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RPOC_ANASK
ID   RPOC_ANASK              Reviewed;        1394 AA.
AC   B4UDT1;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=AnaeK_2270;
OS   Anaeromyxobacter sp. (strain K).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=447217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA   Beliaev A.;
RT   "Complete sequence of Anaeromyxobacter sp. K.";
RL   Submitted (AUG-2008) 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_01322}.
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_01322};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01322};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR   EMBL; CP001131; ACG73497.1; -; Genomic_DNA.
DR   RefSeq; WP_012526294.1; NC_011145.1.
DR   AlphaFoldDB; B4UDT1; -.
DR   SMR; B4UDT1; -.
DR   PRIDE; B4UDT1; -.
DR   EnsemblBacteria; ACG73497; ACG73497; AnaeK_2270.
DR   KEGG; ank:AnaeK_2270; -.
DR   HOGENOM; CLU_000524_3_1_7; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000001871; 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: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; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 2.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
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; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
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   SMART; SM00663; RPOLA_N; 1.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..1394
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353288"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         470
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         474
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         815
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         889
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         896
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         899
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1394 AA;  154659 MW;  6D724FFC3B19B992 CRC64;
     MKDIFNFFEK PKDPLSFSAI RISLASPDKI RQWSHGEVKK PETINYRTFK PERDGLFCAK
     IFGPVKDYEC NCGKYKRMKH RGVVCEKCGV EVIQSKVRRE RLGHITLATP VAHIWFLKSL
     PSRIGNLLDI TLKDLEKVLY CESYIVIDPK ETTFQRGELL SEDRYQKALD EFGDDAFSAG
     MGGEAVLGLL RGVGPASKEH GEGIPGLANE LRAEMKEATS DAKRKKIAKR LKVVEAFVAS
     GNKPEWMMLE VIPVIPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLQELNAPDI
     IIRNEKRMLQ EAVDALFDNG RRGKTITGPN KRPLKSLSDM LKGKQGRFRQ NLLGKRVDYS
     GRSVIVVGPE LKLHQCGLPK IMALELFKPF IYNKLEEKGY VTTIKSAKKM VEKERPEVWD
     ILDEVIREHP VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHV
     PLSIEAQMEA RVLMMSTNNI LSPAHGKPII VPSQDIVLGI YYMTRERAFA RGEGKVFASP
     EEVRAAYDQG EVDLQAKVWV RMDGKRVETT VGRVLLYDIV PRRLSFESIN KVMDKKQLQG
     LIDLTYRLCG EKETVLLADR VRSMGYGNAT RAGISIALDN MVIPRKKVDL LERATREVDD
     IQAQYTEGLI TIGERYNKVI DIWAQVTEEV AQEMMGEIGT ETAVGTGKDG KREERRQPSF
     NPIYIMADSG ARGSAQQIRQ LAGMRGLMAK PSGEIIETPI TANFREGLNV LQYFISTHGA
     RKGLADTALK TANSGYLTRR LVDVAQDAII TEYDCGAMDG ITLGALVEGG EIIEPMGERI
     LGRVALDDML DPFSGNVLVK ANEEIDEGKV KLIENAGIDK VKIRSVLTCQ ARRGICVECY
     GRDLARGRKV NIGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASRRAEQST IENRNAGLIK
     FNNVSVAKKR DGTLIVMNRN GEIIVTDDQG RERERYGVVY GAKLLVREGQ KVEANQLLAE
     WDPYSMPIIT EVAGRVKYGD LVDGVTISEQ VDEITGLARK AVIASKDPDA RPRISIKDEE
     GRTKKLANSD ADARYMLPEG ANLVVNDGDE VDAGDVIAKM PRETTKTKDI TGGLPRVAEL
     FEARKPKEHA VISEIDGVVA FGKDTKGKRK VVITPEVDSK LRPDLAKEYL IGKGKHISVH
     TGDRVRAGEA LMDGAANPHD ILRVLGEKEL ARWLVDEVQE VYRLQGVKIN DKHIETIVRQ
     MLRRVRIVDV GDTEFLADEQ VEKFAFEEEN ERVLKAGGRA AQGEPLLLGI TKASLSTESF
     ISASSFQETT KVLTEAAISG KVDYLRGLKE NVIMGRLVPA GTGLGAYKHL DIEVETPVDA
     VEEAEEALAV GAEE
 
 
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