ID W8PDZ6_9PEZI Unreviewed; 1754 AA.
AC W8PDZ6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=RPB1 {ECO:0000313|EMBL:AHL18109.1};
OS Mycothermus thermophilus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Mycothermus.
OX NCBI_TaxID=85995 {ECO:0000313|EMBL:AHL18109.1};
RN [1] {ECO:0000313|EMBL:AHL18109.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 621.91 {ECO:0000313|EMBL:AHL18109.1}, and CBS 623.91
RC {ECO:0000313|EMBL:AHL18111.1};
RA Tsang A.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; KF958007; AHL18109.1; -; Genomic_DNA.
DR EMBL; KF958009; AHL18111.1; -; Genomic_DNA.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.1360.140; -; 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; 4.10.860.120; RNA polymerase II, clamp domain; 2.
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; IPR000684; RNA_pol_II_repeat_euk.
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; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
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 Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 11.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 244..550
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 151..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 692..719
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 163..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1754 AA; 193986 MW; 7E70EE21321F5B47 CRC64;
MANLIFAHSS APLRTIQEIQ FGLLSPEEIK AMSVCHILYP ETMDETRTKP RDGGLNDPLL
GSVDRQFKCK TCGENMTECP GHFGHIELAR PVYHPGFIRR TKKILEVVCH NCSKVLADRS
DPQYAAAMRI RDPKVRFKRV WEICKTKKRC DNDPPKQAED GEFNPNGDTT NVPTQGHGGC
GNIQPTIRQQ ALTLWAQWER KDDEGVKVKE KKMITPEMAL NIFRRMTDEE MIDIGLNISQ
ARPEWMIITV LPVPPPPVRP SISMDGTGTG MRNEDDLTYK LGDIIRANGN VRQAIAEGSP
QHIISDFESL LQYHVATYMD NDIAGQPQAL QKSGRPVKAI RARLKGKEGR LRGNLMGKRV
DFSARTVITG DANISLDEVG VPRSIARTLT YPETVTPYNI AKLTKLVQNG PNEHPGARFV
VRSDGTRLDL RHYRRAGAVQ LEYGWKVERH LMDGDYIIFN RQPSLHKESM MGHRVKVMPY
STFRLNLSVT SPYNADFDGD EMNLHVPQTE ETRAEVKELC MVPLNIVSPQ RNGPLMGIVQ
DTLAGVYKLC RRDVFLTKEE VMNLMLWVPD WDGVIPLPAI HKPRPRWTGK QIISMIIPKI
INIHMGSESP DKDHPFKDDG LLIQQGAVIY GLLSKKSVGA AGGGIVHLCY NELGPQGAMD
FLNGCQRVVN YWLLHNGHSI GIGDTIPDPK TIELIEKHIN EEKEEVRKLT LQATNNQLEP
LPGMNIRETF ENKVSAALNR ARDKAGTSAE KSLKDLNNAV TMARSGSKGS SINISQMSAL
VGQQIVEGKR IPFGFKYRTL PHFTKDDYSP EARGFVENSY LRGLTPTEFF FHAMAGREGL
IDTAVKTAET GYIQRRLVKA LEDAEARYDG TVRNSLGDII QFIYGEDGLD GIAIEKQRVD
HMNLSNKAFE KRFRLDVMDP ASSGPALDAL EYGREMASDP AVQELLDQEY EQLLADRKLL
REVNKRKGAE DNMQLPLNVA RIIETAKKLF KVDDSHRSDL TPSDVIPAVR ALLDRMVVVR
GDDPISKEAD YNSTILFKCQ LRSRLAYKRL AVEQRINKLA FEHILGELEN RWQRAMVAPG
EMVGVLAAQS IGEPATQMTL NTFHFAGVSS KNVTLGVPRL KEILNVAKDI KTPSMVVYLD
KQNATQEDAK RMRNVVEHTS LRSVTAMTEI YYDPDITSTT IPEDYDMVES YFLIPDASDQ
ESIENQSRWL LRITLDRQKM LDKGLRVEDV AQVIKEEYRR DVAVIFSDNN AEEMVIRIRV
IRQADDKDED GNQIIEDDVM LKRLEKHLLD SCTLRGVKGI ERAFLNKGTK VVERADGSQV
QIKDAPDCTE WYLDTQGTAL REVLTIEGVD ARRTTTNDLY QIVDMLGIEA ARAALLSELT
QVLAFDGSYV NHRHLALLVD VMTYRGSIAA VTRHGINRAD TGALMRCSFE ETVEILLEAA
AVGELDDCRG ISENVMLGQM APMGTGHFDV LLDPKMLETV ISDNSRMGLM PGMTIKGAQL
EGAATPYDTG SPLADEGFMG GYSPTPGNFS PIQGGGSESP SGFGTEYGGG FGSSTVNPYA
TSPRATSPFS TSPTSPFNYG GYSPSSPAGY SPTSPLIGAG RYASSPQFSP SSPSFSPTSP
MLRPGSPTSP NYSPTSPSYS PASPAAARHY SPTSPAQFNS PTSPSYSPTS PSYSPASPAF
QATSPSYSPA SPTWSPTSPN AYSPTSPAFH RSPGQQMSPT SPGYSPTSPS FSPRTPGRQP
GSGDQYSPTS PQND
//
