ID Q4DDX5_TRYCC Unreviewed; 1731 AA.
AC Q4DDX5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=Tc00.1047053509011.20 {ECO:0000313|EMBL:EAN90718.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN90718.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN90718.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN90718.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
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}.
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:EAN90718.1}.
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DR EMBL; AAHK01000598; EAN90718.1; -; Genomic_DNA.
DR RefSeq; XP_812569.1; XM_807476.1.
DR AlphaFoldDB; Q4DDX5; -.
DR SMR; Q4DDX5; -.
DR STRING; 353153.Q4DDX5; -.
DR PaxDb; 353153-Q4DDX5; -.
DR EnsemblProtists; EAN90718; EAN90718; Tc00.1047053509011.20.
DR GeneID; 3543784; -.
DR KEGG; tcr:509011.20; -.
DR eggNOG; KOG0260; Eukaryota.
DR InParanoid; Q4DDX5; -.
DR OMA; KTSDTGY; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000002296};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 225..524
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1679..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1731 AA; 193078 MW; FC783A1468E3BE28 CRC64;
MSGGAPLPPS QMDLQKVVEV QFEMFKEKQI KDYAVCLVEH AKSYERGQPV RGGINDLRMG
TTDFEFACET CHRKHPECPG HFGYIDLAEP VFNIGVFDIV LQVLKCVCKS CGALLMDTND
PQVHKKLQHL TGVNRLRQVV KMCGMKCRMS TDATTPEEAV VARGCGATQP RIGRYLGIYP
TLIIKATLEE QDMVWHADTA RQVLDRVSDE DARVMGFDAL RCHPRDLVLT VLPVPPPQVR
PAISFGSLKS DDELTHQIMS IVKRNNQLRK DKESDVQVAV DRSRALLQEH VAAYFNNASM
YYKPTKVNDT KKLKSLTERL KGKYGRLRGN LMGKRVDFSA RTVITGDPNI DVDEVGVPFS
IAMTLTFPER VSAVNKKRLT EFVRRPVYPS ANYIHHPNGT TTKLALRRDR SKVTLNIGDV
VERHVINGDV VLFNRQPTLH RMSMMGHRVR VLNYNTFRLN LSCTTPYNAD FDGDEMNLHV
PQSLLTKAEL IEMMMVPKNF VSPNKSAPCM GIVQDSLLGS YRLTDKDTFL DKYFVQSVAL
WLDLWQLPVP AVLKPRPLWT GKQVFSLILP EVNHPATPQE RPPFPHNDSS IMIRRGQLLC
GPITKGIVGA APGSLIHVIF NERGSDEVAR FINGVQRITT FFLINFGFSV GVQDTVADAD
TLRQMNEVLV KTRENVEKIG AAANNRTLNR KAGMTLLQSF EADVNSALNK CREEAAKKAL
SNVRRTNSFK VMIEAGSKGT DLNICQIAVF VGQQNVAGSR IPFGFRRRTL PHFMLDDYGE
TSRGMANRGY VEGLKPHEFF FHTMAGREGL IDTAVKTSDT GYLQRKLIKA LEDVHAAYDG
TVRNANQELI QFMYGEDGLD GARIEGGQLF PLPFRDNKEM ESTYKYEYDE TGAFNEKVGG
AYMDPHVKKM LRADPENVRK LQSEFDQLMA DRDWARRMMD LEEREKLKLN LPVNIGRLIQ
NARSTMGKRS QVSNLSPVTI IDHVRKLQED MLKLFPCYHK GVDGRIHNLL SRQRIENALT
LFSVHLRQLL ASKRVLREYK LNDKAFEYLL KEIRTKYLQS LVSPGENIGA IAAQSCGEPA
TQMTLNTFHN AGISSKNVTL GVPRLLELLN VSRHQKHASM NVSLYPPWDK KRTAQQAQHL
IEYCTLESVT KRIQFIYDPD PRETVVEADR AILELEWSVM DESDERARLQ EVENGSPWIA
RLELDADMFV DKALNMKDVK QAILRVDDGY VIETGMANDT KERTIRMRPK KNDGVDSIPR
LKHAIPELLA RVHLRGIPGV RKALLKDRTT FTVDPATGKM TGEKTWLIDT DGTALRRAFI
GIVDEKGNNI INATRTSSNK VPEVCSLLGI EAARYKMLHE LREAYLAYGL NINYRHYTIL
VDTICQRGYL MAVSRVGINR SEMSGPLMRC SFEETVKVLM AAAAFGERDP VRGVSANLVL
GNQARIGTGL FDLVLNMAAL QQAVPQEDAV APGKEVNVYH GLASTQNLPS SMPYRAKDHE
TTPFVNDASL FFREGVGGSS SAAPLTASTL YGGMHEASAV HFSQAYPAMG MSDQRVRASS
VSQPYSVMSS ASVYNPASMQ VPSALPSSVD YSEASSFHIQ SSMAMPSVPS SPQFEAPQAF
GGGRFGGLSP AYVPSVMSSV ATQPYQCVGD SESQQSASYV PTLSPAYSAY TARRSVVASR
ASASRVDQQS QQQEDDSASY LPKSPGLHGL PPPVGEFSLT EDPEEEEEGH Q
//