ID A0A164WRW3_DAUCS Unreviewed; 1654 AA.
AC A0A164WRW3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=DCAR_020471 {ECO:0000313|EMBL:KZM92164.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM92164.1};
RN [1] {ECO:0000313|EMBL:KZM92164.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM92164.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM92164.1}.
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DR EMBL; LNRQ01000006; KZM92164.1; -; Genomic_DNA.
DR STRING; 79200.A0A164WRW3; -.
DR EnsemblPlants; KZM92164; KZM92164; DCAR_020471.
DR Gramene; KZM92164; KZM92164; DCAR_020471.
DR OMA; NREDYQQ; -.
DR Proteomes; UP000077755; Chromosome 6.
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; 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};
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:UP000077755};
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 330..641
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 256..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1362
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1654 AA; 185454 MW; 36B1A5F9C49EB2A2 CRC64;
MALSNEVTSE SVAAVQFSFM SAEDVRKHSV KQITNPILLD PIAEPIPGGL YDPALGPYDL
NKICKTCGQR CNDCPGHCGH IELVSTVFNP LLFDKLYNII ARTCFTCFRF RMDEEEVKLC
ISKLEMIAKG DIIGARRLDE GGVLDTSTSP EDGETSDFQD PNTWSSLQYT ESISVLKKFF
KPRPTACKHC KAKNPKITKP TFGWFYMSGL SAADARANII RASGKTISSV EANSNEDTYV
AEIETVESES CMTTSVETED TRNQRHVQTG KGFSPHSYKQ KNTLSRPFLP SEVHATLEQL
WANESAILSY ICGVQHESPK LTNGQAPSHS MFFIDALLVP PTKFRPPAVT ADSVMEHPQT
GHIIKVLNAN IALCNARANN SEPSIIVRRW LDLQQSINLM FDSKTSMSRS ATPGICQLLE
KKEGIFRQKM MGKRVNHSCR SVISPDPYLA VNEIGIPPYF ALRLTYPVKV TPWNAQKLRE
AIINGPEIHP GATNFVDKVS NSKLPLKKKG RISVSRKLSS SRGEASTKSH EMEGKIVFCH
MKDGDVVLVN RQPTLHKPSI MAHIVRVLPG EKTIRMHYAN CSTYNADFDG DEMNVHLPQD
EVSRAEAYNI VNANNQYIVP TRGDTVRGLI QDHIGAAVLL TMKDTFLTRE QYDQLLYSSG
VFSAGPSLSS KSLSKKISKV ESYGLQPVLP AVWKPKPLWT GKQVITSLLN HLTRGCKPCT
LENEGKIPYQ YFSRNSSNNQ LSKDEEASAE NKVLIRRNEL VRGVIDKAQF GKYGLVHTVQ
ELYGSDTAGI LLSALSRLFT CFLQMHGFTC GVDDLILLPQ YDVLRKEELE GEDVGEEVHC
DFVNFKRGKI GPKELQYEIE KIMRNNGESA VARLDGKMKN ELREKGSKIN KELLLNGLYK
PFPKNCISLM TISGAKGSSV NFQQISSSLG QQELEGKRVP RMTSGKTLPS FSPWDFSSRA
GGYITDRFLT GLRPQEYYFH CMAGREGLVD TAVKTSRSGY LQRCLVKNLE CLKVCYDYTV
RDADGSIVQF CYGEDGVDVH QTSFLNKFEA LAKNQEIIGQ KFHHKLEYNA YIDKLPNKLK
ERVDELIRTS LKGQFLEQLK QQDLLMLMKQ KYISSLAQPG EPVGVIAAQS VGEPSTQMTL
NTFHLAGRGE MNVTLGIPRL QEILMTATSE IKTPIVTCRL LEEKSKDDAK ALVAKLKKVT
VADIIESVEI CVVPLYVYKD EICRLYKLKI KIKKHELVSE EDCRETLEIT YLRELEDAIE
NHVQLLARIS GIKDFTENIE SMSASQTRDA VSGNKSQGND DDDENGDNEG DDFGFDAQKR
KQQASDEIDY EDGIDGKTTE VELSTEVESE IDQDDDEIES SIGHVEDVDV EDEPSNVSYD
KGLITEPTST DRKAQSKSKK KKRGNLARKE TDRSCFVKTE GQRYEVHFRF KDEPHILLSQ
AQIKCYDMIL EWNMLQIVQK AAKKVPLIGS GKIEHCQQLA YDVLEKQVLW QKEENGAAEV
QKDLSNLCAL KVAGVNLTAL WEMQDVLDVN HIYSNNIHLM LKTYGVEVAR KTIIKEVQDV
FKIYGVEIDY RHLSLIADYM THSGEYRPMS RHGMISESLS PLMKMSFETC SKFIVEAASH
GQTDNLETPS SRICLGLPVK LGTGSFDLMQ NLQL
//
