RPO1N_HALS3
ID RPO1N_HALS3 Reviewed; 971 AA.
AC B0R8D4; P15350; Q9HM79;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
GN Name=rpo1N {ECO:0000255|HAMAP-Rule:MF_00863};
GN Synonyms=rpoA1 {ECO:0000255|HAMAP-Rule:MF_00863};
GN OrderedLocusNames=OE_4740R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], BLOCKAGE OF N-TERMINUS, AND SUBUNIT.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00863};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00863};
CC Note=Binds at least 2 Zn(2+) per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00863};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00863, ECO:0000269|PubMed:2495365}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00863}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:2495365}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00863}.
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DR EMBL; X57144; CAA40426.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP15003.1; -; Genomic_DNA.
DR PIR; A33926; A33926.
DR RefSeq; WP_010903996.1; NC_010364.1.
DR AlphaFoldDB; B0R8D4; -.
DR SMR; B0R8D4; -.
DR EnsemblBacteria; CAP15003; CAP15003; OE_4740R.
DR GeneID; 5954243; -.
DR GeneID; 62887872; -.
DR KEGG; hsl:OE_4740R; -.
DR HOGENOM; CLU_000487_3_1_2; -.
DR OMA; AVCPPYN; -.
DR PhylomeDB; B0R8D4; -.
DR Proteomes; UP000001321; Chromosome.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00093; HTH_XRE; 1.
DR CDD; cd02582; RNAP_archeal_A; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR HAMAP; MF_00863; RNApol_arch_Rpo1N; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR InterPro; IPR012758; RPO1N.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 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.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02390; RNA_pol_rpoA1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..971
FT /note="DNA-directed RNA polymerase subunit Rpo1N"
FT /id="PRO_0000409671"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 527
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT MOD_RES 1
FT /note="Blocked amino end (Met)"
FT /evidence="ECO:0000269|PubMed:2495365"
FT CONFLICT 726
FT /note="Y -> I (in Ref. 1; CAA40426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 971 AA; 108734 MW; EA9AE23E8DEDEB43 CRC64;
MSAGQAPKEI GEISFGLMDP EEYRDMSATK VITADTYDDD GFPIDMGLMD PRLGVIDPGL
ECKTCGQRSG GCNGHFGHIE LAAPVIHVGF SKLIRRLLRG TCRECASLLL TEEEKDEYRE
NLDRTRSLRQ DVSDVMTAAI REARKKDHCP HCGEVQYDVK HEKPTTYYEV QQVLASDYSE
RIAASMQPDE DEDDAGVSPQ ELAEQTDIDI SRINEILSGE FRPRREDREA IETAIGADLT
TEDMNKLMPS DIRDWFEDIP GEDLEALGVN SDRSRPEWMI LTVLPVPPVT ARPSITLDNG
QRSEDDLTHK LVDIIRINQR FMENREAGAP QLIIEDLWEL LQYHVTTFMD NEISGTPPAR
HRSGRPLKTL SQRLKGKEGR FRGSLSGKRV NFSARTVISP DPTLSLNEVG VPDRVATEMT
QTMVVNEQNL ERARRYVRNG PEGHPGANYV TRPDGRRVRV TEKVCEELAE RVEPGWEVQR
HLIDGDIIIF NRQPSLHRMS IMAHEVVVMP YKTFRLNTVV CPPYNADFDG DEMNMHALQN
EEARAEARVL MRVQEQILSP RFGENIIGAI QDHISGTYLL TNDNPRFNET QASDLLRQTR
IDELPAAAGT DEDGDQYWTG HQIFSELLPD DLSLEFTGTT GDTVVIEDGQ LLEGTIADDE
VGEYGSEIVD TITKVHGNTR ARIFINEVAS LAMRSIMHFG FSIGIDDETV STEARERIDE
AIQSAYDRVQ ELIETYENGD LESLPGRTVD ETLEMKIMQT LGKARDSAGD VAEENFDEDN
PAVVMANSGA RGSMLNLTQM AGCVGQQAVR GERINRGYED RTLSHFAPND LSSEAHGFVE
NSYTSGLTPK EFFFHAMGGR EGLVDTAVRT SKSGYLQRRL INALSELETQ YDGTVRDTSD
TIVQFEFGED GTSPVQVSSN EEVDIDVEHV ADRILNSEFD SDTQKAEFLE VEEPPTNLSE
HGAAWEVESD D
