1; NC_004113.1.
DR   AlphaFoldDB; Q8DL57; -.
DR   SMR; Q8DL57; -.
DR   STRING; 197221.22294361; -.
DR   EnsemblBacteria; BAC08191; BAC08191; BAC08191.
DR   KEGG; tel:tll0640; -.
DR   PATRIC; fig|197221.4.peg.679; -.
DR   eggNOG; COG0086; Bacteria.
DR   OMA; IEGKSDW; -.
DR   OrthoDB; 4373at2; -.
DR   Proteomes; UP000000440; 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; 1.
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..1324
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067908"
FT   REGION          1293..1324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1324
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         299
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"
SQ   SEQUENCE   1324 AA;  144702 MW;  2A82FE2C94B54976 CRC64;
     MTEKKPIFFN RIIDKKGLRD LIAWSFSNFG TARTAEMADK IKDLGFHYAT RAGVSISVDD
     LLVPPKKQEL LEAAEKEIKT AQERYSRGEI TEVERFQKVI DTWNSTNEEL KNEVVRHFRN
     TDVLNSVYMM AFSGARGNLS QVRQLVGMRG LMANPQGEII DLPIKTNFRE GLTVTEYIIS
     SYGARKGLVD TALRTADSGY LTRRLVDVSQ DVIIREEDCE TERGITLRSM TVGDKVLALQ
     DRLLGRVVLN DVRHPQTGEV LVAKNQAISA DLAKKIVDAG IEEVVVRSPL TCEATGSVCR
     LCYGWSLAHA RLVDMGEAVG IIAAQSIGEP GTQLTMRTFH TGGVFTGEVA RQERAPFAGT
     VEYGKKLRVR PYRTRHGDDA FIVETAGKLV VKGGQQRQEF DLSQGSIVLV ADGETVAAGQ
     LLAEVAQAAR SVRKATEKVT KDVASDLAGQ VKFVNLDAEE KRDRQGTTTR IAPKGGLIWV
     LSGEVYNLPP GAEPVVKNGD RIEAGAVLAE TTVKTEHGGV VRLPEQQDSK GGREVEIITA
     SVMLDKAKVL KETQQGREHY IIETATGQRF SLKAAPGTKV ANGQVVAELI DDRYHTTTGG
     ILKYADIEVA KKGKAKQGYE VLKGGTLLWI PEETHEVNKD ISLLMVEDNQ YVEAGTEVVK
     DIFCQNSGVV EVIQKNDILR EIIIKPGELH LVDDPEAARL KHGTLARPGE EVLPGLVVDT
     LSQVDYLEDT PEGPAILLRP VQEFSVPDEP SVPSQDSSDG SGQSIRLRAV QRLPYKHDER
     VKSVDGVDLL RTQLVLEIGS EAPQLAADIE IVTDEVDPEA QRLQLVILES LIIRRDIAAD
     QTQGSTFTSL LVKDGDHIGP GAVIARTDIK AKQAGEVQGI VRSGESVRRI LVVTDSDRLR
     VETNGAKPTV KVGDLVRPGD ELAKGVTAPE TAAVMAVADD HVILRLARPY LVSPGAVLQI
     EEGDLVQRGD NLALLVFERA KTGDIIQGLP RIEELLEARH PKEKCVLAVR PGTCQVTYNS
     DDSVEIKVIE EDGTIQEYPV LPGQNPLVVD GQKVNLADPL TDGPVDPHDI LSIYFEYYKP
     QGLLKAAQTS LEKVQSFLVN EVQSVYLSQG IEIADKHIEV IVRQMTSKVR IDDAGDTILL
     SGELMTLRQA EQANEPMALT GGAPAQYTPV LLGITKASLN TDSFISAASF QETTRVLTEA
     AIEGKSDWLR GLKENVIIGR LIPAGTGFNS YEESSNGDEE WEEGEDRLGQ THVISPEPES
     PKMTVNVTAD LGEDVLIDDE TAPHVIEKIT GGARDFEFAS SDVEEDELTE EDDDYGDEEE
     EDAF
 
 
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