ID Q6FQS9_CANGA Unreviewed; 1715 AA.
AC Q6FQS9;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=RPB1 {ECO:0000313|CGD:CAL0132390};
GN OrderedLocusNames=CAGL0I03828g {ECO:0000313|CGD:CAL0132390,
GN ECO:0000313|EMBL:CAG60352.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG60352.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG60352.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; CR380955; CAG60352.1; -; Genomic_DNA.
DR RefSeq; XP_447415.1; XM_447415.1.
DR STRING; 284593.Q6FQS9; -.
DR EnsemblFungi; CAGL0I03828g-T; CAGL0I03828g-T-p1; CAGL0I03828g.
DR GeneID; 2889258; -.
DR KEGG; cgr:CAGL0I03828g; -.
DR CGD; CAL0132390; RPB1.
DR VEuPathDB; FungiDB:CAGL0I03828g; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; Q6FQS9; -.
DR OMA; MVQYDRT; -.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001055; F:RNA polymerase II activity; IEA:EnsemblFungi.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0019985; P:translesion synthesis; IEA:EnsemblFungi.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
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; 2.
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; IPR000684; RNA_pol_II_repeat_euk.
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 Pfam; PF05001; RNA_pol_Rpb1_R; 13.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 15.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 232..535
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1537..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1715 AA; 189767 MW; 2052C2F690A6B4CA CRC64;
MVGQQYSSAP LRTVKEVQFG LFSPEEIRAI SVAKIRLPET MDETQTRAKI GGLNDPRLGS
IDRNLKCQTC QEGMNECPGH FGHIDLAKPV FHIGFITKIK KVCESLCMHC GKLLLDEHNE
QMRQAIQIKD PKKRFNAVWS LCKTKMVCET DVPSEDDPTK LISRGGCGNT QPTIRKDGLK
LVGSWKKDKS TGDADEPEQR VLSTEEILNI FKHISPEDSY RLGFNEEFAR PEWMILTVLP
VPPPPVRPSI SFNESQRGED DLTFKLADIL KANISLETLE HNGAPHHAVE EAESLLQFHV
ATYMDNDIAG QPQALQKSGR PVKSIRARLK GKEGRIRGNL MGKRVDFSAR TVISGDPNLE
LDQVGVPKSI ARTLTYPEVV TPYNIDRLSQ LVRNGPNEHP GAKYVIRDNG DRIDLRYSKR
SGDVQLQYGW KVERHIMDDD PVLFNRQPSL HKMSMMAHRV KVVPYSTFRL NLSVTSPYNA
DFDGDEMNLH VPQSEETRAE LSQLCAVPLQ IVSPQSNKPC MGIVQDTLCG IRKLTLRDTF
LEFDQVLNML YWVPDWDGVI PTPAIIKPKP LWSGKQILSV AIPKGIHLQR FDEGTTLLSP
KDNGMLVIDG EIIFGVVDKK TVGSSSGGLI HVVTREKGPT ICARLFGNIQ KVVNFWLLHN
GFSTGIGDTV ADGQTMREIS ETIAEAKQKV EAVTKEAQAN LLTAKHGMTL RESFEDNVVR
FLNEARDRAG RLAEMNLKDL NNVKQMVSAG SKGSFINIAQ MSACVGQQSV EGKRIGFGFV
DRTLPHFSKD DYSPESKGFV ENSYLRGLTP QEFFFHAMGG REGLIDTAVK TAETGYIQRR
LVKALEDIMV HYDGTTRNSL GNVIQFIYGE DGMDAGHIEK QSLDTMGGSD QAFERRYRID
LLNTSNSLEP SLLESGSEII GDLKVQMALD EEYKQLVKDR RFLRTIFSDG ESSWPLPVNI
RRIIQNAQQT FRIDHTKPSD LTIPEIINSV RDLQDRLLVL RSKSEIIKKA QDDAVTLFCC
LLRSRLATRR VLQEYRLTKE AFEWVLNNVE AQFLRSIVHP GEMVGVLAAQ SIGEPATQMT
LNTFHFAGVA SKKVTSGVPR LKEILNVAKN MKTPSLTVYL EPEYSADQEK AKLVRSAIEH
TTLKSVTVAS EIYYDPDPRS TVIPEDDEII QLHFSLLDDE TEKLLDQQSP WLLRLELDRA
AMNDKDLTMG QVGERIKDTF KNDLFVIWSE DNAEKLIIRC RVVRPKALDA ETEAEEDHML
KKIENTMLEN ITLRGIEGIE RVVMMKYDRK VPNETGEYQK VPEWVLETDG VNLSEVMTVP
GVDPTRIYTN SFIDIMEVLG IEAGRAALYK EVYNVIASDG SYVNYRHMAL LVDVMTTQGG
LTSVTRHGFN RSSTGALMRC SFEETVEILF EAGASAELDD CRGVSENVIL GQMAPIGTGA
FDVMIDEESL VKYMPEQKIT ELEDGQDGGA TPYSNEAGLV NTDIDVKDEL MFSPLVDAGS
SDAMSGGFTA YGGAEYGGAT SPFGAYGDAP ASPGFGGVSS PGFSPTSPAY SPTSPSYSPT
SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS
PSYSPTSPSY SPTSPSYSPG SPTYSPKDED EKKDN
//
