ID G7LG09_MEDTR Unreviewed; 2010 AA.
AC G7LG09; A0A0C3XZ72;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN OrderedLocusNames=MTR_8g038990 {ECO:0000313|EMBL:AET02314.2};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AET02314.2, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AET02314.2, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AET02314.2}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AET02314,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:AET02314.2, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AET02314,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:AET02314}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AET02314};
RG EnsemblPlants;
RL Submitted (APR-2015) 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; CM001224; AET02314.2; -; Genomic_DNA.
DR RefSeq; XP_003627838.2; XM_003627790.2.
DR STRING; 3880.G7LG09; -.
DR PaxDb; 3880-AET02314; -.
DR EnsemblPlants; AET02314; AET02314; MTR_8g038990.
DR Gramene; AET02314; AET02314; MTR_8g038990.
DR eggNOG; KOG0260; Eukaryota.
DR eggNOG; KOG2992; Eukaryota.
DR HOGENOM; CLU_002449_2_0_1; -.
DR Proteomes; UP000002051; Chromosome 8.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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:0006366; P:transcription by RNA polymerase II; IEA:GOC.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.450.40; -; 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; 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 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
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 230..529
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1318..1817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1935..2010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1946..2010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2010 AA; 223482 MW; 361B6351D81B7081 CRC64;
MVYDGTLWCN LIHVYRFTKV FIMEDNATTS LLDGKVVGIR FSMATRHEIS TASISDSQIS
HASQLANPFL GLPLEFGRCE SCGTSEAGKC EGHFGYIELP VPIYHPSHVT ELKKILSLVC
LSCLRLKKTK VPSSSSGLAQ RLLSPCCEDV NAAQVSIREV KTADGACYLA LKVSKSKMHD
GFWTFLEKYG YRYGGDHTRA LLPCEAMEII KRLPQETKKK LAGKGYFPQD GYILKYLPVP
PNCLSVPVVS DGVSIMSSDP ALTILRKLLR KVEVIRSSRS GEPNFESHQV EANDLQSVVD
QYLQIRGTSK AARDIETHYG VNKELNDSST KAWLEKMRTL FIRKGSGFSS RNVITGDGYK
KINEVGIPLE VAQRITFEER VSIHNIHYLQ KLVDENLCLT YKEGMSTYSL REGSKGHTYL
KPGQIVHRRI MDGDTVFINR PPTTHKHSLQ ALVVYIHDDH TVKINPLICG PLGADFDGDC
VHLFYPQSLA AKAEVLELFS VEKQLLSSHS GNLNLQLSAD SLLSLKMLVK SCFLDRVAAN
QMAMFLLLPL PMPALLKATT GDSYWTSIQI LQCALPFSFD CTGGRYLIRQ REILEFDFTR
DILPSIINEI AASIFFSKGP QEALNFFDVI QPFLMENIFA HGFSVGLQDF SISRAVKRVI
NRSIGKVSPL LRQLRGMYKE LVAQQLEKVI QDIELPVINF ALKSTKLGDL IDSKSKSAVD
KVIQQIGFLG QQLFERGKFY SKGLVEDVAS HFQLKCFYDK DDYPSAEFGL LKGCFFHGLD
PYEELVHSIA TREIIDRSSR GLSEPGTLFK NLMAILRDVV ICYDGTVRNV CSNSIIQFEY
GIQSGDAAQH LFPAGEPVGV LAATSMSNPA YKAVLDASPS SNSSWGFMKE ILLCKVNFRN
EPNDRRVILY LNDCDCGRNY CRENAAYLVQ NQLRKVSLKD AALDFIVEYQ QQRRRRDGTE
DAGLVCHIRL KEVKLEELKI NMTEVYQKCQ EKLNSFSRKK KLSPFFKRTE LIFSEFCSAP
CVTFLWPDGV DLDQTTKVLA DMICPVLLET IIQGDPRISS ASIIWVNPGT NTWVRNPSKS
SNGELALDVI LEKEAVKQSG DAWRIVLDSC LPVLHLIDTR RSIPYAIKQI QELLGIACTF
DQAIQRLAAS VRMVAKGVLR EHLILLASSM TCGGNLVGFN TGGYKTLARQ LDIQVPFTDA
TLFTPRKCFE RAAEKHHSDS LSSIVASCSW GKHVAVGTGS KFDIVWDPKE IKTNEIEGMN
VYKFLNMVKG LANGEEETNA CLGEDIDDLF DDENGDFDMS PQHASGFDAV FDETFELPNG
STSNGWDSNK DQIDQPNTNS NDWSGWGPNK SDLQVDVIQE DSSKSSAWGA ATNQKSDQSA
SAWGKAVVQE DSSKSGAWGT ATNQNSQQPS WGAATNQKSD QSASAWGKAV VQEDSSKSGA
WGNAKSVVQE DSSKSGAPAN TNHSSDQSCW GQITGGEERA QGESGGTKKW KADVSQEDST
NSGGWKAWGS SKPEVHEGES TKVQDSWNSQ KWKAGEDVTQ KDSQKSSAWG ATKLKSNDIQ
EDSTNSGGWK AWGSSKPEVH EGESTKVQDS WNSQKWKAAE DVSQKDSQKS SAWGATKPKS
NDNRSSWGQK KDEIHVMPED SSRSNAWEQK PENVKDSWVA KVPVANSSWG KAKSPENRPW
DSKNEPNNSF GKPNSQENEP WDSKNESDSS WGKPKSQESQ PWDSKNESNS SWGKPKSQEN
HPWDSKNESN QTAGSRGWDS QVASANSESD KSFQWGKQGR DSFKKNRFEG SQSGGPNAGD
WKNRSRPVRP PGQRFELYTP EEQDIMKDIE PIVQSIRRIM QLQGYNDGDP LANEDQKYVL
ENVFEHHPDK ETKMGVGVDH VMVSKHSNFQ DSRCLYVVLK DGKKEDFSYR KCLENLVRKK
YPETAESFCG KYFRKPQPRV KRDQTPNPAG EQTAAPNPAG EQTAAPNPAG EQTATQNPPG
EQTSTPNPAE EQTPTPAGDQ TSTPVPMETN
//
