ID C3U065_9EURO Unreviewed; 983 AA.
AC C3U065;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:ACO89397.1};
OS Capronia parasitica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=43224 {ECO:0000313|EMBL:ACO89397.1};
RN [1] {ECO:0000313|EMBL:ACO89397.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 123.88 {ECO:0000313|EMBL:ACO89397.1};
RX PubMed=19287533;
RA Gueidan C., Villasenor C.R., de Hoog G.S., Gorbushina A.A.,
RA Untereiner W.A., Lutzoni F.;
RT "A rock-inhabiting ancestor for mutualistic and pathogen-rich fungal
RT lineages.";
RL Stud. Mycol. 61:111-119(2008).
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; FJ358357; ACO89397.1; -; 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 143..445
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 55..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACO89397.1"
FT NON_TER 983
FT /evidence="ECO:0000313|EMBL:ACO89397.1"
SQ SEQUENCE 983 AA; 109638 MW; 04D4248D07D8577B CRC64;
GFMTKVKKIL ETVCHNCGKI KALDTPEFQQ AISTRDRKRR FDAVWRLSKP RNVCEADPPE
EPDQLLKGPP LPKHGGCGNA QPDIRRTGLS LWASWKPRKG DDDEDTTPEK KRIFPQDALN
TFRTLTDETL EMMGLSLDYA RPEWMILTAL PVPPPPVRPS ISVDGSGQGS RGEDDLTFKL
GDIIRANQAV LRTEVDGTPD HIKVDLCDLL QYHIATYMDN EIAGLDKAQH KSGRPIKSIR
ARLKGKEGRL RQNLMGKRVD FSARTVITGD PNLSLDEVGV PRSIARTLTY PETVTAFNIE
KLKRLVANGP SEHPGARYVI RDTGERIDLR HHKRAGEMSL QYGWKVERHI QDGXXXXXXX
XXXXXXXXXX XXXXYSTLRL NLSVTTPYNA DFDGDEMNLH VPQSEESRAE LANLCMVPLN
IVSPQRNGPL MGIVQDTLCG IYKICRRDVF LSREHVMNIL LWVPEWDGVI PQPAIIKPTP
RWTGKQVISM ILPGALNLER LDAKGEDPFV PSNDTGLMVL EGNLMFGMFN KKFVGTSAGG
IIHTIFNEFG HEAAMAFFNG AQCVVNYWLL HNGFSIGIGD TVPDPDTVIK IQAAVDTKKA
EVDEITVRAY KEDLEPSPGM NVRQTFESKV MNSLNQARDQ AGTATEDSLK DLNNGITMAR
AGSKGSTINI AQMTAIVGQQ AVEGKRIPFG FKYRTLPHFA KDDYSAPSRG FVENSYLRGL
TPTEFFFHAM AGREGLIDTA VKTAETGYIQ RRLVKALEEV TVKYDSTVRD SRGNVVQFIY
GEDGLDGAHI ENQKVDIITM SDKAFNNRYA VDIMSGDVSM WRGKLLQARE IQGDTELQEM
FDEVLEKLRD ARIFLRKMGK GTEDSMQLPL NIGRIIDQSQ KNFKIRRGDR TDLDARHVLT
SVDQLLDRLI VVRGEDAISK EAQSNATLLL NAQLRSRLAY KRLVLEHGLN RLAFDNIIGG
IESRFVAAGA NPGEMVGVLA AQS
//
