ID A0A078J372_BRANA Unreviewed; 1869 AA.
AC A0A078J372;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=BnaC03g72290D {ECO:0000313|EMBL:CDY60335.1};
GN ORFNames=GSBRNA2T00028502001 {ECO:0000313|EMBL:CDY60335.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY60335.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY60335.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
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; LK033871; CDY60335.1; -; Genomic_DNA.
DR STRING; 3708.A0A078J372; -.
DR PaxDb; 3708-A0A078J372; -.
DR EnsemblPlants; CDY60335; CDY60335; GSBRNA2T00028502001.
DR Gramene; CDY60335; CDY60335; GSBRNA2T00028502001.
DR OMA; WGSQQKS; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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:0006366; P:transcription by RNA polymerase II; IEA:GOC.
DR CDD; cd02737; RNAP_IV_NRPD1_C; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.450.40; -; 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; IPR040402; NRPD1_C.
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; 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; 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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
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 204..503
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1308..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1869 AA; 205898 MW; 3DF90EA84936F1E2 CRC64;
MEEASSSDIL EAEIVGISFA LATHRQIRLA SISDAGINHA SQLSNAFLGL PLEFGKCEAC
GATEPDKCEG HFGYIHLPVP IYHPAHVSEL KQMLSLLCLK CLKIKKIKST SSGLAERLLG
VCCEEASNIT IKDKSSDGAS YLQLKLPSRT RLQEGFWNFL ERYGYRYGSD HTRPLLAREV
KEILRRIPEE TRKKLTAKGH IPQEGYILEY LPVPPNCLSV PEVSDGSNSM SVDPSRIELK
DVLRKVVAIN NSRSGETNFE SHRAEANEMF RVVDTYLQVR GTAKPTRNID MRFGVSKISD
SSSSKAWTEK MRTLFIRKGS GFSSRSVITG DAFRNVNEVG IPMEIAHRIT FEERVSVHNI
GYLQELVDNK MCLSYTQGST TYSLRDGSKG HTVLKPGQIV HRRVMDGDVV FINRPPTTHK
HSLQALRVYV HEDNTVKINP LMCGPLSADF DGDCVHLFYP QSLTAKAEVL ELFSVDKQLR
SSHTGQLILQ LGLDSLLSLR VMMEQVFLDK ASAQQLAMYG SRSLPSPAVV KSSKSSPAWT
FFQILQLAFP ERLSCRGDGF IVGGSDLLSF DFGVDALASI INGIVTGIMV EKGPKEALAF
FDSLQPLLME HLDPQGFSLS LEDLSMSRED MGVIHNLIVR EISPMVSRLR LSYEDELQLE
NSIQKVKEVA ANFMLKSYSM RNLIDIKSNS AINKLVQQIG FLGLQLSDKK KLYTKTLVED
MAQFYKKKYV STSSSGDFGI VKGCFFHGLD PYEEMAHSVA AREVIVRSSR GLAEPGTLFK
NLMAVLRDIV ITNDGTVRNT CSNSIVQFKY ELSSDNENQG LFEAGDPVGV LAATAMSNPA
YKAVLDFSPN SNSSWELMKE VLLCKVNFQN TTNDRRVILY LNECRCGKKY CQENSAYTVR
NKLKKVSLKD TAVEFLVEYR KQQAISEIFG MDICLHGHIH LNKTLLEGWN ISMQDILQRC
EDAINSLVQK KKKKAEDFKK MNLSVSECCS FRGPGSSKDS DMPCLMFSSY NATDPDLERT
LDVLCNTIYP VLLETVIKGD PRIASANIIW NSPETTTWIR SLHASRRGEW VLDVTVEKSD
VKQSGDAWRV VIDSCLSVLH LIDTKRSIPY SIKQVQELLG LSCAFEQAVQ RLSASVRKVS
KGVLKEHIIL VANNMTCSGD MLGFNSGGYK ALTRSLNIKA PFTEATLIAP RKCFEKAAEK
CHKDSLSTVV GSCSWGKRVD VGTGSQFELL WNKKETGLEN DDETDVFSFL QMVRSTKTAD
AYVSSPGFDV TEEEMAEWAE SPERDSALGE PKFDDSAEFQ NLLDEGKASE SKWDNGSLWE
NGCSSGSEWG VSKNAGGEEN TQSGWGKAAN VENEDASSGW NSKKDAQEAT NTDSWGAWGS
KTKDDAENAT PNWGTKPAQN DSVVIENGEP SSDVWGPKAV SDKPWGKKNS ETEPAPAAWG
KTNSESGATW GSRDKSKFET ESGGAAWGSQ AKNNSETEPG SGAAAWGTWD KKKSETESGG
GGAAWGSQAK NNSETESGSG AAAWGKKKPE TESGGGAAWG SQAKKNSESQ LGAANWGSKD
TNNSENGSDS AAWGKKKNSE AEPTSVAWGS WGQPSPPASD KDAQEDDGNP WVSLKATSSG
DKEGNETSQW GVPNKRYPSA GSQSQGGGGG ADWKRNRPPR TPGSESILGP MFTATRQRVD
MFTSEEQELL SDVDPVMRRL RKIMHQSGYT DGEPISDEDK TYVLEQILNY HPDKDAKLGP
GLDFITVDKH TTFTESRCFF VVSTDGTKQD FSYRKCINNY LVEKHPNLAE EFIAKYFRKR
DNENRDKNSQ EATPPGEQEP QTQPIDNGSQ DSQPQPIGNE GGVTQPQSQI EDIQPIGNGG
EDSQTEPQA
//
