ID A9Q9T0_9EURO Unreviewed; 974 AA.
AC A9Q9T0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:ABV69510.1};
OS Verrucaria sp. AFTOL 2268.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Verrucaria.
OX NCBI_TaxID=469205 {ECO:0000313|EMBL:ABV69510.1};
RN [1] {ECO:0000313|EMBL:ABV69510.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AFTOL-ID 2268 {ECO:0000313|EMBL:ABV69510.1};
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; EF689811; ABV69510.1; -; 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; -; 2.
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; 2.
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 146..445
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 57..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABV69510.1"
FT NON_TER 974
FT /evidence="ECO:0000313|EMBL:ABV69510.1"
SQ SEQUENCE 974 AA; 109383 MW; E0A19E76FD334640 CRC64;
YGFLGKVKKI LETVCHNCGE VKAVDSEELR YALSVRDRKK RFELIWRLSQ KQNVCQADAP
DDDENPIPKE KAGKIRHGGC GNAQPAIRKT GLELWAQYKP RKGDDEEEAV PEKSQIWPAQ
ALQVFQHLSD ETLEMLGLSL DFARPEWMIL QSLPVPPPPV RPSISVDGSG QGQRGEDDLT
FKLGDIIRAN QNLIRINAEG APDHIAKELQ ALLQYHVATY MDNDIANLDK AQHKSGRPIK
SIRARLKGKE GRLRQNLMGK RVDFSARTVI TGDPNLSLDE VGVPRSIART LTYPETATRF
NQERLKQFVT NGPEQHPGAR YIIREQGERI DLRFHKNTSE IVLKTGWKVE RHIMDGXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXTPYNX DFDGDEMNLH VPQSEESRAE LAQLCMVPLN
IVSPQRNGPL MGIVQDTLCG IYKICRRDVF LSRDEVMNIM LWVPDWDGVI PQPAIFKPRP
RWTGKQMISM VLPPALNLVR IDGKPSQPPV ERFAPAGDSG LFVADGQLMF GLFNKKSVGT
GSNGIIHTIF NEFGHETAMA FFNGAQTVVN YWLLHNSFSI GIGDTVPDVG TVEKIKLEVD
KKKAEVERIT QSAVAEDLEA LPGMNVRETF ESKVSAALNG ARDEAGTATE NSLKDINNAI
QMARAGSKGS TINISQMTAI VGQQSVEGKR IPFGFKYRTL PHFAKDDYSA ASKGFVENSY
LRGLTPTEFF FHAMAGREGL IDTAVKTAET GYIQRRLVKA LEEVTVKYDS TVRDSRGNIV
QFIYGEDGLD GAHIESQRVD IIAMSDNAFE KQFRVDLMEP KKVVWQDRLE QASEIHGDVD
VQKMFDEEYE QLVEGRRFLR SIKKAATTSD EMMPLPMNIV RILNQARTTF KIQSGTPSDL
HPSYVIPKVK QLLDRLTIVR GEDRISLEAQ ENATLLIKAQ LRSRLAFKRL VMEYSLNRLA
FDHVVGAVET RFIK
//
