ID A0A0B2WTL8_METAS Unreviewed; 1755 AA.
AC A0A0B2WTL8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=MAM_05363 {ECO:0000313|EMBL:KHN96807.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN96807.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHN96807.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN96807.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN96807.1}.
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DR EMBL; AZHE01000013; KHN96807.1; -; Genomic_DNA.
DR STRING; 1081103.A0A0B2WTL8; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000030816; 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:UP000030816};
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..1755
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..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1755 AA; 192915 MW; 8C33D143D1C9A160 CRC64;
MANYHPPFSS APLKTVEEIQ FGLMSPEEIK NMSVCHILYP ETVDESRTKP RDGGLNDPLL
GSIDRGFKCK TCTQSMSDCP GHFGHIELAK PVYHPGFIKK VKKILEIVCH NCSKVLADTS
DPEFVTAINT RDAKLRFNRV WAVCKKKRRC ENEDRNEKND DEFAPGMKPA 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 LKDTGLLIQS GELLYGLLKK KNVGAAAGGI IHLCYNELGP EGAMAFLNGV
QQVVTYWLLN TGHSIGIGDT VPDKQTIEKI QVHIDTQKAE VAKLTAQATA NELEALPGMN
VRATFENKVS MALNSARDQA GTTTQKSLKD SNNAVTMSES GSKGSSINIS QMTALVGQQI
VEGKRIPFGF KYRTLPHFTK DDYSPEARGF VENSYLRGLT PTEFFFHAMA GREGLIDTAV
KTAETGYIQR RLVKALEDLS ARYDGTVRNS LGDIVQFLYG EDGLDAMCIE KQKLGILKMS
DAAFEKKYRL DLANPPDWFK KDYEYGNELA GDKESMDLLD SEWGTLLSDR QTVRLINRAK
MGEEMMQLPL NIGRMIETAK RVFNVRATDR SSLRPADVIP RMQNLLSELK IVRGSDAIST
EADLNATILF KALIRSRLAF KEIVKVHRLN KLAFDHVLGE LQNRWDRSFV SPGEMVGVLA
AQSIGEPATQ MTLNTFHFAG VSSKNVTLGV PRLKEILNLA KDIKTPSMAV YLDTQLGTQE
QAKKLRSMVE YTNLRSITSV TEIYHDPDIQ GTTIAEDVDM VESYFLIPDD GQDNTDQQSR
WLLRITLDRQ KLLDKEIRID DVAQRIKEEY PNDLAVIFSD NNADEQVIRI RTVRQSDEKD
EDGEKKIEDD VMLKRLEAHL LDTLTLRGVP GIERAFLTKG TRLIVGEDGS ELAIKDDARC
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 PLLDAGAGRY ATSPSFSPSS PSFSPTSPML
RPTSPASPNY SPTSPSYSPT SPTSPRHYSP TSPAQFNSPT SPSYSPASPN YSPASPNLHG
AAGATSPSYS PASPSWSPTS PEAYSPTSPS FQRSPGNQQS PTSPSYSPTS PAFSPRTPGP
GNSGNQYSPN SPSND
//
