ID G0RMT8_HYPJQ Unreviewed; 1755 AA.
AC G0RMT8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=TRIREDRAFT_79315 {ECO:0000313|EMBL:EGR47538.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR47538.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR47538.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(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 -!- 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; GL985068; EGR47538.1; -; Genomic_DNA.
DR RefSeq; XP_006966645.1; XM_006966583.1.
DR STRING; 431241.G0RMT8; -.
DR EnsemblFungi; EGR47538; EGR47538; TRIREDRAFT_79315.
DR GeneID; 18489007; -.
DR KEGG; tre:TRIREDRAFT_79315; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_79315; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000008984};
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 243..549
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1558..1755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1755 AA; 193360 MW; 90E0DBAF6E944E58 CRC64;
MANLYFTHSS APLKTVQEIQ FGLMSPEEIK SMSVAHILYP ETMEEGGTKP RDGGLNDPLL
GSIDRQFKCK TCTQAMGECP GHFGHIELAK PVYHPGFIKK VKKILEIVCH NCSKVLADES
DPEFVAAINT RDAKLRFKRV WAVCKKKRRC ENDDRSEKNK DEEFAPGMKP AVVESHGGCG
NVQPQVRQVA LQLKAAFEVV QEDGPKRKET APITPEMAHS ILRRISEKDL RNMGLNSDYA
RPEWMIITVL PVPPPPVRPS ISMDGTGTGM RNEDDLTYKL GDIIRANGNV KQAIREGSPQ
HIARDFEELL QYHVATYMDN DIAGQPRALQ KSGRPVKAIR ARLKGKEGRL RGNLMGKRVD
FSARTVITGD ANLSLHEVGV PRSIARTLTY PETVTPYNIG KLHQLVENGP NEHPGAKYVI
RSDGTRIDLR HHRRAAQISL EYGWKVERHL MDGDYIIFNR QPSLHKESMM GHRVRVMPYS
TFRLNLSVTS PYNADFDGDE MNLHVPQSEE TRAEVKELCL VPNNIVSPQK NGPLMGIVQD
SLAGAYKLCR RDTFLDKNQV MNLMLWVPNW DGVIPQPAIL KPRPRWTGKQ IISMVIPKEI
SLHAPEDKSD SPLKDAGLLI QAGELMYGLM KKKNIGSASG GVIHLCYNEL GPEGAMAFLN
GVQQVVTYWL LQNGHSIGIG DTIPDKQTIE KVQVHIDTQK AEVARLTAMA TNNELEALPG
MNVRATFENK VSMALNMARD QAGTTTQKSL KDSNNAVTMA ESGSKGSSIN ISQMTALVGQ
QIVEGKRIPF GFKYRTLPHF TKDDYSPEAR GFVENSYLRG LTPTEFFFHA MAGREGLIDT
AVKTAETGYI QRRLVKALED LNAQYDGTVR NSLGDIIQFL YGEDGLDAMC IEKQKLGILK
MSDEAFEKKY RLDLANPPDW FRKDYEYGNE LTGDKASMAL LDEEWDQLLA DRREVREINR
SKMGEEMMQL PLNIGRMIET AKRVFNVKAN DRSNLRPSDV IPVVRNVINK LKIVRGEDQI
SKEADTSATI LFKALLRSRL AFKEVVKEHR LNKLAFEHVL GELQNRWDRS FVNPGEMVGV
LAAQSIGEPA TQMTLNTFHF AGVSSKNVTL GVPRLKEILN LAKNIKTPSM AVYLDTPLAK
QEQAKKLRSL VEYTNLRSIT SVTEIYYDPD VQSTTIPEDL DMVESYFLIP DDSQDTIDQQ
SRWLLRITLD RQKLLDKEIK IDDVAQRIKE EYPNDLAVIF SDNNADEQVI RIRTIRQDEK
DEDGEKKIED DVMLKRLEAH LLDTLTLRGV PGVERAFLTK GTRLVEAADG SELALKDDPR
CTQWYLDTSG SALREVLAVP GVDPTRTYTN DLWQIIEVFG IEGTRAALVK ELTAVLAFDG
SYVNHRHIAL LCDVMTYRGS ISAVTRHGIN RADTGALMRC SFEETVEILL EAAATGELDD
CRGISENVML GQMAPMGTGN FDVYLDPKML ETVISDNSRM GLMPGMPVKE GDVEGAATPY
DTGSPMGDSG YLSLNSPAAG NFSPIQGAGS ETPAGFGTEY GGGGFGGIGS MSPYSMRGAT
SPFSTSPTSP FSSGMGGYSP TSPNAGYSPT SPMIDGGIGR YATSPSFSPS SPSFSPTSPM
LRPTSPASPN YSPTSPSYSP ASPSSPRHYS PTSPAQFNSP TSPSYSPASP NYSPASPNLH
GVGATSPSYS PASPSWSPTS PEAYSPTSPS FSKSPGSQQS PTSPSYSPTS PSFSPRTPGP
GASGNQYSPN SPAND
//
