ID A5H2E2_9LECA Unreviewed; 984 AA.
AC A5H2E2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
DE Flags: Fragment;
GN Name=RPB1 {ECO:0000313|EMBL:ABM81486.1};
OS Myelochroa aurulenta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Parmeliaceae;
OC Myelochroa.
OX NCBI_TaxID=358640 {ECO:0000313|EMBL:ABM81486.1};
RN [1] {ECO:0000313|EMBL:ABM81486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AFTOL-ID 206 {ECO:0000313|EMBL:ABM81486.1};
RX PubMed=17486983; DOI=10.3852/mycologia.98.6.1088;
RA Miadlikowska J., Kauff F., Hofstetter V., Fraker E., Grube M.,
RA Hafellner J., Reeb V., Hodkinson B.P., Kukwa M., Lucking R., Hestmark G.,
RA Otalora M.G., Rauhut A., Budel B., Scheidegger C., Timdal E., Stenroos S.,
RA Brodo I., Perlmutter G.B., Ertz D., Diederich P., Lendemer J.C., May P.,
RA Schoch C.L., Arnold A.E., Gueidan C., Tripp E., Yahr R., Robertson C.,
RA Lutzoni F.;
RT "New insights into classification and evolution of the Lecanoromycetes
RT (Pezizomycotina, Ascomycota) from phylogenetic analyses of three ribosomal
RT RNA- and two protein-coding genes.";
RL Mycologia 98:1088-1103(2006).
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|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; DQ973049; ABM81486.1; -; Genomic_DNA.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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; cd02733; RNAP_II_RPB1_N; 1.
DR Gene3D; 1.10.132.30; -; 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; IPR007075; RNA_pol_Rpb1_6.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 147..452
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 64..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..871
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 64..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABM81486.1"
FT NON_TER 984
FT /evidence="ECO:0000313|EMBL:ABM81486.1"
SQ SEQUENCE 984 AA; 110509 MW; CDAC824DF427F837 CRC64;
SXRKXKNCWK QSAIIAARYX SMKLSNPAFA DAIRRRDPKK RFDLVWRLCK PKMICETTMA
LDDDAPSDKT KETKHDHGGC GNMQPEVRRE GLRLTGTWKA QKGDEENEGQ QPEKKPITPQ
MALNIFRHIS TEDIKKIGLS NDYARPEWMI ITVLPVPPPP VRPSISVDGG NGPRGEDDLT
YKLGDIIRAN GNVRRCETEG SPAHVVNEFE QLLQFHVATY MDNDIAGQPQ ALQKSGRPVK
SIRARLKGKE GRLRGNLMGK RVDFSARTVI TGDPNLSLDE VGVPRSIART LTYPETVTPY
NIQKLHQLVK NGPNEHPGAK YVIRDTGERI DLRHHKRAGE ISLQYGWKVE RHIVDGDYII
FNRQPSLALE SMMGHRVRVM PYSTFRLNLS VTSPYNADFD GDEMNLHVPQ SEETRAEINQ
LCMVPLNIVS PQRNGPLMGI VQDTLCGIYK MCRRDVFLIK EQVMNILLWV PDWDGVIPQP
AIVKPLAMWT GKQILSLVIP TGLNLLRGTE EGFSPLNDDG LLISGGELMY GLLNKKTVGA
SGGGVIHIVF NEKGPEAAMN FFNGAQTVVN YWLLHNGFSI GIGDTIPDRH TIQQIENAVN
NQKAEVMEIT RSATENELES LPGMNVRETF ESKVSKALNK ARDDAGTVTE KSLKDLNNAT
QMARSGSKGS TINISQMTAV VGQQSVEGKR IPFGFKYRTL PHFTKDDYSP ESRGFVENSY
LRGLTPTEFF FHAMAGREGL IDTAVKTAET GYIQRRLVKA LEDVMAKYDG TVRNSLGDVV
QFVYGEDGLD GVHIEQQRVD IIACSTKQFE RKFRIDLMDS KPETSISPEL LEQANEMIGD
VETQKHLDNE YRQLEKDRAE LRKNRQDDSE NLQLPLNIIR ILDTAKTTFK IKNGARSNLH
PAEVIPQVQD LLDRLVVVRG TDELSQEAQH NATLLFKIQL RSRLAFKRLV MENSLNKLAF
QHVLGEIESR FCRAAVNPGE MVGV
//
