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Database: UniProt
Entry: R4PNY9_9BACT
LinkDB: R4PNY9_9BACT
Original site: R4PNY9_9BACT 
ID   R4PNY9_9BACT            Unreviewed;       307 AA.
AC   R4PNY9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-SEP-2023, entry version 45.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|ARBA:ARBA00015972, 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|ARBA:ARBA00012418, ECO:0000256|HAMAP-Rule:MF_00059};
DE   AltName: Full=RNA polymerase subunit alpha {ECO:0000256|ARBA:ARBA00033070, ECO:0000256|HAMAP-Rule:MF_00059};
DE   AltName: Full=Transcriptase subunit alpha {ECO:0000256|ARBA:ARBA00032524, ECO:0000256|HAMAP-Rule:MF_00059};
GN   Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059,
GN   ECO:0000313|EMBL:AGL62694.1};
GN   ORFNames=L336_0995 {ECO:0000313|EMBL:AGL62694.1};
OS   Candidatus Saccharimonas aalborgensis.
OC   Bacteria; Candidatus Saccharibacteria; Candidatus Saccharimonadia;
OC   Candidatus Saccharimonadales; Candidatus Saccharimonadaceae;
OC   Candidatus Saccharimonas.
OX   NCBI_TaxID=1332188 {ECO:0000313|EMBL:AGL62694.1, ECO:0000313|Proteomes:UP000013893};
RN   [1] {ECO:0000313|EMBL:AGL62694.1, ECO:0000313|Proteomes:UP000013893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM71 {ECO:0000313|EMBL:AGL62694.1};
RX   PubMed=23707974; DOI=10.1038/nbt.2579;
RA   Albertsen M., Hugenholtz P., Skarshewski A., Nielsen K.L., Tyson G.W.,
RA   Nielsen P.H.;
RT   "Genome sequences of rare, uncultured bacteria obtained by differential
RT   coverage binning of multiple metagenomes.";
RL   Nat. Biotechnol. 31:533-538(2013).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {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:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00024550,
CC         ECO:0000256|HAMAP-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 associated
CC       with the core the holoenzyme is formed, which can initiate
CC       transcription. {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC       transcription, whereas the C-terminal domain is involved in interaction
CC       with transcriptional regulators and with upstream promoter elements.
CC       {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000256|ARBA:ARBA00007123, ECO:0000256|HAMAP-Rule:MF_00059}.
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DR   EMBL; CP005957; AGL62694.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4PNY9; -.
DR   STRING; 1332188.L336_0995; -.
DR   KEGG; saal:L336_0995; -.
DR   PATRIC; fig|1332188.3.peg.988; -.
DR   HOGENOM; CLU_053084_0_1_0; -.
DR   OrthoDB; 9805706at2; -.
DR   Proteomes; UP000013893; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd06928; RNAP_alpha_NTD; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1.
DR   Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 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   NCBIfam; TIGR02027; rpoA; 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   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF47789; C-terminal domain of RNA polymerase alpha subunit; 1.
DR   SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1.
DR   SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00059};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00059}; Reference proteome {ECO:0000313|Proteomes:UP000013893};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00059};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00059}.
FT   DOMAIN          20..228
FT                   /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT                   /evidence="ECO:0000259|SMART:SM00662"
FT   REGION          1..232
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
FT   REGION          247..307
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   307 AA;  33170 MW;  ED4E89C661F5A463 CRC64;
     MSKVIHNPAL ARVTPSGDNT SSFVIEPLHA GYGDTLGNSI RRVLLSSIRG AAIVAFRIEG
     VTHEFATIPG VKEDVVDIML NLKGVKLKVE TDDPVELRLE KKGSGPVVAG DIKTSADVEV
     INPDHVICTI DDPKKSIVID LVVEAGRGYY DMEASSKNRL HSDMIAIDAM FSPVTRVRFK
     VEATRVGQET NLNRLEITIE TDGSISPQAA FEEANAILVN QYTALAGSTT VESAPALGTQ
     KEDDEGELNT PIEELGLSAR TANALINNEI RTVHDLVTLS EQDLRDLKGF GSKALDEVKD
     KLAELEL
//
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