ID A0A1D6E7H1_MAIZE Unreviewed; 1324 AA.
AC A0A1D6E7H1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=ZEAMMB73_Zm00001d003203 {ECO:0000313|EMBL:ONM16384.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM16384.1};
RN [1] {ECO:0000313|EMBL:ONM16384.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM16384.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; CM007648; ONM16384.1; -; Genomic_DNA.
DR OMA; AVCPPYN; -.
DR ExpressionAtlas; A0A1D6E7H1; baseline and differential.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; 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; cd02583; RNAP_III_RPC1_N; 1.
DR Gene3D; 1.10.132.30; -; 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 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; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 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 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 242..541
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 1324 AA; 147424 MW; EEC2F68AAFC924EB CRC64;
MAKPEEKLRC TKEPFIEDVG TRRIKSIRFS VLSGSEIRKS AEVQVWNNRI YDRDMTPVPN
GLLDPRMGIP TKRGKCNTCH GEFSDCPGHF GYLKLALPVF NVGFFNCILD VLKCICKSCS
RVLLIEKDRR EFLKKMRNPR ADALQKSATM KKVRDKCKLS CCPRCDYRNG VVKKGRAGLI
VVHDCSKVLD GHTEELKNAL QNKKEKVSAS SVLVLDPATV LSLFRRMIDE DCELLNLGDR
PEKLIVTEIA VPPVPIRPSV VVGNSRTSNE DSITVILKSI VNTNSILKET LHTGGPFTKC
FDCWQYLQLQ VVEYVNSDAP SLPESQHRGL VQRLKGKTGR FRGNLSGKRT EYTGRTVISP
DPNLKITEVA IPVLMARVLT YPERVSNYNI EKLRQCIRNG PFKYPGANFV TQPDGMKQSL
KYGDRRITAR DLKCGCIVER HLEDGDVVLF NRQPSLHRMS IMCHRARIMP WRTLRFNESV
CNPYNADFDG DEMNLHVPQT EEARTEALML MGVQNNLCTP KNGEILVAST QDFLTSSFLV
TRKDTFYDRS SFTLLCSYLG DGMENIDLPT PALIKPVELW TGKQLFSVLV RPNAHTKVFL
NLAVQEKIYS KKKGKKEGGE EVKETMCGRE TMCPNDGYVY FRNSELLSGQ VGKATLGNGN
KDGLYSVLLR DYNSHAAASC MNRLAKFSAR FIGNHGFSIG VDDVQPGEHL NRQKKKEIDG
GYKKCHDLIS LFAKGALALH PGCNAAQTLE HNITGVLNEI RSIAGNVCMD TLHWRNSPLI
MSQCGSKGSP INISQMVACV GQQSVGGRRA PDGFLNRTLP HFPINSKTPA AKGFVANSFY
TGLTATEFFF HTMGGREGLV DTAVKTAETG YMSRRLMKGL EDLSVFYDQT VRNASGGIVQ
FLYGDDGMDP AKMEGKDGMP LNLDQLFMKV MATCPQRGSD TLSPVGIKQM LEDKFLQHDT
SSDGGCSAEF KKNLTEFLDK RIELMKCTRR ALHLHEDHVE KKDSCLEESI AAIISGISAK
QLQVFLDTCL SRYQSKKIEA GASIGAIGAQ SIGEPGTQMT LKTFHFAGVA SMNVTLGVPR
IKEIINAAKK ISTPIITAQL LSRKDVLSAR IVKGSMEKAV LGEVAATIQT VLKSSLPNLV
VKLDMQLIET LHMGISADSV KLSILNHPKL KLKSEHVRVI DRAKLRIYPA GTDKLKLQLE
LHNLKSILPK VIVKGIPTVE RVVIDEVKVN NATERYQLLV EGTNLLAVMG TPGVDARKTK
SNHIMETNQT LGIEAARRSI IDEIQYTMKS HGMNIDRRHM MLLADLMTYK NIYSMPHTVV
VRIR
//
