(data stored in SCRATCH zone)

HOGENOM: CHABO1_1_PE111

ID   CHABO1_1_PE111                       STANDARD;      PRT;   376 AA.
AC   CHABO1_1_PE111; Q5L6Z9;
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; (CHABO1_1.PE111).
GN   Name=rpoA; OrderedLocusNames=CAB113;
OS   CHLAMYDOPHILA ABORTUS S26/3.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
OX   NCBI_TaxID=218497;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHABO1_1.PE111.
CC       Chlamydophila abortus S26/3, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:RPOA_CHLAB
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates.
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; Q5L6Z9; -.
DR   EMBL; CR848038; CAH63571.1; -; Genomic_DNA.
DR   RefSeq; YP_219543.1; NC_004552.2.
DR   ProteinModelPortal; Q5L6Z9; -.
DR   GeneID; 3338100; -.
DR   GenomeReviews; CR848038_GR; CAB113.
DR   KEGG; cab:CAB113; -.
DR   OMA; VRSHNCL; -.
DR   ProtClustDB; PRK05182; -.
DR   BioCyc; CABO218497:CAB113-MON; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
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   Gene3D; G3DSA:2.170.120.12; RNAP_insert; 1.
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; CHABO1_1.PE111; -.
KW   Complete proteome; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
SQ   SEQUENCE   376 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDCSQNLLY DKFELPESVK MMAVEGSGGS VDKQASFIAE PLERGMGHTL GNALRRALLI
     GLEAPAIISF SMTGVLHEYM AINGIIEDVT NIILNLKGAL LKKYPFQDSE NGRCTQLLKS
     KVSIDASDLA ACGGQKAVTL ADLLQEGGFE SVNPDYVIFT VTQPMQLDIT LRVAFGRGYT
     TSERIVLEDK GVNEIVLDAA FSPVVLVNYF VEDTRVGQDT DFDRLILHVE TDGRVSPKEA
     LAFSTQILTK HFSIFEKMDE KKIVFEEAIS LEKENKDDIL HKLVLGINEI ELSVRSTNCL
     SNANIETIGE LVIMPEPRLL QFRNFGKKSL CEIKNKLKEM KLELGMDLSQ FGVGLDNVKE
     KMKWYADKIR SKNGKG
//

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