ID A9Q9Q3_9EURO Unreviewed; 999 AA.
AC A9Q9Q3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:ABV69483.1};
OS Thelidium papulare.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Thelidium.
OX NCBI_TaxID=364727 {ECO:0000313|EMBL:ABV69483.1};
RN [1] {ECO:0000313|EMBL:ABV69483.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AFTOL-ID 2249 {ECO:0000313|EMBL:ABV69483.1};
RX PubMed=17981450; DOI=10.1016/j.mycres.2007.08.010;
RA Gueidan C., Roux C., Lutzoni F.;
RT "Using a multigene phylogenetic analysis to assess generic delineation and
RT character evolution in Verrucariaceae (Verrucariales, Ascomycota).";
RL Mycol. Res. 111:1145-1168(2007).
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; EF689784; ABV69483.1; -; 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; 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; 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 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 155..454
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 65..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABV69483.1"
FT NON_TER 999
FT /evidence="ECO:0000313|EMBL:ABV69483.1"
SQ SEQUENCE 999 AA; 111911 MW; C320031F419DA902 CRC64;
IKLAVPVYHY GFLGKVKKLL ETVCHNCGKI KAVDSEDLRY AVSVRDRKKR FDLIWRLSQK
QHVCQADSPE DEDDPNAKEK GGKLRHGGCG NAQPVIRKAG LELWAQYKPR KGDDEEETVP
EKSQIWPAQA LQVFQHLTDE TLETLGMNLD FARPEWMILQ SLPVPPPPVR PSISVDGSGQ
GQRGEDDLTF KLGDIIRANQ NLIRINTEGA PDHIAKELQA LLQYHVATYM DNDIANLDKA
QHKSGRPIKS IRARLKGKEG RLRQNLMGKR VDFSARTVIT GDPNLSLDEV GVPRSIARTL
TYPETVTPFN ISKLKNLIIR GPEHHPGARY IIRENNERID LRYHKDLKGI ALKVGWKVER
HIMDGDIILF NRQPXXXRVR VMPYSTFRLN LSVTTPYNAD FDGDEMNLHV PQSEESRAEL
AQLCMVPLNI VSPQRNGPLM GIVQDTLCGI YKICRRDVFL SREAVMNIML WVPDWDGVIP
QPAIFKPRPR WTGKQIISMV LPPALNLVRI DGKASQPPGE RFAPAGDSGL FVADGQLMFG
LFNKKSVGTG SNGVIHTIFN EFGHETAMAF FNGAQTVVNY WLLHNGFSIG IGDTVPDFGT
VEKIKFEVDK KKAEVERITQ SAVAEDLEAL PGMNVRETFE SKVSAALNGA RDEAGTATEN
SLKDINNAIQ MARAGSKGST ISISQMTAIV GQQSVEGKRI PFGFKYRTLP HFAKDDYSAA
SKGFVENSYL RGLTPTEFFF HAMAGREGLI DTAVKTAETG YIQRRLVKAL EEVTVKYDST
VRDSRGNIVQ FVYGEDGLDG AHIESQRVDV IAMSDHAFEK LFRVDLMEPK KLVWQDRLEQ
ASEIHGDVDV QKLFDEEYEQ LTEDRNFLRS IKKAATSGDE MMPLPMNVVR ILNQARTTFK
IQSGALSDLH PSYVIPKIKQ LLDRLIIVRG EDRISLEAQE NATLLIKAQL RSRLAFKRLV
MEYSLNRLAF DHVVGAIETR FIKAIASPGE MVGVLAAQS
//
