ID U4LUT0_PYROM Unreviewed; 1453 AA.
AC U4LUT0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=PCON_11993 {ECO:0000313|EMBL:CCX31916.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX31916.1};
RN [1] {ECO:0000313|EMBL:CCX31916.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX31916.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX31916.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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; HF935702; CCX31916.1; -; Genomic_DNA.
DR STRING; 1076935.U4LUT0; -.
DR eggNOG; KOG0261; Eukaryota.
DR OMA; AVCPPYN; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000018144; 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 Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 252..555
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 1453 AA; 162132 MW; D58166FFC618A34A CRC64;
MKSQVIDNVP KKIGEVQFGI MSPQDVVKQG VVEVATRELY ELEGGRSLKK NGALDARMGT
SAKNGICETC GEGLQNCNGH FGHVKLALPA FHIGYFKAIV TMLQNICKDC SRVLLDDNQG
RQYLKMLRTP NMDNLRRMGI CKKINEQCKK ARSCPHCGAI NGVVKKLGAL KIIHDKWRAF
NSSTSAKKIP PASKTEFDNS FTEAKKTNPD LDKHVKKAMD DLNPLKVLNL FKQVTAVDCE
LLGMNPEKGR PEMFIWQYVP APPVCIRPSV QQDSASNEDD LTVKLTEIIF MSSLIRAGLQ
QGKGIQSLME QWDYMQAQIA MYIDSSQPSI TRNYTELKPI RGFCQRLKGK QGRFRGNLSG
KRVDFSGRTV ISPDPNLSIE QVAVPILVAK NLTYPEKVNR YNIKKLQKLV ENGTEVWPGA
NYVIKKGTDF KLFLKFGDRK RTAENLQFGD VVERHLEDND VVLFNRQPSL HKLSILSHYA
KIRPWKTFRL NECVCNPYNA DFDGDEMNLH VPQTEEARTE AIQLMGVKNN LCTPRNGEPI
IAAIQDFITA AYLLSSKDVF YDRKTFGHIC MYMVDGNEQM DIPPPAIIKP QALWTGKQVF
NLMMRPNKKS PVLVNLDAKC RDFKPGSIAP GQAPDMCSQD GFLVIRGSEV MCGLMDKSTV
GSGKKDSVFY VILRDYGPDQ AVLAMNRLAK LCARWLANKG FSIGINDVLP GSVLRKEKDL
MVEDAYKQCD DLILQYKEGK LEKAAGCDEE TTLENKVQGI LSNVRDRVGD ICMRELSKYN
SPLIMASSGS KGSKINVSQM VACVGQQVIA GKRVPDGFDD RSLPHFAKNS KQPPSKGFVR
NSFFSGLTPT EFLFHAISGR EGLVDTAVKT AETGYMSRRL MKSLEDLSAN YDETVRTSSS
GIVQFRYGGD SLDPVDMEGD AQPVNFKRTY YHSENITYDN DAPGLLPYEI MELCDKVIRP
LEQKTTRKDL LGNIITDDQL DKLTGRDALM ALDENESLRG FYNSIRSYVG GKAQQLADLR
EKFGLPRQDE TPEPALRGKD IDSFYPAASV KAVRQVLKIS QRCMEEFLSQ CLTKYERAKI
EPGSAVGAVG AQSIGEPGTQ MTLKTFHFAG VASMNVTLGV PRIKEIINAS KIISTPIITC
KLVTKDDERA ARVVKGRMEK TYLSDIIHYV EDVCAPDSSY VSVRIDWKTI EALQLEIGTN
EITQALVKAK LKILPQDIRI SGNKVHITVR ELPAKERTSK EDGDIYMRVQ ALKRAIPGVI
VNGYPNCVRA VVKKNEKTGD NELLVEGYGL RQCMNTDGVI GTQTTSNHIM EMKEVLGIEA
ARGSIIGEVS YTMREHGMDI DPRHMQLLGD VMTYKGEVLG ITRFGLSKMR DSVLQLASFE
KTTDHLFDAA FYMKTDAVEG VSECIILGQS MSIGTGAFGV VRNLMVSEED LKPKQMMFED
KLKRIYKKGR AGK
//