(data stored in SCRATCH zone)

SWISSPROT: D4YYI1_SPHJU

ID   D4YYI1_SPHJU            Unreviewed;       354 AA.
AC   D4YYI1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE            Short=RNAP subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00059};
DE   AltName: Full=RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE   AltName: Full=Transcriptase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
GN   Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059,
GN   ECO:0000313|EMBL:BAI95413.1};
GN   OrderedLocusNames=SJA_C1-05790 {ECO:0000313|EMBL:BAI95413.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95413.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95413.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00059};
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. {ECO:0000256|HAMAP-Rule:MF_00059}.
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. {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00059}.
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DR   EMBL; AP010803; BAI95413.1; -; Genomic_DNA.
DR   RefSeq; WP_013039135.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-05790; -.
DR   EnsemblBacteria; BAI95413; BAI95413; SJA_C1-05790.
DR   GeneID; 29272254; -.
DR   KEGG; sjp:SJA_C1-05790; -.
DR   eggNOG; ENOG4105CTF; Bacteria.
DR   eggNOG; COG0202; LUCA.
DR   HOGENOM; HOG000218481; -.
DR   KO; K03040; -.
DR   OMA; LMKFRNF; -.
DR   Proteomes; UP000007753; Chromosome 1.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.170.120.12; -; 1.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR   InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR   InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR   InterPro; IPR011773; DNA-dir_RpoA.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR011260; RNAP_asu_C.
DR   InterPro; IPR036643; RNApol_insert_sf.
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; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
DR   TIGRFAMs; TIGR02027; rpoA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYI1.
DR   SWISS-2DPAGE; D4YYI1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059,
KW   ECO:0000313|EMBL:BAI95413.1};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   DOMAIN       28    235       RPOLD. {ECO:0000259|SMART:SM00662}.
FT   REGION        1    236       Alpha N-terminal domain (alpha-NTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   REGION      264    354       Alpha C-terminal domain (alpha-CTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
SQ   SEQUENCE   354 AA;  38326 MW;  30E8BC20AB389502 CRC64;
     MTVNMKNWQE LKKPNSLEIK VAGDGRRKAT FVAEPLERGF GLTLGNALRR VLLSSLQGAA
     VTSIKIENVL HEFSSLAGVR EDVTDIVLNI KQVALRMEGD GPRRLQLSAT GPAEVRAGDI
     TTVGDIEVMN PDLVICHLDQ GATLNMELTA DVGKGYVPAV ANRPADAPIG LIPIDALYSP
     VRQVAYKVDN TRVGQELDYD KLSLTVETDG TVTPEDAVAY AARILQDQLQ LFVHFEDALP
     AAAPAAGAAA GGSASEGESD ANQINRYLLK KVDELELSVR SANCLKNDNI IYIGDLVQKT
     EAEMLRTPNF GRKSLNEIKE VLSSMGLRLG MDIPGWPPEN IEEMAKKLEQ ELLG
//

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