ID S2EWZ2_9ARCH Unreviewed; 1263 AA.
AC S2EWZ2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00411, ECO:0000256|HAMAP-Rule:MF_00863};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000256|HAMAP-Rule:MF_00411};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00411};
DE AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000256|HAMAP-Rule:MF_00411};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1N {ECO:0000256|HAMAP-Rule:MF_00863};
DE AltName: Full=DNA-directed RNA polymerase subunit A' {ECO:0000256|HAMAP-Rule:MF_00863};
GN Name=rpoA {ECO:0000313|EMBL:EPA06709.1};
GN Synonyms=rpo1C {ECO:0000256|HAMAP-Rule:MF_00411}, rpo1N
GN {ECO:0000256|HAMAP-Rule:MF_00863}, rpoA1
GN {ECO:0000256|HAMAP-Rule:MF_00863}, rpoA2
GN {ECO:0000256|HAMAP-Rule:MF_00411};
GN ORFNames=BG20_I1472 {ECO:0000313|EMBL:EPA06709.1};
OS Candidatus Nitrosarchaeum limnium BG20.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=859192 {ECO:0000313|EMBL:EPA06709.1, ECO:0000313|Proteomes:UP000014065};
RN [1] {ECO:0000313|EMBL:EPA06709.1, ECO:0000313|Proteomes:UP000014065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG20 {ECO:0000313|EMBL:EPA06709.1,
RC ECO:0000313|Proteomes:UP000014065};
RX PubMed=22461554; DOI=10.1128/JB.00007-12;
RA Mosier A.C., Allen E.E., Kim M., Ferriera S., Francis C.A.;
RT "Genome Sequence of "Candidatus Nitrosoarchaeum limnia" BG20, a Low-
RT Salinity Ammonia-Oxidizing Archaeon from the San Francisco Bay Estuary.";
RL J. Bacteriol. 194:2119-2120(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 part of the jaw domain.
CC {ECO:0000256|HAMAP-Rule:MF_00411}.
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_00411, 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_00411}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00411}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|HAMAP-Rule:MF_00411,
CC ECO:0000256|RuleBase:RU004279}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPA06709.1}.
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DR EMBL; AHJG01000013; EPA06709.1; -; Genomic_DNA.
DR RefSeq; WP_010189657.1; NZ_AHJG01000013.1.
DR AlphaFoldDB; S2EWZ2; -.
DR PATRIC; fig|859192.6.peg.164; -.
DR OrthoDB; 371812at2157; -.
DR Proteomes; UP000014065; Unassembled WGS sequence.
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; cd06528; RNAP_A; 1.
DR CDD; cd02582; RNAP_archeal_A; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 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; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
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; IPR012757; RPO1C.
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_00411};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00411};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00411};
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_00411}; Reference proteome {ECO:0000313|Proteomes:UP000014065};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00411};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00411}; Zinc {ECO:0000256|HAMAP-Rule:MF_00863}.
FT DOMAIN 208..513
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
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 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
SQ SEQUENCE 1263 AA; 140691 MW; 89CFA4BD4FF7E8B6 CRC64;
MSIQAIKSID AIRFSVWSPT EIRKYSVAEI TAPETYDEDG MPVQGGLMDG RLGTLEPGQK
CLTCGNTAAR CPGHFGHIEL AEPILHIAFI DNIYKLLQST CRSCARLKVP QEDLDEFRKI
KEKHAAYTVI SEKRIPEQII EKAKKAKECP HCGKTQYELI FTKPTIFVEK TEIGEHRLLP
ITIRERFSQI IDDDLHLLAY DPVTARPEWF ILQALPVPPV TVRPSIILET GIRSEDDLTH
KMVDIIRVNQ RLKESKEAGT PPLIVQDLVD LLQYHATTYF DNEVSGIPQA HHRSGRPLKT
LTQRLKGKEG RFRGSLSGKR VDFSSRTVIS PDPNLDLSEV GVPEQIAMKL TIPEIVTEWN
IERMRKLVIN GPNTFPGVNY IVRPDGVKIR LDFVEDRSTI AETLEIGYLV ERHLANGDIV
LFNRQPSLHQ MSIMAHYVRV LPGKTFRLHP SVCPPYNADF DGDEMNLHVP QSEEARAEAI
LLMRVQDQLI SPRYGGPIIG ALRDFVTGAY LLTKDDTLLT PQEFYNYAML GGYNEKFPKP
GSKNKDGPMY TGKQLFSLFL PKDFNYVITS KWSKGTKGAQ KDVVIKNGEL ISGVIDKSSI
GAEEPESVLH RIAKDYGNTK AKNFLNSILI MVKQYITHYG FSYGYADLEV PEKEKQQILD
DIQETYGIIS DLTSQYEKGT LKLTRGMKPE EALEAYIVNE LGKARDKAGM TADQSLDQSN
AGRIMATTGA RGSSLNIGQM AGALGQQSRR GSRLHAGYNN RALPHYQEHD NNPDAHGFVK
SNYREGLSAL EFFFHAMGGR EGLVDTAVRT QQSGYMQRRL INALEHIRLE YDGTVRDPHG
HIIQFLYGED GIDVAKSDHG EAFNINRLIE SQTIVDSGKK ATKEEITDLA KKYTKTFNPR
LKQLVTDGLL DSKLSKEGAE IVCKKGLSLY NKAKVEPGQA VGIITAQSIG EPGTQMTLRT
FHFAGIAERN VTLGLPRLIE LVDARKKPVT PTMDIYLDNE SKKSREKAID VARNILQTKV
SALISDSETD YTTQIKLILS PNRLKERGCT VGEVEAALQS NKKFKMETTG ELITLKLVEE
SDAPTVIAIR NKVLNTTVKG VPDIERVTLV QKDDEWVIQT TGSNIAKVLE VSGIDKKNVR
TNNVFEIAGT LGIEASRNAL INELNNTLED QGLEVDDRYI MLVSDLMCSR GYMQQIGRHG
IAGTKDSVLA RAAFEITVPT IAHAALAGEV EQLKGITENV IVGSIIPIGS GTVDLYMQVS
KKK
//
