ID   RPO1N_HALMO             Reviewed;         349 AA.
AC   P15349;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo1N {ECO:0000255|HAMAP-Rule:MF_00863};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00863};
DE   AltName: Full=DNA-directed RNA polymerase subunit A' {ECO:0000255|HAMAP-Rule:MF_00863};
DE   Flags: Fragment;
GN   Name=rpo1N {ECO:0000255|HAMAP-Rule:MF_00863};
GN   Synonyms=rpoA1 {ECO:0000255|HAMAP-Rule:MF_00863};
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 (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. Forms the clamp head domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00863}.
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:0000255|HAMAP-Rule:MF_00863};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00863}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00863}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00863}.
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   AlphaFoldDB; P15349; -.
DR   SMR; P15349; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
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; IPR045867; DNA-dir_RpoC_beta_prime.
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   PANTHER; PTHR19376; PTHR19376; 1.
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   Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
FT   CHAIN           <1..349
FT                   /note="DNA-directed RNA polymerase subunit Rpo1N"
FT                   /id="PRO_0000074002"
FT   REGION          306..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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