ID A0A0T5ZH09_9ARCH Unreviewed; 1263 AA.
AC A0A0T5ZH09;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=rpo1C {ECO:0000256|HAMAP-Rule:MF_00411};
GN Synonyms=rpo1N {ECO:0000256|HAMAP-Rule:MF_00863}, rpoA1
GN {ECO:0000256|HAMAP-Rule:MF_00863}, rpoA2
GN {ECO:0000256|HAMAP-Rule:MF_00411};
GN ORFNames=XU09_C0001G0179 {ECO:0000313|EMBL:KRT62116.1};
OS Thaumarchaeota archaeon CSP1-1.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1640512 {ECO:0000313|EMBL:KRT62116.1, ECO:0000313|Proteomes:UP000051388};
RN [1] {ECO:0000313|EMBL:KRT62116.1, ECO:0000313|Proteomes:UP000051388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-1 {ECO:0000313|EMBL:KRT62116.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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 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:KRT62116.1}.
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DR EMBL; LDXL01000001; KRT62116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZH09; -.
DR STRING; 1640512.XU09_C0001G0179; -.
DR PATRIC; fig|1640512.3.peg.179; -.
DR Proteomes; UP000051388; 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 NCBIfam; TIGR02389; RNA_pol_rpoA2; 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};
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; 140536 MW; E1BA026F8A7775CF CRC64;
MSLQTIKSID SIRFSVWSPT EIRKYSVAEI TAPETYDEDG MSVQGGLMDG RLGTLEPGQK
CLTCGNTAAR CPGHFGHIEL AEPVLHIAFI DNIYKLLLST CRSCSRLRMS QEDLDKFAII
RKREAAFTII SQKRIPEQIL EKAKKAKECP HCGKPQYDLI FTKPTIFIEK TEIGENRLLP
ITIRERFSQI INEDLKLLGY DPDTARPEWF ILQALPVPPV TVRPSIILET GIRSEDDLTH
KMVDIIRVNQ RLKESKEAGT PPLIVQDLVD LLQYHATTYF DNEVSGIPQA HHRSGRPLKT
LTQRLKGKEG RFRGSLSGKR VDFSSRTVIS PDPNLDLSEV GVPESVAMKL TIPEIVTEWN
IERMKKIVIN GPSQFPGVNY IVRPDGVKIR LDFVEDRQTI ADNLEIGYLI ERHLANGDIV
LFNRQPSLHQ MSIMAHYVRV LPGKTFRLHP SVCPPYNADF DGDEMNLHVP QSEEARSEAI
LLMRVQDQLI SPRYGGPIIG ALRDFITGAY LLTKDGSTLT PQEFSNYAML GGYEGDLPTP
ATKDKDGPLY TGKQLFSLFL PEDFNYVMTS KWSKGTKGIP KDVVIKKGQL ISGVIDKSSI
GAEEAESVLH RIAKDYGNAQ AKNFLNSVLI IVKQYITHYG FSYGYSDLEL PEKVKQKILD
DIETSYEKVY DLTEEAKKGT LKLTRGLSPK EALEAYIVNE LSKARDAAGS MADQSFDETN
AGRIMATTGA RGSSLNIGQM AGALGQQSRR GERLLTGYNN RALPHFKEHE NNPDSHGFVK
SNYREGLSAI EFFFHAMGGR EGLVDTAVRT QQSGYMQRRL INALEHIKLE YDGTVRDPHG
HIMQFLYGED GIDVARSDHG EAFNINRLIE SQTIVDTGKK STKDETSELA KKYTKTYNSR
LKNLVTEALL DAKISKEGIE KVCKKGLDLY NKAKVEPGQA VGIVTAQSIG EPGTQMTLRT
FHFAGIRERN VTLGLPRLIE LVDARKKPVT PTMDIYLEKE SKTSREKAIE AARNILQTKV
SALISESETD YSTEIKLHLN ANRLKERGCT VEDVEAALES NKKFKSETNG LTITLKLVDE
SDAPTAITIR NKILNTTVKG VPDIGRVTIV QKDNEWVIQT TGSNLAKVLE VPGIDKKNVR
TNNVFEIAGT LGIEAARNAL INELSSTLED QGLEVDIRYL MLVADTMCSK GYMQQIGRHG
IAGTKDSVLA RAAFEITVPT IAHAALQGEI ERLKGITENV IVGSNIPIGS GTVDLYMQIS
KKN
//
