ID E9AQU6_LEIMU Unreviewed; 1810 AA.
AC E9AQU6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012418};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
GN ORFNames=LMXM_16_1350 {ECO:0000313|EMBL:CBZ25317.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ25317.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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};
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DR EMBL; FR799569; CBZ25317.1; -; Genomic_DNA.
DR RefSeq; XP_003873823.1; XM_003873774.1.
DR GeneID; 13450156; -.
DR KEGG; lmi:LMXM_16_1350; -.
DR VEuPathDB; TriTrypDB:LmxM.16.1350; -.
DR OMA; NREDYQQ; -.
DR OrthoDB; 169836at2759; -.
DR PhylomeDB; E9AQU6; -.
DR Proteomes; UP000007259; Chromosome 16.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd01435; RNAP_I_RPA1_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; 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; 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; 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 4: Predicted;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000313|EMBL:CBZ25317.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:CBZ25317.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBZ25317.1}.
FT DOMAIN 396..712
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1114..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1810 AA; 200173 MW; 4033D62D3FF92CEA CRC64;
MSLTTAFPFH AYVGDLRTRT VHERKSGVSL SLMTSEDMAR LAFVEVRVRC GQEDRLAPWT
PAVRRDGTHA TFYDTRMGNF DARTFPPQAC STCCNTLNSK YGNERCQGHY GYISMPRRYP
NDPNRSQERL SVINPHLAQE VEQLLQAECF FCHRFRVPEF DVMRYQQALR LVDSGLIGEA
LRFLDMVANA HGQDMRSRRR RDANETVIND IPLMLDHVDT LLRRRGAGAP PLPRVASGEA
GAHGDVNGDA GAAGALAHAD GSDDGFHKPV LDVRNEICKQ ALRSFREFGN VCSHCQGISP
RITTKNGHLF FFFNKKNADF NVANGGLTTA QLREWEEMNY RQGRSHTYFR TSWVREHIKQ
LCQRESAILA ALFSHLGEAT LHMPYACSLP STYYYKVFFV DKLLVPPLPL RLSSGVQISE
SGGIIPDAGT RALSDVLEFV EQIEAYYVLA NHSTPERNLV STAQEIAQEH NLRNLQAKVT
EVYTDVLESF AKKEGLFRMH MMGKRVNQAC RSVISPDYLV EPNEVLLPRP FARALTFPEL
VSSYSPARMM FLKRCVMNGP DVYPGATHLE IGLPSGETRF VDLHVPELIR RQHAMKYFAM
AQNGSLTVHR HILDGDHLIF NRQPTLHKVS MMAYRAKVLS GLKTLRFHYV NGSSYNADFD
GDEMNIHVVQ SLEAKAELEC LMDANLNYLV PTSGKPIRGF IQDHVVAGVL LTLRDNFLPH
HTFVQFVYNG IAPYMHKHGK PLSAHATLTE LIPMPAVLKP RPLWTGKQLI SVIVHYVTGV
VESRGGAPKS NGVSMHGTSL IQPSTYTTTD PHTGELVAAS RKCMEDDHVQ FFESELITGI
LCKNQLGSSN LSVVHVIHEI YGPHMVGELF GALGRVLSMS LQREGFSIGM DDMMLLQEER
RTALLRELDS APLSLPDDEA TVMPVIMGMA TSLQKEFVPG RMLRPFPHNQ LLTMTMSGAK
GSNTNTIQMS LGLGQQLFDG RRVKRMNSGK TLPPFFVAET RARSLGYAIG RFTSGIRPAE
YTFHAMAGRD GLIDTAVKTS RSGHLQRCLV KGLESLVVQW DHSVRDANGS VIQFLYGGDG
LDPMRTSSLQ AWEVVKDNCV DLGRKMNVNT GVMTGEEEAE EAASRNSQGK RERPHEAAAA
MRAAQRALLE AEAQRDPLPA HYKASLDTYL ETKAQYPLFK KVSQVARWAK NGVLNEKLRE
KREESIRYYR DVMTELTTRR RVRAYCDAGE PVGLLAAQAA GEPSTQMTLN TFHSAGSTVT
HVTEGIPRLR ELLIYASVQK VAIVVPVEKA TEVDEEAISR ILQAGVATRL TDCMARVPAA
VTAGVDGGAA ARVQTTPGYH YRVTRSAEGT QMTVSLLFSK GLLMHKQHAM CMSRVEHLQS
FTQTLKNFAR QVVTALRGRS KDEHEGAGGP LRGTAQDPSS QIDDGGAAAG GGMSDNEDDM
EDRSTQMNTP ALGAASAPSV AGSELGRDDM IPERGDNGGS SGSDEDDYEE EAVDAADGSR
RRKGGNGNSP LHKKSRAEED DNEEEDEDVN GLFWKSASNG VTSSEAAAAA SGKVNYDCFP
MVCAMYGNKK YRVEIAPLQR EAATRDGVVP LPEDLFVVNV SIQTSDQVVT VIPDVLESAL
AQQMFPSWLT QFDSVTYTRK AEDPTSGEMV FQGSSATIRS VTAFLALFTV RARAIKVQKA
RSTDIRDMCT SFGVESGYKA LFDELEKLFK RYSVDYHHLT LIADAATHRG VWENYNFTGV
ISHSASPLFQ MTFASSKRFL HTALTRGVGD ELNSISSAIM VGERPRVGTA LVKVGQDPQI
LRDVIEKNFA
//
