ID F8D4N2_HALXS Unreviewed; 975 AA.
AC F8D4N2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1N {ECO:0000256|HAMAP-Rule:MF_00863};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00863};
DE AltName: Full=DNA-directed RNA polymerase subunit A' {ECO:0000256|HAMAP-Rule:MF_00863};
GN Name=rpo1N {ECO:0000256|HAMAP-Rule:MF_00863};
GN Synonyms=rpoA1 {ECO:0000256|HAMAP-Rule:MF_00863};
GN OrderedLocusNames=Halxa_1734 {ECO:0000313|EMBL:AEH36363.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH36363.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|EMBL:AEH36363.1, ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
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:0000256|HAMAP-Rule:MF_00863}.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU004279}.
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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|HAMAP-Rule:MF_00863, ECO:0000256|RuleBase:RU004279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00863};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00863};
CC Note=Binds at least 2 Zn(2+) per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00863};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000256|HAMAP-
CC Rule:MF_00863}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00863}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|HAMAP-Rule:MF_00863,
CC ECO:0000256|RuleBase:RU004279}.
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DR EMBL; CP002839; AEH36363.1; -; Genomic_DNA.
DR RefSeq; WP_013879257.1; NC_015666.1.
DR AlphaFoldDB; F8D4N2; -.
DR STRING; 797210.Halxa_1734; -.
DR GeneID; 10796700; -.
DR KEGG; hxa:Halxa_1734; -.
DR eggNOG; arCOG04257; Archaea.
DR HOGENOM; CLU_000487_3_1_2; -.
DR OrthoDB; 371812at2157; -.
DR Proteomes; UP000006794; 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-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd00093; HTH_XRE; 1.
DR CDD; cd02582; RNAP_archeal_A; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 2.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
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 NCBIfam; TIGR02390; RNA_pol_rpoA1; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00863};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00863};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00863};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00863};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00863};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00863}; Reference proteome {ECO:0000313|Proteomes:UP000006794};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00863};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00863}; Zinc {ECO:0000256|HAMAP-Rule:MF_00863}.
FT DOMAIN 274..578
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 933..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 524
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
SQ SEQUENCE 975 AA; 109485 MW; 48863942BD24E2F4 CRC64;
MQNSTPKDIG SINFGLMEPE EYREMSATKI ITADTYDDDG FPIDMGLMDP RLGVIDPGLE
CKTCGKHSGS CNGHFGHIEL AAPVIHVGFT KLIRRLLRGT CRECSRLLLT EDERDEFRGQ
LDESRKLGRD LNDVTKAAIR QARKKDRCPF CGEIQYDIDH EKPTTYYEVQ QVLTSEYSQQ
IAAAMQGEED GERMSPDELA EETDIDLGRV NEILSGSFRP RESQRKAIEK ALDIDLTEED
TNKLMPSDIR DWFEDIPDED IEVLGIDSDR SRPEWMILTV LPVPPVTARP SITLDNGQRS
EDDLTHKLVD IIRINQRFME NREAGAPQLI IEDLWELLQY HVTTFMDNEI SGTPPARHRS
GRPLKTLSQR LKGKEGRFRG SLSGKRVNFS ARTVISPDPT LSLNEVGVPD RVAKEMTQTM
NVTERNLEDA RRFVANGPEA HPGANYVRRP DGRRLKVTEK NCEALAEKVE AGWEVNRHLV
DGDIVIFNRQ PSLHRMSIMA HEVVVMPYKT FRLNTVVCPP YNADFDGDEM NMHALQNEEA
RAEARVLMRV QEQILSPRFG ENIIGAIQDH ISGMYLLTAD NPRFNETQAL DLLRATRIDE
LPEPSGIDDE GKPFWTGYDV FSELLPDDLN LEFTGTVGDQ VVIEDGQLVE GTIAEDEVGE
FGGEIVDTIT KIYGNTRARI FINEVSTLAM RAIMHFGFSI GIDDETIPTE AQERIDETID
DAYDRVQELI EAYENNELES LPGRTIDETL EMKIMQTLSR ARDNAGNIAD EHFDDENPAV
VMANSGARGS MLNLTQMAGA VGQQAVRGER INRGYEDRTL SHYEPNDLSA EAHGFVENSY
TSGLTPREFF FHAMGGREGL VDTAVRTSKS GYLQRRLINA LSELETQYDG TVRDTSDTIV
QFEFGEDGTS PVKVSSGDEN NIDVAQIASR VLDSEFDSEE EREEFLGSKP RPTNLSEHAD
GRLSEGQSKG VSSDD
//
