ID A0A1S7UIU5_ROSNE Unreviewed; 1585 AA.
AC A0A1S7UIU5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=SAMD00023353_0401460 {ECO:0000313|EMBL:GAP83144.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP83144.1};
RN [1] {ECO:0000313|EMBL:GAP83144.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP83144.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004279}.
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DR EMBL; DF977449; GAP83144.1; -; Genomic_DNA.
DR STRING; 77044.A0A1S7UIU5; -.
DR OMA; AVCPPYN; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000054516; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_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; 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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 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:UP000054516};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 264..569
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 1585 AA; 177098 MW; 1D078981100224CA CRC64;
MATITATGVA APVKHQVVDK LPKRFKNLKF GIQSNQDIVN QGVLEVSDRS MYDVDKGREP
THNGVLDKRL GTSSKTGICT TCNQRVADCI GHFGHVRLPL PAFHIGYIKF TISILQNICK
DCSRVLLVEQ ERRAYLKELR RPNIDNMKRV AICKKINDQC RKTKHCPYCK AVNGQIRKVG
ALKLVHDKFV SYNKSTSAKK QPPLSKIEFD NSFAEARKHV NDLDKHIRKA FEDLNPLRVL
NLFKHITPDD CELLGLNPSE GRPEMFLWQY LPAPPVCIRP SVAQEGASNE DDITTRLGDI
VFACGLIRAA LQKGTALQTI MEQWEYLQLQ IAVYVNSDVP GLRDNGVTKT MRGFCQRLKG
KQGRFRGNLS GKRVDFSGRT VISPDPNLAV NQVAVPMLVA KNLTYPERAH RDNMTKLRQC
IVNGTNVWPG AQAILKSNGD HPPFRVSLRF GDREAAAKEL RIGDIVERHL EDGDIVLFNR
QPSLHKLSIM SHLVKVRPWR TFRLNECACG PYNADFDGDE MNLHVPQTEE ARAEAVTLMS
VKHNLATPKN GEPIIAATQD FITASYLLSS KDMFFDRRTF TYIVMHMMDG IVHLDLPAPA
ILAPKRLWTG KQVFSMLMRP NKSTPVKVNL DAKCREYVDP PPAPPGHRKR APDMCPNDGW
LVVRNSVVMC GRMDKSTVGS GKKDSIFYVI LRDYGPDEAV AAMNRLAKLC ARMLTNRGFS
IGVGDVFPNA ALTAAKNKLV EDAYIESDNF IKQFNENQLP KATGCSMEET LEAKISGVLS
KVRQNAGELC INSLSPNNAP LVMASSGSKG SNLNVAQMIA AVGQQIIGGS RVADGFQDRT
LPHFHKNTRH ALAKGFVRNS FYTGLVPTEF LFHAISGREG LVDTAVKTAE TGYMSRRLMK
SLEDLSTKYD DTVRTSGDGV VQFQFGGDKL DPVDMEGKAV PVHFERTFSH AENLTWNNAD
RALLPFEILA VCDSMLKKER DRYRRRGLLH GEPLRYDDTT DYGVDEHESG RNFLETIHEH
VRGLAHKFSD LRVAAGLESM LTTPNIQSFP LTNTEQKSLA ALISDVDQAR IKQLARIDVA
DGHRQNAKLL RIKSENHKLM YEDLLNLRPV LEGLDFQRPA KAKTVVEKQE FARLLELNDR
LDKLDLGYLS RMACEIELQE RQYVSKTASE RPAKVSEKTL RHFIGFCLEK YSKAHVEPGH
AVGAVGAQSI GEPGTQMTLK TFHFAGVAGM SITQGVPRIK EIINASKLIS TPVITCPLQN
SRSLEAAKIV RARIEKTYIE DVLRYVDDEW QPHRSFITLH INTETLESMH LGIKLSDIAD
AIAKQKKLKI MKADMQVFEQ DASIEITVRP LDADSSARRT TRTKTVTEAM ADLSVRISHL
RRVLPSVPIS GYPDANRAII QQSDKDSTNT VLVEGYGLRQ CINTEGVIGT KVTSNSVMEC
RDVLGIEAAR TTIAKEISLV MGDMGIDPRH MQLLADVMTY KGEILGITRF GLSKMRDSVL
QLASFEKTAD HLFDAASGMK TDPIEGVSEK IIMGETMSIG TGAFQVVRRL NLLDEHFATM
PTVFEDAWAH NQKERPTKRI RKRIL
//
