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RPO1C_METJA
ID   RPO1C_METJA             Reviewed;         859 AA.
AC   Q58446;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00411};
DE   AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411};
DE   Contains:
DE     RecName: Full=Mja rpo1C intein;
DE     AltName: Full=Mja rpoA'' intein;
DE     AltName: Full=Mja rpoA2 intein;
GN   Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
GN   Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411}; OrderedLocusNames=MJ1043;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. Forms part of the jaw domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00411}.
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_00411};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00411}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}.
CC   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00411}.
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DR   EMBL; L77117; AAB99047.1; -; Genomic_DNA.
DR   PIR; B64430; B64430.
DR   RefSeq; WP_010870556.1; NC_000909.1.
DR   AlphaFoldDB; Q58446; -.
DR   SMR; Q58446; -.
DR   STRING; 243232.MJ_1043; -.
DR   EnsemblBacteria; AAB99047; AAB99047; MJ_1043.
DR   GeneID; 1451940; -.
DR   KEGG; mja:MJ_1043; -.
DR   eggNOG; arCOG03145; Archaea.
DR   eggNOG; arCOG04256; Archaea.
DR   HOGENOM; CLU_351851_0_0_2; -.
DR   InParanoid; Q58446; -.
DR   OMA; KVHWKRI; -.
DR   OrthoDB; 66811at2157; -.
DR   PhylomeDB; Q58446; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd06528; RNAP_A; 1.
DR   Gene3D; 3.10.28.10; -; 1.
DR   HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR012757; RPO1C.
DR   PANTHER; PTHR19376; PTHR19376; 2.
DR   Pfam; PF14528; LAGLIDADG_3; 2.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; SSF51294; 1.
DR   SUPFAM; SSF55608; SSF55608; 1.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR   TIGRFAMs; TIGR02389; RNA_pol_rpoA2; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Cytoplasm; DNA-binding;
KW   DNA-directed RNA polymerase; Endonuclease; Hydrolase; Intron homing;
KW   Nuclease; Nucleotidyltransferase; Protein splicing; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..859
FT                   /note="DNA-directed RNA polymerase subunit Rpo1C"
FT                   /id="PRO_0000453741"
FT   CHAIN           1..75
FT                   /note="DNA-directed RNA polymerase subunit Rpo1C, 1st part"
FT                   /id="PRO_0000031065"
FT   CHAIN           76..546
FT                   /note="Mja rpo1C intein"
FT                   /id="PRO_0000031066"
FT   CHAIN           547..859
FT                   /note="DNA-directed RNA polymerase subunit Rpo1C, 2nd part"
FT                   /id="PRO_0000031067"
SQ   SEQUENCE   859 AA;  97087 MW;  A05799E007899015 CRC64;
     MDMEALKQKI EGLDIPQSLK DELFEKLSKE KDLTEEMVDE IIDEVVNAYR KALVEPYEAV
     GIVAAQSIGE PGTQMSLPYE EKIIIKEGEF IKPVEIGKLV DEMIERFGFE KIGNSEVCDL
     PIDIYALSLD QDEKVHWKRI ISCIRHKHNG KLIKIKTKSG REITATPYHS FVIRKDNKII
     PVKGSELKIG DRIPVVKHIP ANCVEAINIS DYVSGNYVVD NINNKIAPKI NGKSIPNNIK
     LDYDFGYFIG IYLAEGSVTK YFVSISNVDE LILNKIRAFA DKLGLNYGEY DNNNGFAESH
     DIRIYSSTLA EFLSNFGTSS NTKKIAEFVF GANKEFVRGL IRGYFDGDGN VNADRKVIRV
     TSNSKELIDG IAILLARFNI FSIKTKTKNQ FVLIIPHRYA KKFHEEINFS VEKKKSELER
     LVSSLNDDKT YDSIDMIPSI GDALTKLGEK VDYPKVILKK FERKQKIGRA TLQRHLRRIE
     ELAVKKGVNI LALKEYWLLK KAVESDVIWD EIVKIEEISC DKKYVYDISV EGLETFTTFD
     GVLTHNTMRT FHYAGVAEIN VTLGLPRMIE IVDARKEPST PIMTIYLKEE YKDNREKAEE
     IAKEIESLTL GSIAESISID LWTQSIKVEL DENRLADRGL TIDDVIEAIK KKLKVKIDVD
     GTTLYLKIKT PSIKALRKRI PKIKNIQLKG IPGIERVLVK KEGGEYVLYT QGSNLREVFK
     IDGVDTTRTI TNNIIEIQEV LGIEAARNAI INEMRNTLEQ QGLEVDIRHL MLVADIMTAD
     GEVKPIGRHG VAGEKGSVLA RAAFEETVKH LYAAAERGDV DKLKGVIENV IVGKPIYLGT
     GCVELTIDRE YEEGKNMEE
 
 
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