RPO1N_THECE
ID RPO1N_THECE Reviewed; 905 AA.
AC P31813;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
OS Thermococcus celer.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=2264;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35543 / DSM 2476 / JCM 8558 / Vu 13;
RX PubMed=1408768; DOI=10.1093/nar/20.17.4659;
RA Klenk H.-P., Schwass V., Lottspeich F., Zillig W.;
RT "Nucleotide sequence of the genes encoding the three largest subunits of
RT the DNA-dependent RNA polymerase from the archaeum Thermococcus celer.";
RL Nucleic Acids Res. 20:4659-4659(1992).
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; X67313; CAA47723.1; -; Genomic_DNA.
DR PIR; S25564; S25564.
DR AlphaFoldDB; P31813; -.
DR SMR; P31813; -.
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; 1.10.274.100; -; 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; 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 3: Inferred from homology;
KW Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..905
FT /note="DNA-directed RNA polymerase subunit Rpo1N"
FT /id="PRO_0000074010"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
SQ SEQUENCE 905 AA; 102725 MW; 9B71DC59BCF9A9AA CRC64;
MQSIKKVIGS IDFGILSPQE IRKMSAAEIT VPDTYDEDGY PIEGGLMDKR LGVIDPGLRC
ETCGARAGEC PGHFGHVELA RPVIHVGFAK TIHRVLESTC RECGRIKLTD EEIEEYFHKF
EVTGNRKKAK DRLIKEIHKK AKERMVCPHC GSPQFPIKFE RPTVYWELRK DEEGNEYKHR
MMPSEVRDRL EKIPDRDLPL IGLDAEKARP EWMVLTVLPV PPVTMRPSIT LESGIRAEDD
LTHKLVDIIR INNRLKSNIE AGAPQLIIED LWDLLQYHVT TYINNETSGI PPAKHKSGRP
LKTLSQRLKG KEGRFRGNLS GKRVNFSART VISPDPMISI NEVGVPMAIA MELTVPEKVT
EFNFEKLRKM VLNGPEKYPG ANYVIDPEGR RIRLMENNLE TVAEKLDIGW TVERHLLDGD
VVLFNRQPSL HRMSIMAHRV RVMPYRTFRL NLSVCPPYNA DFDGDEMNLH VPQTEEAQAE
AKILMEVQNH IISPRYGGPL IAGIQDHISG GYLLTREGAY FERTEVEQML MFAGVDVDRL
PEPDKVENGV ELWSGKTIFS LLLPKDLTIW YRNKLCDEPG RCEALEKLIE EKLIPDEEEV
RALAYDGFTY ILNGKLLSGA IDKTAYGRED GKLLDIIVRE YGVERARQFL DQVTKLAIWV
ITHKGFTTAI DDEDLPTEAL DRIREIIREA EERVNRLIEA YRNGELEPIP GKTLEETLES
KIMAALAEAR DNAGKVAERY LGMSNHAVIM AKTGARGKIL NITQMAAMLG QQSIRGKRLY
RGYRERVLTH FKPGDLGARA RGFVINSYKS GLTPQEYFFH AMGGREGLVD TAVRTAQSGY
MQRRLINALQ DLKVEYDGTV RDPTGIIVQF RYGEDGIDPM RSWKGKTIDV NRVVLRTLLK
LRGKG
