ID A0A2G5EC92_AQUCA Unreviewed; 1774 AA.
AC A0A2G5EC92;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=AQUCO_00900157v1 {ECO:0000313|EMBL:PIA53383.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA53383.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA53383.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; KZ305026; PIA53383.1; -; Genomic_DNA.
DR STRING; 218851.A0A2G5EC92; -.
DR InParanoid; A0A2G5EC92; -.
DR OrthoDB; 7998at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd01435; RNAP_I_RPA1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 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 InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
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 PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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 DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 345..660
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1415..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1774 AA; 199051 MW; 2CE166E7A62D2B26 CRC64;
MAHSTELATE SIDSVKFSFL NTEEVQRISV KEITKVTLFD DLDRPEPGGL YDSALGAEHP
MVRAPCKTCG QLPLLCPGHC GHIELVLPVY NPLLFATLSN MLKMMCFFCH HFMEEKERVE
KIASQLELIL KGDIVGANRP VLRTGLSLYD GDGTPHVEDA TYHSPALSDN LKGKYWTSLQ
YTQAMSLLED FMKKSSKKKD RKCARCKGKS PRMTHPTFGW IYMDTSNSTI RQNVIKGAHV
NERFIDESEE INSIGGGENL NDSSTIGALY DGKPGSSARA KKKSGVGKLP PDFFKQKELF
TGPLLPSEVK FHIELLWKNE IQLCSLICDI HQERLSTSAK KMSYAMFFIE ALLVPPTKFR
PSTRAGDTVT NHPQTVLLSR VLESNIALRD TDRSDGSKFV TRWRDLQQSV NLLFGNSRSI
GQRDNVGNGI CQLLEKKEGI FRQKMMGKRV NFSCRSVISP DPYLAVNEIG IPPCFALKLT
YPERVTPWNV DKLRTAIING PDVHPGATAF SDQSAYNRLP PNTKTRISIS RKLPSSRGVA
TQTGKNVEHE HEGKVVYRHL QDGDIVLVNR QPTLHKPGIM AHVVRVLNGE KTLRMHYANC
STYNADFDGD EMNVHFPQDE ISRAEAFHIV NADNQYIIPT SGDTKRGLIQ DHIVAAVLLT
IKDTFLSQED FTYLLYSSGV SAAARGSFVG RPGKKVSLLH SEDEIELIKP AILKPMPLWS
GKQVITSLLN HLSQSEGLPP FTFEGKCTID KKFLTNQTSF DDSPSEKSDD PPFKIDKNDF
LFGVIDKAQF GKFGLIHTVQ ELYGSHTAGV LLSALSRLFT VFLQLHGFTC GIDDLLLKHN
IDIERRRTLK DGDKVKKLKD AEKIDKELYS KFVKDESTIK HSEKVDVQSA DAKDELLERM
KLQEGIEKAV RVFGESAISL LDKMMSNTAT KLNNEVNDII FPKKNSDQSA NKSKGNSGDK
STDIGLVKAF PKNCFFLMTS SGAKGSQANF TQVSSLLGQQ SLEGKRVPLM ISGKTLPCFP
PWDPVLRAGG FITDCFLTGL RPQEYYFHCM AGREGLVDTA VKTSRSGYLQ RCLVKNLECL
KVGYDRTVRD ADGSIVQFCY GEDGVDVHKS SFMSKFETIA DNQTVVLGRL QDQLKDGRLL
QRKIKNKVAK LKRFKNPEEL SEELEKIVRD AKLTRFENFK ELRMELEKKV KGVKVAKLLK
FGKLEEVEGD RKECRKVVHQ KNQAILNMME QDSFMNNLMM VKYLSSLAEP GEPVGVIAAQ
SVGEPSTQMT LNTFHHAGQK DSNVTLGMPR LQEILMRASE KIQTPVMSCC LKDGKTKEDA
ERLAGTLRKV SVADIVESME VSVEPFSVQD HGVSTIYKLK MKLYSHELFP KNSSIKKLED
CEEILRVVFV RELERAIHTH VKMLLKNAGI NSIQKAESDS PEEIAEDDSG HKSKQKDDEN
DVSDDEDEAD DLGTDALKRR RQQTDEIEYE NCTENQNVEG EPDGAENQNV EGELDCTENQ
NVEGEPLGFE SENDHVEDNE NSNISEDEMV DAADESRERP VSNCTPSKET EEKKADTDMR
DSDRRFHVDF RGSEFEIHFR MPKEPHMPKE PHILLSQIAQ RAAKNVYIRK SSRVDRCSVI
NDTKRDEPPT ISTSGVDFHA LWDMQDDLDI NSVKSNDIHA ILQTYGVEAA RTTIVNELRN
VFSLYGISTD FRHLGLIADF MTHSGKFRAM SRYGMADSIS PFSKMTFETA SDFIINAAYR
GEVDTLESPS ARICLGLPVK MGTGCFDLMQ KVQV
//
