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RPOB2_NOCFA
ID   RPOB2_NOCFA             Reviewed;        1163 AA.
AC   Q5YPE0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNAP subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=RNA polymerase subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB2 {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=NFA_50990;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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_01321}.
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_01321};
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_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; AP006618; BAD59951.1; -; Genomic_DNA.
DR   RefSeq; WP_011211633.1; NC_006361.1.
DR   AlphaFoldDB; Q5YPE0; -.
DR   SMR; Q5YPE0; -.
DR   STRING; 247156.NFA_50990; -.
DR   PRIDE; Q5YPE0; -.
DR   EnsemblBacteria; BAD59951; BAD59951; NFA_50990.
DR   GeneID; 61135673; -.
DR   KEGG; nfa:NFA_50990; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_11; -.
DR   OMA; FMTWEGY; -.
DR   BioCyc; NFAR247156:NFA_RS25265-MON; -.
DR   Proteomes; UP000006820; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.30.150.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR   InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR   InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR010243; RNA_pol_bsu_bac.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   TIGRFAMs; TIGR02013; rpoB; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1163
FT                   /note="DNA-directed RNA polymerase subunit beta 2"
FT                   /id="PRO_0000224085"
SQ   SEQUENCE   1163 AA;  128607 MW;  400DA656CDE80B41 CRC64;
     MLEGRILAVS TQTKAVAGIP GAPKRVSFAK IREPLEVPGL LDLQTESFAW LIGSPEWRER
     AAARGDVGLV GGLEEVLEEL SPIEDFSGSM SLSFSDPRFE EVKASIDECK EKDMTYAAPL
     FVTAEFINNN TGEIKSQTVF MGDFPMMTDK GTFIINGTER VVVSQLVRSP GVYFDHSIDK
     GTEKDLHSVR VIPSRGAWLE FDVDKRDTVG VRIDRKRRQP VTVLLKALGW TTEEIAERFG
     FSEIMMSTLE KDNTAGQDEA LLDIYRKLRP GEPPTKESAQ TLLENLFFKE KRYDLARVGR
     YKINKKLGIH VGEPVTGSVL TKEDIVTTIE YLVRLHAGDK TMTAPGGVEV PVEVDDIDHF
     GNRRLRTVGE LIQNQIRVGL SRMERVVRER MTTQDVEAIT PQTLINIRPV VAAIKEFFGT
     SQLSQFMDQN NPLSGLTHKR RLSALGPGGL SRERAGLEVR DVHPSHYGRM CPIETPEGPN
     IGLIGSLSVY ARVNPFGFIE TPYRKVVDGR VTDEVVYLTA DEEDRHVRAQ ANSPVGPDGR
     FLEDRVLCRR GNEEMEYVAA TEVDFMDVSP RQMVSVATAM IPFLEHDDAN RALMGANMQR
     QAVPLIRSEA PIVGTGMELR AAVDAGDVVV NEKAGVVEEV SADYVTVMAD DGTRKSYRMR
     KFNRSNQGTC SNQRPIVDEG QRVEAGQVLA DGPCTENGEM ALGKNLLVAI MPWEGHNYED
     AIILSQRLVE QDVLTSIHIE EHEIDARDTK LGAEEITRDI PNVSDEVLAD LDERGIVRIG
     AEVRDGDILV GKVTPKGETE LTPEERLLRA IFGEKAREVR DTSLKVPHGE SGKVIGIRVF
     SREDDDDLPP GVNELVRVYV AQKRKIQDGD KLAGRHGNKG VIGKILPTED MPFLPDGTPV
     DIILNTHGVP RRMNIGQILE THLGWIGKAG WKVEGNPEWA KDLPEEMWEA PADSNIATPV
     FDGAREEELT GLLGSTLPNR DGERMVDDNG KAVLFDGRSG EPFPYPVAVG YMYILKLHHL
     VDDKIHARST GPYSMITQQP LGGKAQFGGQ RFGEMECWAM QAYGAAYTLQ ELLTIKSDDV
     VGRVKVYEAI VKGENIPEPG IPESFKVLLK ELQSLCLNVE VLSSDGAAIE LREGEDEDLE
     RAAANLGINL SRNEAATVDD LAN
 
 
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