ID M7X7C7_RHOT1 Unreviewed; 1787 AA.
AC M7X7C7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=RHTO_00418 {ECO:0000313|EMBL:EMS25990.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS25990.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS25990.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS25990.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(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|RuleBase:RU004279}.
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DR EMBL; KB722642; EMS25990.1; -; Genomic_DNA.
DR RefSeq; XP_016277109.1; XM_016414102.1.
DR GeneID; 27364431; -.
DR eggNOG; KOG0262; Eukaryota.
DR HOGENOM; CLU_000487_2_3_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
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; cd02735; RNAP_I_Rpa1_C; 1.
DR CDD; cd01435; RNAP_I_RPA1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.357.120; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 1.
DR Gene3D; 6.10.250.2940; -; 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; IPR047107; DNA-dir_RNA_pol1_lsu_C.
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; 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; 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; 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 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 410..767
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 144..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..339
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1513
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1787 AA; 197210 MW; 2F078FDD8B743C18 CRC64;
MDIANPVATQ VTSLSFSYLH APDIRRMSVK QVVNPVLFDN LNNPNAGGLY DPAFGPLGKG
DICSTCHLTS FECPGHFGHI ELPAPVFHPL YMVQAFQLLR GTCTYCHRFL VGEIQLLKQI
ARLTLLEHGL VTHALELDAH FQGPAPASKS KSAKARAAAA AADNVEDAEQ GESTDETADE
FRARLDAFVQ GALRAAKKGK GVGMEHHGRD EYKESGTAFD VRRKVIAQFL KTLGAKRRCE
HCGAYAHRVR KEGHTKIIQY SLVAKQKAIH KTMRLKAPNV LREARLAGMK ANGNGKAKME
VDGETDESED DSEEEEEEDK EMHVDGADEV EEREEEEDED AIGSVRGKQT ERIVTPDEVR
AHLRRLFANE QELVTLIYAP HGPLSRASSS RIPRSSPGQK QGGKPAASAD IFFMDVVSVP
PSRFRPASTM GDQVFENPQN SLLNNILRQS IVVRDLNVRL LQAQTQPDHP DLVGEDGKPR
VTIERMTTML YESLIDLQVT VNSMMDAGKN PMLVKQGKLP TPGVKQLLEK KEGLFRKNMM
GKRVNYAARS VISPDVNIET NEIGVPPVFA RKLTFPEPVT DHNYQQLKQA VINGPHQHPG
ASFVQMEDGN LISLDRMSLE DRTAIANKLL APETSTAGQR LAASSRPDVG LPPTRTPQIN
RKVYRHLQDG DIVILNRQPT LHKPSMMCHR VKVLKGEKTI RMHYANCNSY NADFDGDEMN
MHFPQSLIAQ AEARMIANTD NQYLVPTSGN PLRGLIQDHV VAGVWLTNKD TFFTRDQYYQ
LVYGALRPEN DYTGEGTVKT VPPAVWKPRP MWTGKQVIST VLKNIQPADM CGIHFTSKGK
VPGSAWGVFA EEGEVLVHDG DMLTGIIDKA QIGASPFGLV HSVYELYGAS TAGKLLSILS
RLLTKFLQSR AFSCRMDDLV LTAKGNHDRR RMLQTVNEKG LSAALDYTGL ASADRADPAT
ADDLRNRLEE ILRDDYKLAG LDATVEGETN QVTTQLIKTC LPNGLVKPFP HNNMQTMTVS
GAKGSNVNAS QISCLLGQQS LEGRRVPVMV SGKTLPSFKA FETAPRAGGF VAGRFLTGIR
PQEYYFHCMA GREGLIDTAV KTSRSGYLQR CLIKHLEGLR VHYDHTVRNA DQSVLQFHYG
EDSLDVTKQK HLLQFEFAVR NMQSIISRYN PRDALERTND VEDVLPDAMK KSLKKPDTHP
PVLSLASPST VSGAVSERYA RAIEDYVKNP KQRLLRPKKK RDMADWPAHI RRDDLVSIEH
FRSLMNMRYM RSLVEPGEAV GLLASQGVGE PSTQMTLNTF HFAGHGAANV TLGIPRLREI
VMTASQDIKT PTMNLPIVES VSDARLKTFC QSSTRLTLSQ VVDDVTVEER LTPKTSDNSY
TRSKLYTVRL NLFPRADYEA EYSVSSEQIL AGIARTFVPL LDKAIAKEIK QNDRELKSQA
ADVGRGKKEG KRRGGKTSGA DEDGAGEEDA GVVGRDEGEV IDGDADDERR GRQADDEQNY
DDEDEGDEAA DPEEELEAKF KSDAEEDEES SDEEDDDPEA VARRSKAESL ERMKQYERRV
SGSSRFINKL VFDKEQGESC EFELEFSSQA AKLLLVGIVE EVCRIAVVHE VPGISRCFVA
KAANANAAAQ RNAVTEGVNL RQLWQIGYGI VDLNKLGTND IGAILRTYGV EAARTAIINE
MSAVFSVYGI GVDYRHLTII ADYMTCEGGY KPFNRTGLGN NASPLTKASY ETTSAFIAEA
ALHGDFDNMI SPSSRVVVGR PPEAGTGAFA IRSIVEAAAG AGSLDEM
//
