RPO1N_METJA
ID RPO1N_METJA Reviewed; 1341 AA.
AC Q58445;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 130.
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 Contains:
DE RecName: Full=Mja rpo1N intein;
DE AltName: Full=Mja rpoA' intein;
DE AltName: Full=Mja rpoA1 intein;
GN Name=rpo1N {ECO:0000255|HAMAP-Rule:MF_00863};
GN Synonyms=rpoA1 {ECO:0000255|HAMAP-Rule:MF_00863}; OrderedLocusNames=MJ1042;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00863}.
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DR EMBL; L77117; AAB99046.1; -; Genomic_DNA.
DR AlphaFoldDB; Q58445; -.
DR SMR; Q58445; -.
DR STRING; 243232.MJ_1042; -.
DR PRIDE; Q58445; -.
DR EnsemblBacteria; AAB99046; AAB99046; MJ_1042.
DR KEGG; mja:MJ_1042; -.
DR eggNOG; arCOG03158; Archaea.
DR eggNOG; arCOG04257; Archaea.
DR HOGENOM; CLU_258181_0_0_2; -.
DR InParanoid; Q58445; -.
DR OMA; AVCPPYN; -.
DR Proteomes; UP000000805; 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:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 3.10.28.10; -; 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; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
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 PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Cytoplasm; DNA-binding;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Protein splicing; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..1341
FT /note="DNA-directed RNA polymerase subunit Rpo1N"
FT /id="PRO_0000453784"
FT CHAIN 1..460
FT /note="DNA-directed RNA polymerase subunit Rpo1N, 1st part"
FT /id="PRO_0000031062"
FT CHAIN 461..911
FT /note="Mja rpo1N intein"
FT /id="PRO_0000031063"
FT CHAIN 912..1341
FT /note="DNA-directed RNA polymerase subunit Rpo1N, 2nd part"
FT /id="PRO_0000031064"
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 918
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 920
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 922
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
SQ SEQUENCE 1341 AA; 152781 MW; 4D98546ED552AF12 CRC64;
MERYEIPKEI GEIMFGLLSP DYIRQMSVAK IVTPDTYDED GYPIDGGLMD TRLGVIDPGL
VCKTCGGRIG ECPGHFGHIE LAKPVIHIGF AKTIYKILKA VCPHCGRVAI SETKRKEILE
KMEKLERDGG NKWEVCEEVY KEASKVTICP HCGEIKYDIK FEKPTTYYRI DGNEEKTLTP
SDVREILEKI PDEDCILLGL NPEVARPEWM VLTVLPVPPV TVRPSITLET GERSEDDLTH
KLVDIIRINN RLEENIEGGA PNLIIEDLWN LLQYHVNTYF DNEAPGIPPA KHRSGRPLKT
LAQRLKGKEG RFRYNLAGKR VNFSSRTVIS PDPCLSINEV GVPEVVAKEL TVPEKVTKYN
IERIRQLLRN GSEKHPGVNY VIRKMIGRDG TEQEYKVKIT ESNKDFWAEN IREGDIVERH
LMDGDIVLYN RQPSLHRMSI MAHRVRVLPY RTFRHNLCVC VDGDTTVLLD GKLIKIKDLE
DKWKDVKVLT SDDLNPKLTS LSKYWKLNAD EYGKKIYKIK TELGREIIAT EDHPFYTTNG
RKRCGELKVG DEVIIYPNDF PMFEDDNRVI VDEEKIKKVI NNIGGTYKNK IINELKDRKL
IPLTYNDQKA SILARIVGHV MGDGSLIINN KNSRVVFRGD IEDLKTIKED LKELGYDGEE
IKLHEGETEI TDYNGKKRII KGKGYSFEVR KKSLCILLKA LGCVGGDKTK KMYGIPNWIK
TAPKYIKKEF LSAYFGSELT TPKIRNHGTS FKELSFKIAK IEEIFDEDRF IKDIKEMLKE
FGIELKVRVE EGNLRKDGYK TKVYVASIYN HKEFFGRIGY TYANKKETLA RYAYEYLLTK
EKYLKDRNIK KLENNTKFIT FDKFIKEKCL KNGFVKEKIV SIEETKVDYV YDITTISETH
NFIANGFLTG NCPPYNADFD GDEMNLHVPQ SEEARAEAEA LMLVEKHILS PRFGGPIIGA
IHDFISGAYL LTSNYFTKDE ATLILRSGGI KDELWEPDKV ENGVPLYSGK KIFSKALPKG
LNLRYKAKIC RKCDVCKKEE CEYDAYVVIK DGELIKGVID KNGYGAEAGL ILHTIVKEFG
PEAGRKFLDS ATKMAIRAVM LRGFTTGIDD EDLPEEALKE IEKVLDEAEE KVKEIIEKYE
RGELELLPGL NLEESREAYI SNVLREARDK AGAIAERYLG LDNHAVIMAV TGARGNILNL
TQMAACLGQQ SVRGKRIFRG YRGRVLPHFE KGDLGARSHG FVRSSYKKGL SPTEFFFHAM
GGREGLVDQA VRTAQSGYMQ RRLINALQDL KTEFDGTVRD SRGIMIQFKY GEDGIDPMLA
DRGKAVNIDR IIDKVKMKYN Q
