ID A9Q9S4_9EURO Unreviewed; 999 AA.
AC A9Q9S4;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:ABV69504.1};
OS Verrucaria muralis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Verrucaria.
OX NCBI_TaxID=429478 {ECO:0000313|EMBL:ABV69504.1};
RN [1] {ECO:0000313|EMBL:ABV69504.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AFTOL-ID 2265 {ECO:0000313|EMBL:ABV69504.1};
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; EF689805; ABV69504.1; -; 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..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABV69504.1"
FT NON_TER 999
FT /evidence="ECO:0000313|EMBL:ABV69504.1"
SQ SEQUENCE 999 AA; 111864 MW; 5A91F152E1B3B444 CRC64;
IKLAVPVYHY GFLGKVKKLL ETVCHNCGKI KAIDSEELRY AQTVRNRKNR FELIWRLSQK
QNICQADSPE DEDDPMGKER SGKIRHGGCG NAQPAIRRSG LELWAQYKPR KGDDEEEAVP
EKSQIWPAQA LQIFQHLTDE TLETLGLSLD FARPEWMILQ SLPVPPPPVR PSISVDGSGQ
GSRGEDDLTF KLGDIIRANQ NLIRINAEGA PDHIAKELQA LLQYHVATYM DNDIANLDKA
QHKSGRPIKS IRARLKGKEG RLRQNLMGKR VDFSARTVIT GDPNLSLDEV GVPRSIARTL
TYPETVTRFN ISRLKELVTR GPEMHPGARY IIRENNERID LRYHKDPAGI ALKVGWKVER
HIMDGDVILF NRQPXXXRVR VMPYSTFRLN LSVTTPYNAD FDGDEMNLHV PQSEESRAEL
AQLCMVPLNI VSPQRNGPLM GIVQDTLCGI YKICRRDVFL SREAVMNIML WVPDWDGVIP
QPAIFKPRPR WTGKQIISMV LPPALNLVRI DGKASQPPGE RFAPAGDSGL FVADGELMFG
LFNKKSVGTG SNGIIHTIFN EFGHETAMAF FNGAQTVVNY WLLHNGFSIG IGDTVPDVGT
VEKIKSEVDK KKAEVERITQ SAVAEDLEAL PGMNVRETFE SKVSAALNGA RDEAGTATEN
SLKDINNAIQ MARAGSKGST INISQMTAIV GQQSVEGKRI PFGFKYRTLP HFAKDDYSAA
SKGFVENSYL RGLTPTEFFF RAMAGREGLI DTAVKTAETG YIQRRLVKAL EEVTVKYDST
VRDSRGNIVQ FIYGEDGLDG AHIESQRVDV IAMSDNAFEK LFRVDLMEPK KLVWQDRLEQ
ASEIHGDVDV QKLFDEEYDQ LVEDRKFLRY VKKAATSGDE MMPLPMNVVR ILNQARTTFK
IQSGALSDLH PSYVIPKVKQ LLDRLIIVRG EDRISLEAQD NATLLIKAQL RSRLAFKRLV
MEYSLNRLAF DHVVGAIETR FIKATASPGE MVGVLAAQS
//
