RPO1N_METVS
ID RPO1N_METVS Reviewed; 889 AA.
AC P41556; A6UQ07;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=rpoA, rpoA1 {ECO:0000255|HAMAP-Rule:MF_00863};
GN OrderedLocusNames=Mevan_0673;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Palm P., Arnold-Ammer I., Lechner K.A., Zillig W.;
RT "DNA sequence of the genes of the large subunits of the DNA dependent RNA-
RT polymerase of Methanococcus vannielii.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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}.
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DR EMBL; X73293; CAA51728.1; -; Genomic_DNA.
DR EMBL; CP000742; ABR54579.1; -; Genomic_DNA.
DR PIR; S47162; S47162.
DR RefSeq; WP_011972481.1; NC_009634.1.
DR AlphaFoldDB; P41556; -.
DR SMR; P41556; -.
DR STRING; 406327.Mevan_0673; -.
DR EnsemblBacteria; ABR54579; ABR54579; Mevan_0673.
DR GeneID; 5325060; -.
DR KEGG; mvn:Mevan_0673; -.
DR eggNOG; arCOG04257; Archaea.
DR HOGENOM; CLU_000487_3_1_2; -.
DR OMA; AVCPPYN; -.
DR OrthoDB; 3905at2157; -.
DR Proteomes; UP000001107; 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; cd02582; RNAP_archeal_A; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR HAMAP; MF_00863; RNApol_arch_Rpo1N; 1.
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; 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 3: Inferred from homology;
KW Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..889
FT /note="DNA-directed RNA polymerase subunit Rpo1N"
FT /id="PRO_0000074006"
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 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
SQ SEQUENCE 889 AA; 99098 MW; 08D9E5933FD9FCB6 CRC64;
MDRFDVPKEI GDITFGLLSP EQIRTMSVAK IVTADTYDDD GYPIDGGLMD TRLGVIDPGL
VCKSCSGRVG TCPGHFGHIE LSKSVIHIGF AKDIYKLLKA VCPHCGKVTV TEIKRDEYLE
KMLKLEEDGG DPWTLSDDLL KEAAKSSVCP SCGEVKYDIK YDKPTTYHQL DGKSQKQLTS
SEVREILEKI PNEDCKLLGI NSRVARPEYM VLTVLPVPPV TVRPSITLES GERSEDDLTH
KLVDIIRINQ RLEENINGGA PNLIIEDLWD LLQYHINTYF DNEAPGIPPA RHRSGRPLRT
LAQRLKGKEG RFRHNLAGKR VNFSARTVIS PDPRLSINEV GIPELIAKEL TVPEKVTPYN
IERIRKLIEN GSDKHPGVNY VIKKVKTKDG KEEEYKIKIT DTNKKMWVEN IVDGMVVERH
LGDGDVVLYN RQPSLHRMSI MAHKVKVLPY RTFRHNLCVC PPYNADFDGD EMNVHVPQSE
EARAEAETLM LVEKHIISPR YGGPIIGAIH DFVSGAYVLT SSNFIKDEAL TLLKSSGFGS
ELGEPDFVEN GIEYYSGKSL FSKTLPKGLN LQYKAKVCKK CVQCKREECE NDAFVIIRNG
RLVQGVIDKN GFGAETGVVL NTIVKDFGSE DARTFLDSAT KMSVKSMMLR GFTTGIDDED
IPSEAIQEIQ DLLDKAESDV QEIVERYEGG TLDPLPGRGI EESREAYIMQ ILGKARDDTG
KVAEKYLSKE NHAALMARTG ARGSLLNITM MAASVGQQSV RGGRVFRGYR GRTLPHFGEG
SLDAKSHGFV RSCYKKGLAP TEYFFHAMGG REGLVDQAVR TAQSGYMQRR LVNALQDIKA
EYDGTVRDSR GIIVQFNYGE DLVDPSKADH GKGVDLDKVF TKVISKYEN
