ID A0A0S3SU91_PHAAN Unreviewed; 1646 AA.
AC A0A0S3SU91;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=Vigan.08G333300 {ECO:0000313|EMBL:BAT96398.1};
GN ORFNames=VIGAN_08333300 {ECO:0000313|EMBL:BAT96398.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT96398.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT96398.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015041; BAT96398.1; -; Genomic_DNA.
DR Proteomes; UP000291084; Chromosome 8.
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; cd02735; RNAP_I_Rpa1_C; 1.
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; IPR047107; DNA-dir_RNA_pol1_lsu_C.
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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000291084};
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 316..632
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 234..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1646 AA; 184174 MW; 5459AEBB74A5D9D3 CRC64;
MVLYTESATN SVKAVAFSFL TSDDLQRSSL VKITNPILLN ALLHPVPGGL YDPAMGPLDD
KSLCKSCGQA SKLCPGHFGH IELVSPVYNP LMFNILSSII QRTCFSCYHF QASRKEVDMR
TTQLELIMKG DIIRAKSLDS INLDEFTHSG DGDESHHCSA EQQGENWTSL QFSEAMSILK
KFLKRQYKKC QNCGVVNPKI SKPTFGWFHM NVLSADAARA NTIRVVESEI NNDDMSLGGG
ETTDEEDISS VGAVKRDKRK KGNLSHKLAA QNKLSGSLLP SQVKGILELL WENEARLCSY
ISDIQDQGFG KKAGHSMFFL ENIFVPPIKF RPPAKAGDDV MEHPQTVLLT KVLQGNISLG
EAHINKLDPS KVLSRWMDLQ QSINLLFDSK TASGQRDVAA GICQLLEKKE GIFRQKMMGK
RVNFACRSVI SPDPYLAVNE IGIPPYFAIR LSYPERVTPW NAMKLRNAIL NGPDSHPGAT
HYSDKQATVK LQRSPKLLAM ISRKLPSSRG VILDQGKISD QEFEGKVVYR HLKDGDVVLV
NRQPTLHKPS IMAHIVRVLK GEKTVRMHYA NCSTYNADFD GDEINVHFPQ DEISRAEAYN
IVNANNQYVK PTSGDPIRAL IQDHIVSASL LTKKDTFITY EEFNQLLYSS GVSMAGVGSF
SGKHGQKVFM TNSECEMFLF PPAIWKPEPL WTGKQVISAL LYYITRGSPP FTVEKNAKIP
SNFFKTQVRE GERYTRDKSR DKDLPDEDKL LIYKNNLVRG VVDKAQFGDY GIIHTVQEFY
GSNVAGNLLS ALSRLFTSFL QMHGFTCGVD DLMIIEEKDV ERMNQLSSCE EIGDIVHREF
IGVMNGDNID TTTMQLNIEK KVRSNGEAAL TYLDRKMISN LNSRTSSGIL KELLSEGILK
PSGKNCISLM TTSGAKGSMV NFQQISSHLG QQELEGKRVP RMVSGKTLPC FAPWDCSPRA
GGFIIDRFLT GLHPQEYYFH CMAGREGLVD TAVKTSRSGY LQRCLMKNLE CLKVCYDHTV
RDADGSIIQF HYGEDGVDVH QTSFINKFEA LSTNKELVYS NCCRQLDRSS PYINKLPDAL
KGKAENFFRD SLKQRNLGLK RRDLLKLMEH KYVSCLAQPG ESVGVLASQS VGEPATQMTL
NTFHLAGRGE MNVTLGIPRL QEIVMAASRD IKTPFMTCPL RPNKSMEDAI CLADKLKKIT
VADIIKSMKV SVVQVTVHAG QVCSIYKLVM KLYKPKQYPK YTDITLEDWE DTLRVFFVRE
LEDAIESHMA LLSKISGIKK FKTDPQSNYS NSSEDGHGNE SESETKGKNK DDDDDDGVVE
DTEGYEDLGS DAQKRKRQGT DEVDYEDGPE EEMHDGEQSE ETENDEDGSD VDVNENDNDM
TLDANNSQGL EKSSKFKPIV EKNSLKREKK KSKAITKKYD RAVFVKAKGM HFEIHFKFTG
EPHILLAQIA QRTAKKVCIQ NFGRVGECKA ITCKESGVIY YGEDGRNRDD IPASMKEKIP
ALQTSGIHFK TFWELQDDLD VRYIYSNSVH AMLSAYGVEA ARETIIREVQ NVFKSYGISV
NIRHLTLIAD FMTHSGGYSP MNRTGSIADC TSPFIKMCFE TASKFIVEAA YHGQVDNLET
PSSRICLGLP VKVGTGCHDL IQKLEI
//
