ID A0A1D6QSY4_MAIZE Unreviewed; 1932 AA.
AC A0A1D6QSY4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=103654914 {ECO:0000313|EnsemblPlants:Zm00001eb207920_P001};
GN ORFNames=ZEAMMB73_Zm00001d053872 {ECO:0000313|EMBL:AQK60565.1};
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:AQK60565.1};
RN [1] {ECO:0000313|EnsemblPlants:Zm00001eb207920_P001, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb207920_P001,
RC ECO:0000313|Proteomes:UP000007305};
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2] {ECO:0000313|EMBL:AQK60565.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK60565.1};
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.
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb207920_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb207920_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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; CM000780; AQK60565.1; -; Genomic_DNA.
DR EMBL; CM000780; AQK60572.1; -; Genomic_DNA.
DR EMBL; CM000780; AQK60580.1; -; Genomic_DNA.
DR RefSeq; XP_008679943.1; XM_008681721.1.
DR EnsemblPlants; Zm00001eb207920_T001; Zm00001eb207920_P001; Zm00001eb207920.
DR GeneID; 103654914; -.
DR Gramene; Zm00001eb207920_T001; Zm00001eb207920_P001; Zm00001eb207920.
DR KEGG; zma:103654914; -.
DR OrthoDB; 455034at2759; -.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; A0A1D6QSY4; baseline and differential.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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; cd02737; RNAP_IV_NRPD1_C; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.450.40; -; 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; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D6QSY4};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
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 210..510
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1334..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..1932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1932 AA; 212906 MW; 48D63E01B711A6B1 CRC64;
MEEDHSVILI SEGAIKSIKL SLSTGEEICT YSINECPVTH PSQLGNPFLG LPLEAGKCES
CGASENDKCE GHFGYIELPV PIYHPCHVTE LRQLLSLICL KCLRIKKGKV KQSNGKGNAA
PTLCSYCRDI PALSLKEIKT TDGAIRLELR APHNKHMTER SWNFLDKYGF HHGGCSHHRT
LLPEEALNIL KKVPDDTRRK LAARGYIVQT GYVMKYLPVP PNCLYIPEFT DGQSIMSYDI
SIALLKKVLQ KIEQIKRSRS GSPNFESHDA ESCDLQLAIG QYIRLRGTTR GPQDNTKRFT
VGSADSAALS TKQWLEKMRT LFISKGSGFS SRSVLTGDPY IGLGVVGLPS EVAKRMTFEE
QVTDININRL QDVVDKGLCL TYRDGQATYA ITVGSKGYTT LKVGQTISRR IVDGDVVFLN
RPPSTHKHSL QAFYAYVHDD HTVKINPLMC GPFSADFDGD CVHIYYPQSL AAKAEALELF
SVERQLISSH SGKVNLQLGN DSLVAMKAMS HTTMLHKELA NQLAMFVPFS LLAPAVIKPV
PSWTISQIVQ GAFPANLTCQ GDTHLVRDST IIRLDLGKES VQDSFPDLVS SILREKGPKE
ALQFLNVLEP LLMEFLLLDG LSISLRDFNV PKALLEEAQK DIRNQSLILE QSRCSTSQFV
EFRVENNLKN VKQQISDSVG KFSDLGLLID PKKEASMSKV VQQVGFVGLQ LYREGKLYSR
RLVEDCFTNF VNKHLAIGDE YPPEAYGLVQ SSYFHGLNPY EELIHAISTR EAMIRSSRGL
SEPGTLFKNL MAILRDVVIC YDGTVRNICS NSIIQLKYGE DDETDSSSVV PPGEPVGVLA
ATAISNPAYK AVLDSSQSNN ASWESMKEIL QTRTSYKNDV KDRKVVLFLN DCSCAKKFCK
ERAALAVQSC LKRVTLGDCA TDICIEHQKQ INLDGTSEAA PTLVGHIHLD KGHLERINIS
TQDILQKCQE VSGRFGKKKG HLCHIFKKIT FATCDCSFTQ MPIDGKLHKV PCVQFAFSDD
IVLSESIERA VNVIADSVCS VLLDTIIKGD PRIQAAKVIW VESDAASWVK HTRKVSKGES
ALEIIVEKDD AVSNGDAWRT AIDACLPVLN LIDTRRSIPY GIQQVRELIG ISCAFDQVVQ
RLSTTVKMVN KGVLKDHLIL VANSMTCTGN LIGFNIAGYK ATFRSLKVQV PFTESTLFTP
MKCFEKAAEK CDSDSLGCVV SSSAWGKHAA VGTGSSFQIL WNENQLKSNK EYGDGLYDFL
ALVRTDQEKT DYMFLDDVDY LVEENAADDM CLSPEPDGTL GKPTFEDNFE EQNIQKGSSW
EIGITTNSSW EQNASVANDS GDWGGWSSGG GAAAKPADQD NSWEVHAKVQ DNSTTDWGGW
SVEKPTGEAT VSGEPAETDT WADKGAKMES DAGDGNWEKS STPEASKKND SSENTWDKRK
GDGGDGAWGN RSDDGHGNWE HPSNWNGQSL DVDQDTWGNA RGKKKADGNY CQWEEQPSNY
KQKKTNADHD SSYNNVMPSS EIAWNAGDGT GRPNAKSNAE SSWGEEDKME SDDHPKVPKE
SDTWNTGRSN ESPWDNTDAL QDSWVKSAAR NNNTQDGSWD KVVSMKDLDS LQDSWSKATI
QTNDAQNDSW DNVAKNAPDS AAEDSWGAAT PAETTDSGNK EWKSDGWGAK SGNWSSQRNN
PGRPPRRPDE RGPPPPRQRF ELTVAEKNIL LEVEPIKLRV RSIFREACDG VRLNPEDEKF
ILEKVLEHHP EKQSKVSGEI DYLTVNKHQT FQDTRCFFVV STDGSQADFS YLKCLENFVR
KSYTEDADTF CMKYLRPRRR QAPPADVGTA SGAPDEVPPS TAAETEQGTP PAPQAEVPQE
TWGSPAVPLE GGTHIAGPDS TGDAVILGEQ HDLTPASPAV APQVASEPDT TDGTGLLGKA
PQADWGPRFD AD
//
