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RPO2C_METVS
ID   RPO2C_METVS             Reviewed;         611 AA.
AC   P41557; A6UQ06;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo2C {ECO:0000305};
DE            EC=2.7.7.6 {ECO:0000250|UniProtKB:P11513};
DE   AltName: Full=DNA-directed RNA polymerase subunit B' {ECO:0000303|Ref.1};
GN   Name=rpo2C {ECO:0000305}; Synonyms=rpoB {ECO:0000303|Ref.1}, rpoB1;
GN   OrderedLocusNames=Mevan_0672;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Palm P., Arnold-Ammer I., Lechner K.A., Zillig W.;
RT   "DNA sequence of the genes of the large subunits of the DNA dependent RNA-
RT   polymerase of Methanococcus vannielii.";
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. The Rpo2 subunit (Rpo2N and Rpo2C in this
CC       organism) is implicated in DNA promoter recognition and in nucleotide
CC       binding. {ECO:0000250|UniProtKB:B8YB55}.
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:0000250|UniProtKB:P11513};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:B8YB55};
CC       Note=Binds 1 Zn(2+) per subunit. {ECO:0000250|UniProtKB:B8YB55};
CC   -!- SUBUNIT: Part of the RNA polymerase complex.
CC       {ECO:0000250|UniProtKB:B8YB55}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB55}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA51727.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X73293; CAA51727.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000742; ABR54578.1; -; Genomic_DNA.
DR   PIR; S47161; S47161.
DR   RefSeq; WP_011972480.1; NC_009634.1.
DR   AlphaFoldDB; P41557; -.
DR   SMR; P41557; -.
DR   STRING; 406327.Mevan_0672; -.
DR   EnsemblBacteria; ABR54578; ABR54578; Mevan_0672.
DR   GeneID; 5325059; -.
DR   KEGG; mvn:Mevan_0672; -.
DR   eggNOG; arCOG01762; Archaea.
DR   HOGENOM; CLU_000524_2_2_2; -.
DR   OMA; YQKLYHM; -.
DR   OrthoDB; 5510at2157; -.
DR   Proteomes; UP000001107; 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-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 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; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007646; RNA_pol_Rpb2_4.
DR   InterPro; IPR007647; RNA_pol_Rpb2_5.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   InterPro; IPR019969; RNAP_Rpo2.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR   Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   TIGRFAMs; TIGR03670; rpoB_arch; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..611
FT                   /note="DNA-directed RNA polymerase subunit Rpo2C"
FT                   /id="PRO_0000048105"
FT   BINDING         547
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B8YB55"
FT   BINDING         550
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B8YB55"
FT   BINDING         565
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B8YB55"
FT   BINDING         568
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   611 AA;  68481 MW;  FDAC89B41896BE40 CRC64;
     MEKQANVYVN GKLIDTSKDP ENLVKSLRIQ RRSGKLSPNT SISFNEESND IHISTDGGRA
     VRPLVVVENG FSKLTNELLE KVNNNELTFE YLVKTGVIEF LDAEEEENAR IAMYNDEITF
     ENTHVEIDPL VILGIGAGVA PYPEHNSAPR ITMAAAMGKQ SLGIPMANIK WRMDTRGHLL
     HYPQVPLVRT KHQEILGFDK RPAGQNFVVA VMSYEGYNME DAFVINKASL ERGLGRSTFF
     RSYESFEKRY PGGQLDKFEV PEKGVRGYRA EEAYRNLGDD GLIDLESEVR SGDVILGKTS
     PPRFLEEQEI TLQTKSQRRD TSVTIRHGEE GVVDLVILSE TKEGNRLGKV RVRDLRVPEF
     GDKFASRHGQ KGVIGLVVPQ EDLPFTEDGV IPDLIINPHA IPSRMTIGQV LEMIGGKVGS
     LECRRVDGTI FSGEGEWALR HALENYGFTH SGKETMYDGK TGRKLECEIF VGVAYYQKLH
     HLVAGKIHAR SRGPIQVLTR QPTEGRAREG GLRFGEMERD VLVAHGAALL LKERLLDESD
     PHEDYVCAKC GEIAIFDYKR GMKFCPVCGE SEDIQDNRKI PPVKIAYAFK LLLDELKSMG
     IDPKLKLKDR A
 
 
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