(data stored in ACNUC8465 zone)

HOGENOM: UNCTG_1_PE109

ID   UNCTG_1_PE109                        STANDARD;      PRT;   323 AA.
AC   UNCTG_1_PE109; B1GZB0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha; Short=RNAP
DE   subunit alpha; EC=2.7.7 6;AltName: Full=RNA polymerase subunit
DE   alpha;AltName: Full=Transcriptase subunit alpha; (UNCTG_1.PE109).
GN   Name=rpoA; OrderedLocusNames=TGRD_109;
OS   UNCULTURED TERMITE GROUP 1 BACTERIUM PHYLOTYPE RS-D17.
OC   Bacteria; Elusimicrobia; environmental samples.
OX   NCBI_TaxID=471821;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS UNCTG_1.PE109.
CC       Uncultured Termite group 1 bacterium phylotype Rs-D17, complete genome.
CC       1..870428 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:B1GZB0_UNCTG
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
CC       beta, 1 beta' and 1 omega subunit. When a sigma factor is
CC       associated with the core the holoenzyme is formed, which can
CC       initiate transcription (By similarity).
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and
CC       basal transcription, whereas the C-terminal domain is involved in
CC       interaction with transcriptional regulators and with upstream
CC       promoter elements (By similarity).
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC   -!- GENE_FAMILY: HOG000218481 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B1GZB0; -.
DR   EMBL; AP009510; BAG13592.1; -; Genomic_DNA.
DR   RefSeq; YP_001956053.1; NS_000191.1.
DR   ProteinModelPortal; B1GZB0; -.
DR   STRING; B1GZB0; -.
DR   GeneID; 6373354; -.
DR   GenomeReviews; AP009510_GR; TGRD_109.
DR   KEGG; rsd:TGRD_109; -.
DR   OMA; EKPIATI; -.
DR   GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:HAMAP.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   HAMAP; MF_00059; RNApol_bact_RpoA; 1; -.
DR   InterPro; IPR011261; DNA-dir_RNA_pol_dimersation.
DR   InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR   InterPro; IPR009025; DNA-dir_RNA_pol_RBP11-like.
DR   InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR   InterPro; IPR011773; DNA-dir_RpoA.
DR   InterPro; IPR011260; RNAP_asu_C.
DR   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF03118; RNA_pol_A_CTD; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   ProDom; PD001179; RNAP_asu_C; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF47789; RNAP_alpha_C; 1.
DR   SUPFAM; SSF56553; RNAP_insert; 1.
DR   SUPFAM; SSF55257; RNAP_RBP11-like; 1.
DR   TIGRFAMs; TIGR02027; RpoA; 1.
DR   HOGENOMDNA; UNCTG_1.PE109; -.
KW   DNA-directed RNA polymerase alpha chain;
KW   Complete proteome; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
SQ   SEQUENCE   323 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKALDLEKLR KLILDEKTAT KFYGHFSAGP FERGYGHTIG NSLRRILLSS LEGAAITSVK
     IAGAFHEFAV LKGVKEDVAQ IVLNLKRIKV KLHSEGPEKL YLKVKKAGTV TAKDIEANAS
     VEIMNPEQEI ANIDNGTTLE MELEASLGKG YVLAEEMKSN GYSSGTIILD SLFSPIIKVN
     YEVENTRVEQ TLNYDKLIIE IWTDGSVSPK DALMRSAEIL RKILVIFTDN AFKTEEVSAD
     KEEQDGILGK PVSIMDISVK TLKSLKSAGI ETVEDLVKIK EEDLLNFNNL SKRSCEEIKN
     RVKELGLSLG MKIEDGEVND KNL
//

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