ID A5H286_9LECA Unreviewed; 996 AA.
AC A5H286;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 50.
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:ABL85584.1};
OS Vulpicida pinastri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Parmeliaceae;
OC Vulpicida.
OX NCBI_TaxID=78078 {ECO:0000313|EMBL:ABL85584.1};
RN [1] {ECO:0000313|EMBL:ABL85584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AFTOL-ID 198 {ECO:0000313|EMBL:ABL85584.1};
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; DQ912366; ABL85584.1; -; 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 159..464
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 76..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 856..883
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 76..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL85584.1"
FT NON_TER 996
FT /evidence="ECO:0000313|EMBL:ABL85584.1"
SQ SEQUENCE 996 AA; 111541 MW; 5F3E2779549A2DB7 CRC64;
ILNSQCLFIM LVLXRKSRNC WKQSATIAAR FXXMKLSNPA FADAMRRRDP KKRFDSVWRL
CKPKMICETT MALDDDAPSD KAKEPKHDHG GCGNIQPEVR REGLKLTGTW KAQKGDEENE
GQQPEKKPIT PQMALNIFRH ISADDIKRMG LSNDYARPEW MIITVLPVPP PPVRPSISVD
GGNGPRGEDD LTYKLGDIIR ANGNVRRCET EGSPAHVVNE FEQLLQFHVA TYMDNDIAGQ
PQALQKSGRP VKSIRARLKG KEGRLRGNLM GKRVDFSART VITGDPNLSL DEVGVPRSIA
RTLTYPETVT PYNIQKLHQL VKNGPNEHPG AKYVIRDTGE RIDLRHHKRA GEISLQYGWK
VERHIVDGDY IIFXXXXXXH KESMMGHSVR VMPYSTFRLN LSVTSPYNAD FDGDEMNLHV
PQSEETRAEI NQLCMVPLNI VSPQRNGPLM GIVQDTLCGI YKMCRRDVFL TKEQVMNILL
WVPDWDGVIP QPAIVKPLAM WTGKQILSLV IPTGLNLLRG SEEGFSPLND DGLLISGGEL
MYGLLNKKVV GASGGGVIHI VFNEKGPEAA MTFFNGAQTV VNYWLLHNGF SIGIGDTIPD
RDTIAQIERA VIAQKEEVTA ITASATANEL ESLPGMNVRE TFESKVSKAL NKARDDAGTV
TEKSLKDLNN ATQMARSGSK GSTINISQMT AVVGQQSVEG KRIPFGFKYR TLPHFTKDDY
SPESRGFVEN SYLRGLTPTE FFFHAMAGRE GLIDTAVKTA ETGYIQRRLV KALEDVMAKY
DGTVRNSLGD IVQFVYGEDG LDGVHIEQQR VDIIACSTKQ FERKFRVDLM DSKPETSISP
EFLELANEMI GDVETQKHLD DEYRQLEKDR AELRKNRQDD TENLQLPLNV IRILDTAKTT
FKIKNGARSN LHPAEVIPQV HDLLDRLVVV RGTDKLSEEA QHNATLLFKI QLRSRLAFKR
LVMENSLNKL AFQHVLGQIE SRFCRAAVNP GEMVGV
//
