ID A0A2G5E9S9_AQUCA Unreviewed; 1996 AA.
AC A0A2G5E9S9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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_01000412v1 {ECO:0000313|EMBL:PIA52516.1};
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:PIA52516.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA52516.1, 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|RuleBase:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; KZ305027; PIA52516.1; -; Genomic_DNA.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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 Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.450.40; -; 2.
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; 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; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF51; DNA-DIRECTED RNA POLYMERASE V SUBUNIT 1; 1.
DR Pfam; PF11523; DUF3223; 2.
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; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
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 203..502
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1336..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1996 AA; 224173 MW; F0ED807056A6160B CRC64;
MEGALLSPVV DGRITDIRFS IATDDEICTA SISGCPINHP SQLTNPFLGL PLETGKCESC
GTAEPGQCEG HFGYIELPIP IYHPCHVSEL KMILRLVCLN CLRLKRGKNV GSDRSSAPCL
FCPDIPRINI NEFKTTDGVV LLELEVTRRS TSHNCWNFLD RFGYRYGNDR TRILLPCEVQ
EILKRFPEET KKKLSGKGYL SQDGYILQKL PVPPNCLSIP EISDGVSIMS SDLSVSMLRK
VLKQVEIIKS SRSGRPNFES HKVEVNDLQL TVAQYLRARG TAKDSRDIKM RAGASKLADD
SATKAWHEKM RTFFISKGSG HSSRSVITGD AYKSVNEIGL PIEVAQKITF EEKVTECNKG
YLQELVDKKL CLTYKDGASM YSLREGTKGH TFLRVGQVVH RRIMDGDVVF INRPPSTHKH
SLQALSVYVH EDHTVKINPL ICGPLDADFD GDCVHLFYPQ SLAARAEVLG LFSVEQQLLS
SHSGSLNLQL KNDALLSLKT MFKRFFLDKP TAQQLAMFIS SNLPPSALLK ADSVGSQWTI
LQILQATLPH HFDCSGERFL ISQSEILKVD FNRDLVQSMF NELISSVYFE MGSKEALNVF
NSLQPLLMEN LFLEGYSICL KDFSIPKLIL EDILGRIQEV SHLLHNLRST YNELVELQVG
SHLKNLKAPI VSFILKSSGL GNLIDSKSDS SVNKVVEQIG FLGLQLADRG KFYSRNLVED
MTSLFLHKYA VNGVEYPSEA FGLIKSSFFH GLNPYEDLVH SISSREVQVR SSRGLTEPGT
LFKHLMNILR DVIICYDGTV RNVCSNSIIQ FEYGVEAGMN FHRFYPAGEP VGALAATAIS
NPAYKAVLDS SSSSNVSWEL MKEVLLCKAN LKNDDTDRQV ILYLNDCGCV KEHCKETAAY
LVQKQLKKVS LRDISVNFLI EYQNQQTSPE NPGTSLVGHI HIDKERLKEL DRSMHEIFLK
CQETAALFNK RKKSKPGISD FLKNICLSVS ECCCSQQSYD SERSYVPCLQ FSWRLDATGA
SLETVSQIMA NTICPILLDT IIKGDRRVRA ANIIWISPET TTWVKSFCGT QHGEIALELV
LEKKFVKKHG DAWKLALDAC LPVIHLIDMT RSIPYPIRQV QEILGISCAF DQAVQRLSMS
IRMVNKGVLK EHLVLAASSI TCTGSLIGFS KGGYKSLFRS LNVQIPFTEA TMFTPRKCFE
RAAEKCHTDT LSGIVASCSW GKHVSVGSGT SFEILWNKKE MGLDHNGVED IYNFLLLVSS
TRESNTSCLG GDFDDLEFEN RVAELRLSPE QNLDSSKPTF DDGELLCDFE QPQSTGKGFF
NESNWGKATS VFKSGGSSDW NQHVDAENGW GASADKLPSS EPVDAWGKET RESDTNGWGA
TADKLPSSEP ADAWGKETRE SNTNGWGATA DKLQTQLCLS ERPSEKRPEA GWDTMESQDL
PISEPDDAWK KQTNEPDANG WGATGDKLQA ALSLSERPSE EGREACWNTI ESQKLPLNEP
IDAWGRQAKE SVTNDWDENV DSQWNVCPES HSTKASGESL KSTCWNAMES QRRTPQTGIL
DGREHRAKAQ LDKNEKNQDE QERELPTDTW GTIAEEAKND SSWSQPEQVN QPTDSLDWNS
SSDTKWTTKK QSQDEEDGKL PTDSLGWNSS SDTNWTTKKQ SQDEEDRKVP WGSNMIREQG
KGPSGPRKWA SSNSGDWKLK KNYPAQSPGR LDNRNARQKL DQFTLEEQKI LSVVEPIMAS
IKRIMHQSRY NDGDPLSSDD QSYILDNVLN YHPEKGVKIG PGVDYLMINK HNSFQGTRCF
YIVSTDGCRE DFSYRKCLEN FVKEKYPEMA GSFIGKYWPQ DRRSDNRTAS GNFTATRQKL
DQFTLEEQKI ISDIEPIIMS LRKIMNRSSY NDDDRLSPED QSFVLDNVLK YHPERALKIG
LGVDYVTVSK HNSFQDSRCL YIVSIDGHRE DFSYHKCLEN FVKEKYPDLA ESFIGKYWPP
RNRGGHVQEQ RAVSQV
//
