(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_1_PE1199

ID   ACAM1_1_PE1199                       STANDARD;      PRT;   313 AA.
AC   ACAM1_1_PE1199; B0C430;
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; (ACAM1_1.PE1199).
GN   Name=rpoA; OrderedLocusNames=AM1_1253;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE1199.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:B0C430_ACAM1
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: In cyanobacteria the RNAP catalytic core is composed of 2
CC       alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC       factor is associated with the core the holoenzyme is formed, which
CC       can 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: HOG000218480 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0C430; -.
DR   EMBL; CP000828; ABW26290.1; -; Genomic_DNA.
DR   RefSeq; YP_001515604.1; NC_009925.1.
DR   ProteinModelPortal; B0C430; -.
DR   STRING; B0C430; -.
DR   GeneID; 5680076; -.
DR   GenomeReviews; CP000828_GR; AM1_1253.
DR   KEGG; amr:AM1_1253; -.
DR   OMA; VRSHNCL; -.
DR   ProtClustDB; PRK05182; -.
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   GO; GO:0006281; P:DNA repair; 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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; SM00278; HhH1; 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; ACAM1_1.PE1199; -.
KW   DNA-directed RNA polymerase subunit alpha;
KW   Complete proteome; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
SQ   SEQUENCE   313 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAQFQVECLE TTVEEDFSQY SRFILEPLDR GQGTTVGNAL RRVLLANLRG TAVTAVRIAG
     VNHEFATIPG VREDVLDILL NMKQVVLRSH TNDPQIGRLF VQGPATVTTD DFELPTEVEI
     VNPTQYVATL SSDATLEMEF RIEQGKGYHA VGKNRDEAAA LDFLEIDAIY MPVRRVNYEV
     EDARVGGALE KDRLILDIWT NGNLTPQESL SQAATILVDL FNPLKDATFN VVEDIELEEE
     DETNQIPIEG LNLSVRAYNC LKRAQINSVA DLLEYSQEDL LEIKNFGAKS ADEVIAALQD
     HLGITMPTEK SKS
//

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