ID   A9Q9N4_9EURO            Unreviewed;       989 AA.
AC   A9Q9N4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 46.
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:ABV69464.1};
OS   Clavascidium lacinulatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Clavascidium.
OX   NCBI_TaxID=2591477 {ECO:0000313|EMBL:ABV69464.1};
RN   [1] {ECO:0000313|EMBL:ABV69464.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AFTOL-ID 2287 {ECO:0000313|EMBL:ABV69464.1};
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; EF689765; ABV69464.1; -; 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   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABV69464.1"
FT   NON_TER         989
FT                   /evidence="ECO:0000313|EMBL:ABV69464.1"
SQ   SEQUENCE   989 AA;  110910 MW;  203AA7A1588703F6 CRC64;
     IKLAVPVYHY GFLGKVKKLL ETVCHNCGKI KALDSEELRY ALSVRDRKKR FELIWRLSQK
     QNVCQADAPE DEDDPIVKEK GGKIRHGGCG NAQPAIRKTG LELWAQYKPR KGDDEEETVP
     EKSQIWPAQA LQVFQHLTDE TLETLGMNLD FARPEWMILQ SLPVPPPPVR PSISVDGSGQ
     GQRGEDDLTF KLGDIIRANQ NLIRINAEGA PDHIAKELQA LLQYHVATYM DNDIANLDKA
     QHKSGRPIKS IRARLKGKEG RLRQNLMGKR VDFSARTVIT GDPNLSLDEV GVPRSIARTL
     TYPETVTRFN ISRLKQFVTN GPEMHPGARY IIREHNERID LRYHKDTSQI ALKVGWKVER
     HIMDGDVILF NRQPXXXRVR VMPYSTFRLN LSVTTPYNAD FDGDEMNLHV PQSEESRAEL
     SQLCMVPLNI VSPQRNGPLM GIVQDTLCGI YKICRRDVFL SREEVMNIML WVPDWDGVIP
     QPAIVKPRPR WTGKQMVSMV LPPALNLVRI DGKASLPPGE RFAPAGDSGL FVADGQLMFG
     LFNKKSVGTG SNGVIHTIFN EFGHETAMAF FNGAQTVINY WLLHNGFSIG IGDTVPDVGT
     VEKIKSEVDK KKAEVERITQ SAVAEDLEAL PGMNVRETFE SKVSAALNGA RDEAGSATEN
     SLKDSNNAIQ MARAGSKGST INISQMTAIV GQQSVEGKRI PFGFKYRTLP HFAKDDYSAA
     SKGFVENSYL RGLTPTEFFF HAMAGREGLI DTAVKTAETG YIQRRLVKAL EEVTVKYDGT
     VRDSRGNIVQ FIYGEDGLDG AHIENQRVDV IAMSDDAFEK QFRVDLMEPK KLVRHDRLEQ
     ASEIHGDVDV QKLFDEEYEQ LLEDRKFLRY IKKAATSADE MMPLPMNVVR ILNQARTTFK
     IQSGGPSDLH PSYVIPKVKQ LLERLTIVRG DDSISLEAQE NATLLIKAQL RSRLAFKRLV
     MEYSLNRLAF DHVVGAIETR FIKAIASPG
//