ID RPOA1_HALMO Reviewed; 349 AA. AC P15349; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 11-DEC-2019, entry version 68. DE RecName: Full=DNA-directed RNA polymerase subunit A'; DE EC=2.7.7.6; DE Flags: Fragment; GN Name=rpoA1; OS Halococcus morrhuae (Micrococcus morrhuae). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Halococcaceae; Halococcus. OX NCBI_TaxID=2250; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 17082 / DSM 1307 / JCM 8876 / NBRC 14719 / NCIMB 787; RX PubMed=2495365; DOI=10.1016/0022-2836(89)90519-6; RA Leffers H., Gropp F., Lottspeich F., Zillig W., Garrett R.A.; RT "Sequence, organization, transcription and evolution of RNA polymerase RT subunit genes from the archaebacterial extreme halophiles Halobacterium RT halobium and Halococcus morrhuae."; RL J. Mol. Biol. 206:1-17(1989). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. 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, ChEBI:CHEBI:83400; CC EC=2.7.7.6; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC -!- SUBUNIT: This RNA polymerase is composed of 5 large subunits: CC A',A'',B',B'' and epsilon, present in stoichiometric amounts, and 3 CC small ones, E, F and G, present in sub-stoichiometric amounts. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC {ECO:0000305}. 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; X57145; CAA40431.1; -; Genomic_DNA. DR PIR; S03575; S03575. DR SMR; P15349; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.274.100; -; 1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR038120; Rpb1_funnel_sf. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. PE 3: Inferred from homology; KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription; KW Transferase; Zinc. FT CHAIN <1..349 FT /note="DNA-directed RNA polymerase subunit A'" FT /id="PRO_0000074002" FT CONFLICT 336..339 FT /note="Missing (in Ref. 1; CAA40431)" FT /evidence="ECO:0000305" FT NON_TER 1 SQ SEQUENCE 349 AA; 38074 MW; 62EEA0E03C5D2ED1 CRC64; EFTSSTGDTV MIDEGALVEG TIDEDAVGAF GGEIVDTIVK QYGETRARVF INEVASLAMR AIMHFGFSIG IDDESISDAA EAQIDESMDN AYERVQELID TYENDDLESL PGRTVDETLE MKIMQTLGKA RDSAGDIADE HFDDDNPAVI MAESGARGSM LNLTQMAACV GQQAVRGERI NRGYEGRTLS HFKPGDLSAE AHGFVEDSYR SGLTPREFFF HAMGGREGLV DTAVRTSKSG YLQRRLINAL SELETQYDGT VRDTSDNIVQ FEFGEDNTSP VKVSSSDDNE IDVDEIADRV LAAEFEDEGE EFAGEQATNL SESADDRMDR DRPSSHGAAP IDVPEVGDD //