ID E3QRH3_COLGM Unreviewed; 1707 AA.
AC E3QRH3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=GLRG_08740 {ECO:0000313|EMBL:EFQ33461.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG697370; EFQ33461.1; -; Genomic_DNA.
DR RefSeq; XP_008097481.1; XM_008099290.1.
DR STRING; 645133.E3QRH3; -.
DR EnsemblFungi; EFQ33461; EFQ33461; GLRG_08740.
DR GeneID; 24414105; -.
DR VEuPathDB; FungiDB:GLRG_08740; -.
DR eggNOG; KOG0262; Eukaryota.
DR HOGENOM; CLU_000487_2_4_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000008782; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 371..696
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 270..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1707 AA; 188384 MW; B49CE4DCD58AC5A1 CRC64;
MNISQPISSS IETVEFTFLT DEEIKAISVK RIENDSTFDN LLNPVPGGLY DPALGSWGDA
LCATCNLNQS SCPGHAGHIE LPVPVYHPIF LDQVLRLLRS QCVYCKGFRM RHREINRYSC
KLRLLQHGLL HEAHLVDAIG EELKGLALPG VPTDYESEAE EEGTSSVDNI IGAREAYVRQ
ALKSHKLSLG EVRKGKHEGA IEMRRELIKD FLTQITKPRR CDNCGGISPA YRKDRFVKIF
EKALSERDLA QMAQRNLHVK DSMATAARVR KSKSKRNAVD ADEGVADIDM TSAEENDVEM
RDASDDEQDL ADKEDGSLVD AVAVAPGQQR YISAMEVRAR LRELFEKEQD IMSLVYSSKP
MTKKSAKVSA DMFFIRTILV PPNKFRPEAR TGDSQISEAQ QNSLYKMIMR NCGNIARIHQ
SVGATDQYGR PRDITDLHQV WTELQESVNS LIDKSKNPVQ GAAAKRNEDG IKQKLEKKEG
LFRKNMMGKR VNFAARSVIS PDPNIETNEI GVPPVFARKL TYPEPVTSHN FRDMQQAVIN
GVDKWPGAAA IEYENGQIVN LRSKSVDDRV SLANQLLAPT NNQMSGMKSK KVYRHLTNGD
VVLMNRQPTL HKPSIMGHRV RVLPGEKTIR MHYANCNTYN ADFDGDEMNM HFPQNEVARA
EALQIADTDH QYLSGTAGKP LRGLIQDHLS VSVALCNKDT FFDRDSYQQL IYSALRPESG
HILGERIELL PPAVIKPRPR WTGKQVISTI LKNIKPPNGE GLWMAGKCQV KGEQWGKSHV
EEGSVLFQDG QFLTGILDKA HLGPSSGGLI HSIHEIYGPA VAGKLLSGMG RLLTRYLNMR
AFTCGMDDLR LTSEGEQARR EALKAARTIG LEVAAKYVSL EDKAPNSTDP ELLIRLEEVM
RDDTKQEGLD MLMNQSSGMV SSAVTTACLP VGLVKQFPKN QMQSMTTSGA KGSQVNANLI
SCNLGQQVLE GRRVPLMVSG KSLPCFKPFE TDVRAGGYIV QRFLTGIRPQ EYYFHHMAGR
EGLIDTAVKT SRSGYLQRCI IKGMEGLTVT YDSTVRDADG TLVQFLYGED GLDPTKQKYL
TDFSFVLRNV GSESAQLNFS NGFKEKLAGS KDEILKHMKS AIKHAKLNSA AAKDPIISMV
NPARVAFATS EKFYEQMTKY IKDNEDGLIR DKSAVSSGLI NAPAVSKKSA ELVFAAKYMR
SLVEAGEGVG IVAGQSVGEP STQMTLNTFH LAGHSAKNVT LGIPRLREIL MTASRSISTP
AMNLLLHEEL SAAEGEVFAK SISVLPLADV LDTAIVNERI GKGNNGALAK LYDVRLNFFP
ANEYTKAYAI DTSDVMDTIE KRFLDHLLKI MVREIKKRRS ESTSATPDVG VKAGVVEMAT
GNGEARAAND DNDEDDDDGD NDATNAKNKA NREEAVSYGP NDDEDDAIQR QMERENSPEE
DEGFEGSPPP RTDKDGSDDE YDGDGDVDSD EGALRAERVK DRYLRVTKFR NDEAGEWCEF
TLEFEANTPK VLMLNIVQAA VKKSVIQQIP GVGSCTFTAD HKIKDSAGND VSVPAIYTSG
CNLKAMQKYG DFINPNKIAT NDIGAVLDVY GVEACRNNIV SELAGVFSGH GISVDNRHLN
LIADYMTRNG DYTPFNRNGL RGNVSPFTKM SFETTLAFLK DAVLDGDWDD LRTPSGRIVM
GRLGKIGTGA FDVLTALPTH HMSSNAE
//
