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Database: UniProt
Entry: G0UT19_TRYCI
LinkDB: G0UT19_TRYCI
Original site: G0UT19_TRYCI 
ID   G0UT19_TRYCI            Unreviewed;      1754 AA.
AC   G0UT19;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=TCIL3000_8_7610 {ECO:0000313|EMBL:CCC92532.1};
OS   Trypanosoma congolense (strain IL3000).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX   NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC92532.1};
RN   [1] {ECO:0000313|EMBL:CCC92532.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IL3000 {ECO:0000313|EMBL:CCC92532.1};
RX   PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA   Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA   Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA   Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA   Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA   Hertz-Fowler C., Berriman M.;
RT   "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT   African trypanosome species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR   EMBL; HE575321; CCC92532.1; -; Genomic_DNA.
DR   OrthoDB; 169836at2759; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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; cd02733; RNAP_II_RPB1_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; 3.30.1360.140; -; 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; 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; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
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:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 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   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          242..534
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1633..1662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1697..1754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1754 AA;  195453 MW;  C7BE1A55CE405B14 CRC64;
     MSGGAPLPPS HMELQKVNEV QFEIFKERQI KSYAVCLVEH AKSYERGKPV RGGINDLRMG
     TTDFEFACET CHRKHPECPG HFGYIELAEP VFNIGVFDLV LQVLKCVCKS CGALLLNTRA
     DDVHKKLHNL TGLSRLRQAA KMAETKCRMS TDLEDEVGDD GLNGGSFGGG GAVAGARAAR
     GCGASQPRVS RFYGIYPTLI VKAVHGDQDA EWHADKVRQV LDRVSDEDAR LMGFDPLRCH
     PRDLVLTVLP VPPPQVRPAI SFGGLKSDDE LTHQIMAIVK RNNQLRKDKE SDVQAAIDRS
     RALLQEHVAT YFNNSSTYYK PTKVNDSKKL KSLTERLKGK YGRLRGNLMG KRVDFSARTV
     ITGDPNIDVD EVGVPFSVAM TLTFPERVNT VNKKRLTEFV RREVYPSANY IHHPNGTITK
     LALLRDRSKV TLNIGDIVER HVINGDVVLF NRQPTLHRMS MMGHRVRVLN YNTFRLNLSC
     TTPYNADFDG DEMNLHVPQS LLTKAELIEM MMVPKNFVSP TSQRRAWELC RTVCSEATGD
     KDTFLDKYFV QSVALWLDLW QLPIPAVLKP RPLWTGKQVF SLILPEVNHP TTPHDKPPFP
     HNDSSVMIRR GELLCGPITK GIVGAAPGSL IHVIFNEQGS DEVARFINGV QRVTTFFLLN
     FGFSVGVQDT VADTDTLRQM NEVLVKTREN VEKIGAAANN RTLNRKAGMT LLQSFEADVN
     SALNKCREEA AKKALSNVRR TNSFKVMIEA GSKGTDLNIC QIAVFVGQQN VAGSRIPFGF
     RRRTLPHFML DDYGETSRGM ANRGYVEGLK PHEFFFHTMA GREGLIDTAV KTSDTGYLQR
     KLIKALEDVH AAYDGTVRNA NEELIQFMYG EDGLDGARIE GGQLFPLPFR DNKEMEQMYK
     YEYEADGTFT GKVGGNYMDP HVKKMLRADP ENVRKLHGEY EQLMADREWS RKMLDLEDRE
     KLKLNLPVNP GRLIQNARST MGKRSQVSNL SPITIIDHVR KLQEDLMKLF PSYHRDADRR
     ITNVLSRQRI ESALTLFNVH LRQLLASKRV LKEYKLNDKA FEYLLKEIRT KYHQSLATPG
     ENIGAIAAQS CGEPATQMTL NTFHNAGISS KNVTLGVPRL LELLNVSRHQ KHASMTVTLF
     PPWDKKRVAQ KAQHLIEYCT LESITQRIQF IYDPDPRHTV VEVDRDILEL EWDVMDESDA
     EQRVREVEEG SPWVVRLELD VDMVTDKALD MKDVKQAIQR VDTNYIIETG MANNVRRRTI
     RLRSRTNDGA DSIPKLKRDI PALLARVHLR GIPGVRRALL KDTTKFTVDE STGKLTGEKT
     WVIDTDGTAL RRAFIGVVGE DGKNIINATK TSSNKVPEVC SLLGIEAARY RMLTELREAY
     LAYGLNINYR HYTILVDTIC QRGYLMAVSR TGINRSDTSG PLMRCSFEET VKVLMAAASF
     GEHDPVRGVS ANLVLGNQAR VGTGLFDLII NMPALQQAVT QEDAVAPGKN VNVYHGLGST
     LQQNLQSSMV YRPRENDATP FVNDASIFFH GGPAGGSSSA PATASAPLNP SLPYGGRFEA
     STVHHSQIYP SASVTEYSAR EVSYSQQYSV ASASAFNPIS THLPSTAQVS VDYSAMSSYH
     LQYSVAAPSM HTSFPRSETS MATPSANREQ STSAPYMPSA MSSTALPSHA YASTEVDLLP
     SDNSRSQSAL YVPTFSPAHA GASTHHNEPG DRQRAGGTAA AEDEDLSVNY LPTTQVQSSA
     VPPAEYVDEE EEEQ
//
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