ID K7K551_SOYBN Unreviewed; 1454 AA.
AC K7K551;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=100810483 {ECO:0000313|EnsemblPlants:KRH77475};
GN ORFNames=GLYMA_01G215700 {ECO:0000313|EMBL:KRH77475.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH77475.1};
RN [1] {ECO:0000313|EMBL:KRH77475.1, ECO:0000313|EnsemblPlants:KRH77475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH77475};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH77475.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH77475}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH77475};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH77475.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH77475.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; CM000834; KRH77475.1; -; Genomic_DNA.
DR RefSeq; XP_014632415.1; XM_014776929.1.
DR EnsemblPlants; KRH77475; KRH77475; GLYMA_01G215700.
DR GeneID; 100810483; -.
DR Gramene; KRH77475; KRH77475; GLYMA_01G215700.
DR HOGENOM; CLU_002449_0_1_1; -.
DR OMA; NCEITDG; -.
DR OrthoDB; 451894at2759; -.
DR Proteomes; UP000008827; Chromosome 1.
DR ExpressionAtlas; K7K551; baseline and differential.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; 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; cd10506; RNAP_IV_RPD1_N; 1.
DR Gene3D; 1.10.132.30; -; 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; IPR040403; NRPD1_N.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF36; DNA-DIRECTED RNA POLYMERASE IV 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; PF05000; RNA_pol_Rpb1_4; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
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 211..499
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 1454 AA; 163418 MW; 88CDCD6DB5274240 CRC64;
MDDDLLQRNK TPSVVIKAIK FDVLTEEDIE NISVLEINAA GQVTGSNLGL PNASDECATC
GTKDKKFCEG HFGVIKFPTP ILHPYFMLEI AHILNKICPV CKSIRHKSKG ARLIYGTKRS
NDCNYCSVYP SMQFRVSSND LFRRTAIIVE VKASKKTLGT EIPADFWNFI PCDAQQEENY
VNRRVLSPVQ VNYLLNDVDP DFIEKYIPRK NLLCLNCFPV TPNCHRVTEV PYAISSGSRL
SFDDRTRSCK KLVDFRGTAN ELSSRVLDCL RISKLNPDKT PNSIFADIQQ RKIGENAFNS
SGLRWIKDVV LGKRNDSSFR TVVVGDPDLE LSEIGIPCHI AESLQVSEYV NRQNREKLLY
CCELHLLEKG KINVCRKGSI VHLYKKEDLQ IGDKFYRPLA DGDKVLINRP PSIHQHSMIS
LTVRVLPISS VVCINPLCCS PLRGDFDGDC LHGYIPQSVT ARIELNELVA LDRQLINGQS
GRNLLSLSQD SLTAAYLLME DGVLLNVYQM QQLQMLSISN KRLIPPAVVK APSSNSSLWN
GKQLFSMLLP YDFDYSFPSD GVVVSDGELV SSSEASGWLR DSDYNVFQSL VEHYQGKTLN
FLYAAQKVLC EWLSMTGFSV SLSDLYLSSD SYARENMIEE IFYGLQDAER ACNFKQLLLD
YYCDFLSGSL QESENAITVN ADRLNYERQI SASLSQASVD AFRQVFRNIQ SLADKYACKG
NSFLAMFKAG SKGNLLKLVQ HSMCLGMQNS LVRLSYRLPR HLSCADWNSQ KWVDSIQMSS
GTLESVQSYI PYAVVESSFL TGLNPLECFV HSVTNRDSSF SDHADLPGTL TRRLMFFMRD
LYDAYDGTVR NLYGNQLIQF SYDIEEDSSC NKGFQQYALG GESVGAISAC AISEAAYSAL
GQPVSLLETS PLLNLKNVLE CGSRKRNGDQ TVSLFLSEKL GKQRHGFEYA ALEVKNYLER
LLFSNIVSKV MIIFTPHDSR SQEKYSPWVC HFHLDKEIVT RRKLKVHSII DSLYQRYYSQ
RKDSKVCFTN LKISSRKCSA DSMVKEGEDT SIDKEEGDDC IMVTIVENSK NPIQLDSVRD
LVIPFLLGTA IQGFLDVKKV DILWNNQSKV TNSRNGFSGE LYLRVTLSSE GSRGRFWGVL
LKLCHKIMHI IDWTRSHTDN INHFSSAYGI DAGWQYFFNS LACATSDTGK SILPKHLCLV
ANSLSCSGEF VGLNAKGMAL QRKHASVSSP FVQACFANPG SCFIKAAKSG ATDNLQGSLD
GLAWGNCLSM GTSGMFDVIY SEKVAKSVDV YELLEASFDK PNNKIGTHLH KYSSDKCGSE
FRHKNGYALK EGKQWKTILR NFVTVNDIQK LTFASRCILN KYSIDELLSE SDRSTMLRVL
NFHPHKSEKF GIGPQDIKVG WHPKYKDSRC FHIIRTDGTV EDFSYRKCIL GALDIVDPKK
SKIQEKKWSG HGDT
//
