ID E9EC10_METAQ Unreviewed; 1746 AA.
AC E9EC10;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=MAC_07408 {ECO:0000313|EMBL:EFY86546.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY86546.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY86546.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698544; EFY86546.1; -; Genomic_DNA.
DR RefSeq; XP_007813748.1; XM_007815557.1.
DR STRING; 655827.E9EC10; -.
DR GeneID; 19251719; -.
DR KEGG; maw:MAC_07408; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; E9EC10; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000002499; 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; 3.
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:UP000002499};
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 241..547
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 736..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1746 AA; 192127 MW; 14AF39325C08B646 CRC64;
MANYHPPFSS APLKTVEEIQ FGLMSPEEIK NMSVCHILYP ETMDESRTKP RDGGLNDPLL
GSIDRGFKCK TCTQSMSDCP GHFGHIELAK PVYHPGFIKK VKKILEIVCH NCSKVLADTS
DSEFVTAINT RDAKLRFNRV WAVCKKKRRC ENEDRNEKND DEFAPGMKPV AHNHGGCGNV
QPQVRQAALQ LKAAFDVAQE DGPKRRETVP ITPEMAHGIL RRISEEDLRH MGLNSDYARP
EWMILTVLPV PPPPVRPSIS MDGTGTGMRN EDDLTYKLGD IIRANGNVKQ AIREGSPQHI
ARDFEELLQY HVATYMDNDI AGQPRALQKS GRPVKAIRAR LKGKEGRLRG NLMGKRVDFS
ARTVITGDAN LSLHEVGVPR SIARTLTYPE TVTPYNIGKL HQLVENGPNE HPGAKYVIRA
DGTRIDLRHH RRAAQISLEY GWKVERHLMD GDYIIFNRQP SLHKESMMGH QVRVMPYSTF
RLNLSVTSPY NADFDGDEMN LHVPQTEETR AEVKELCLVP NNIVSPQKNG PLMGIVQDSL
AGVYKLCRRD TFIDKEMVMN MMLWVPNWDG VIPQPAILKP RPRWTGKQLI SMVIPQEISL
HAPEGDSDIP PKDTGLLIQS GELLYGLLKK KNVGAAAGGI IHLCYNELGP EGAMAFLNGV
QQVVTYWLLN TGHSIGIGDT IPDKQTIEKI QVHIDTQKAE VAKLTAQATA NELEALPGMN
VRATFENKVS MALNSARDQA GTTTQKSLKD SNNAVTMSES GSKGSSINIS QMTALVGQQI
VEGKRIPFGF KYRTLPHFTK DDYSPEARGF VENSYLRGLT PSEFFFHAMA GREGLIDTAV
KTAETGYIQR RLVKALEDLS ARYDGTVRNS LGDIVQFLYG EDGLDAMCIE KQKLGILKMS
DAAFEKKYRL DLANPPDWFK KDYEYGNELA GDKESMDLLD SEWETLLSDR QTVRLINKSK
MGEEMMQLPL NIGRMIETAK RVFNVRATDR SNLRPADVIP RIQNLLSELK IVRGSDPISA
EADMNATILF KALVRSRLAF KEIVKVHRLN KLAFDHVLGE LQNRWDRSFV SPGEMVGVLA
AQSIGEPATQ MTLNTFHFAG VSSKNVTLGV PRLKEILNLA KDIKTPSMAV YLNTKLGTQE
QAKKLRSMVE YTNLRSITSV TEIYYDPDIQ GTTIAEDMDM VESYFLIPDD GQDNTDQQSR
WLLRITLDRQ KLLDKEIRID DVAQRIKEEY PNDLAVIFSD NNADEQVIRI RTVRQSEEKD
EDGEKKIEDD VMLKRLEAHL LDTLTLRGVP GIERAFLTKG TRLTVGEDGS ELAIKDDPRC
TQWYLDTSGS ALRDVLAVDG VDASRTYTND LWQIVEVFGI EAARSALVKE LTNVLAFDGS
YVNHRHIALL VDVMTYRGSI SAVTRHGINR ADTGALMRCS FEETVEILLE AAATGELDDC
RGISENVMLG QLAPMGTGNF DVLLDPKMLE TVISDNSRMG LMPGMPVKDG EAEGAATPYD
TGSPMSNDSG YMSMNSPAAG NFSPIQGAGS ETPAGFGTEY GGGGFGNVGS MSPYSRGATS
PFSTSPTSPF SSGMVGYSPS SPNAGYSPTS PLLDGGAGRY ATSPSFSPSS PSFSPTSPML
RPTSPASPNY SPTSPSYSPT SPTSPRHYSP TSPAQFNSPT SPSYSPASPN YSPASPNLHG
AAGATSPSYS PASPSWSPTS PEAYSPTSPS FQRSPGNQQS PTSPSYSPTS PAFSPRTPGP
GNSGNQ
//
