GenomeNet

Database: UniProt
Entry: A0A132MYA8_9ACTN
LinkDB: A0A132MYA8_9ACTN
Original site: A0A132MYA8_9ACTN 
ID   A0A132MYA8_9ACTN        Unreviewed;       343 AA.
AC   A0A132MYA8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=LI90_3723 {ECO:0000313|EMBL:KWX02680.1};
OS   Carbonactinospora thermoautotrophica.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Carbonactinosporaceae; Carbonactinospora.
OX   NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWX02680.1, ECO:0000313|Proteomes:UP000070188};
RN   [1] {ECO:0000313|Proteomes:UP000070188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA   Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KWX02680.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LAXD01000001; KWX02680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A132MYA8; -.
DR   STRING; 1469144.LI90_3723; -.
DR   PATRIC; fig|1469144.10.peg.3997; -.
DR   Proteomes; UP000070188; Unassembled WGS sequence.
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:UP000070188};
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          22..229
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          236..343
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
FT   REGION          321..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  37340 MW;  18A9DE26A398A533 CRC64;
     MEDPLLIAQR PTLTEEVVDE YRSRFVIEPL EPGFGYTLGN SLRRTLLSSI PGAAVTSIRI
     DGVLHEFSTV PGVKEDVTDI ILNIKQLVVS SEHDEPVVMY LRKQGPGVVT AADIAPPAGV
     EVHNPDLHIA TLNAKGKLEM ELTVERGRGY VSAAQNKQAG QEIGRIPVDS IYSPVLRVSY
     RVEATRVEQR TDFDKLIIDV ETKPSMKPRD AVASAGKTLV ELFGLARELN VEAEGIDMGP
     SPTDAALAAD MALPIEELEL TVRSYNCLKR EGIHTVGELV SRSEADLLDI RNFGQKSIEE
     VKQKLAAMGL SLKDSPPGFD AGAAAASYGT DDDDQRFAET EQY
//
DBGET integrated database retrieval system