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RPOB_MYCGA
ID   RPOB_MYCGA              Reviewed;        1390 AA.
AC   P47715;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNAP subunit beta {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 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=MYCGA2130;
GN   ORFNames=MGA_1000;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A5969Var.B;
RX   PubMed=8714123;
RA   Skamrov A.V., Rozovskaia T.A., Gol'dman M.A., Feotistova E.S.,
RA   Bibilashvili R.S.;
RT   "Determination of the nucleotide sequence of the part of the Mycoplasma
RT   gallisepticum genome, containing the rpoB gene, during the use of the Bal-
RT   pTM method for obtaining sequential deletions of the sequenced fragment.";
RL   Mol. Biol. (Mosk.) 30:61-75(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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; L38402; AAB40951.1; -; Genomic_DNA.
DR   EMBL; AE015450; AAP56563.2; -; Genomic_DNA.
DR   RefSeq; WP_011113454.1; NC_004829.2.
DR   AlphaFoldDB; P47715; -.
DR   SMR; P47715; -.
DR   PRIDE; P47715; -.
DR   GeneID; 57203527; -.
DR   KEGG; mga:MGA_1000; -.
DR   HOGENOM; CLU_000524_4_1_14; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001418; 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..1390
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047918"
FT   REGION          556..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        353
FT                   /note="S -> A (in Ref. 1; AAB40951)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="D -> H (in Ref. 1; AAB40951)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        575
FT                   /note="S -> G (in Ref. 1; AAB40951)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        701
FT                   /note="R -> T (in Ref. 1; AAB40951)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        747
FT                   /note="D -> V (in Ref. 1; AAB40951)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        937
FT                   /note="T -> I (in Ref. 1; AAB40951)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        990
FT                   /note="A -> V (in Ref. 1; AAB40951)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1390 AA;  156053 MW;  4E1004A6135074BD CRC64;
     MKKNSAFHNT QYSPKVVRRD YSKVHNKYNP LNLPGIQVNA YKQFLEKELE EIIGSYFPIK
     SPNGKYSVEF HGMKILDPQI TKEEASAESK TYDASLYVNL SLVNHQTGTV KKISKKSAKS
     KAEGIYFADI PLMTENGAFI VNGIEKFVVA QIVRSPGAYI LNKSQVKLSN SRKRNQEGYI
     CEVFPSKGTL MLFYIAENKD FVQAVVRDVG GESAKVFSIT TLLKAFGLSE IKIKEIFNNN
     DYILRSLESE FYNEKQILNE ADIAQLIRDI ESDRISKVKS LPIDQKWKNL VLDWYKLNQE
     KQELLNSSNP NPTKIESLNT HIGVVLRKLI CEKAAKHVIQ ELSISTRSLD NVSQKEEISY
     QSILLQHFFQ KKRYDLSSAG RHKFVRKLRV SERLYQRTIA QDIKDLDGNV VIKQGTLMLK
     EQLDLFKRLS KEKRLDIIKQ IDFINPELNT QFTDVNTYEE VQIYVNNDLR NETTQIIGID
     GSNESIETLT LADLISIVSY IVNLPFNIGL YDDIDHLGNK RLKLINELLK SKVQTGMMRI
     EKYIKDKLQT ADGNNKLADQ DAENDPDSDL GTKSSNDLTV KSVINPKPFQ IVIKDFFNTH
     QLTQFLDQQN PLSELTNKRR ISAMGPGGIS REDPNLDIRD VHYSHYGRIC PIETPEGMNI
     GLIMSLAFYA TIDKNGFLMT PYLKVENGKI TDKVEHLTAL REDEYIIAEA SSYMDVAKDG
     TINNEKIIAR YRSSQDLYDP KQVDYIDVSP KQVVSVAASL IPFLENDDSS RALMGANMQR
     QATPLLKPYS PLVGTGVEYK IAQDSGMLVT AKNPGTVTYV DASKITVKGE DNKSTDYNLL
     KFVKSNKNTC YNQSPIVAVG DKIETNQALA DGPSMKNGEL ALGQNVLVGF TTWSGYNYED
     AVIISDRLFK DDVYSSIHID EYTIECLRTK NGDEEITRDI PNISESAKRY LDEEGVIMVG
     AEVKEGDILV GKTSPKGQVE LTPEEKLIQA ILGDKVKQVR ESSLKVPNGG DGIVAGIKRF
     SIANGDELED DVLELVKVYV VQKRKIQIGD KVAGRHGNKG IISKIVAQED MPHLEDGTPL
     DILLNPLGVP SRMNIGQIFE LHLGYAAREL AKAKLIEACF DKKLADQLDT VFGLEKSKTQ
     SLIKNLVEHM KSIGVTSLAQ TKNRVRTIDI DIVLKQLGLT YDDLAFKIAT PVFEGVNMED
     LKAIMSEAGI DPDKTEGKFK LIDGRTGEPF EKPISVGIMY MLKLDHMVDD KIHARAVGPY
     SKITQQPLGG KSQNGGQRFG EMEVWALQAY GAAHNLREIL TIKSDDVRGR NMTYNAIVKG
     LSIPEPGVPE SFKLLTKELQ GLGMTLNVLY DDDSIENINN ISVVDESLEP KIHDAEFDTF
     TLDDYNDDNF
 
 
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