ID A0A428QFG5_9HYPO Unreviewed; 1749 AA.
AC A0A428QFG5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=CEP54_004834 {ECO:0000313|EMBL:RSL64073.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL64073.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL64073.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL64073.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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}.
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:RSL64073.1}.
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DR EMBL; NKCI01000035; RSL64073.1; -; Genomic_DNA.
DR STRING; 1325734.A0A428QFG5; -.
DR Proteomes; UP000288168; 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:UP000288168};
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 1553..1749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1749 AA; 192220 MW; 641EB6532D28C1B5 CRC64;
MANLIFTHSS APLKTVEEIQ FGLMSPEEIK NMSVCHILYP ETMEENKTKP RDGGLNDPLL
GSIDRQFRCK TCTQAMGECP GHFGHIELAK PVYHPGFIKK VKKILEIVCH NCSKVLADTR
DPEFAAAIAT RDPKVRFSRV WEVCKKKRRC DNDEPKQKDE EFAPGMKLGP VEGHGGCGNM
QPNVRQAALQ LKAAFDVVEE GGGKRRETTP ITPEMAHNIL RRISEEDLRD MGLNSDYARP
EWMVLTVLPV PPPPVRPSIS MDGTGTGMRN EDDLTYKLGD IIRANGNVKQ AIREGSPAHI
ARDFEELLQY HVATYMDNDI AGQPRALQKS GRPVKAIRAR LKGKEGRLRG NLMGKRVDFS
ARTVITGDAN LSLHEVGVPR SIARTLTYPE TVTPYNIGRL HQYVENGPNE HPGAKYVIRA
DGQRIDLRHH RRAGAISLEY GWKVERHLID GDYIIFNRQP SLHKESMMGH RVRVMPYSTF
RLNLSVTSPY NADFDGDEMN LHVPQSEETR AEVKELCLVP LNIVSPQKNG PLMGIVQDSL
AGVYKLCRRD TFLTKEQIMN SMLWVPNWDG VIPQPAILKP RPRWTGKQLI SMVIPKEVTL
HNASDKKEDA PLKDEGILIQ AGQLMYGLPT KKIVGAAAGG IVHISYNELG AEGAMAFLNG
VQQVVTYWLL NNGHSIGIGD TIPDKATIEK VQVHIDEEKA EVARLTAMAT ANELEALPGM
NVRATFENKV SMALNQARDK AGTTTQKSLK DSNNAVTMAS SGSKGSSINI SQMTALVGQQ
IVEGKRIPFG FKYRTLPHFT KDDYSPEARG FVENSYLRGL TPSEFFFHAM AGREGLIDTA
VKTAETGYIQ RRLVKALEDL SARYDGTVRN SLGDVVQFLY GEDGLDAMCI EKQKMGILNM
SNAAFKAKYR LDLANPPEWF KQDYEFGNEL TGDRPSMALL DTEWEALLKD RQMIRHINKA
KQTEEMMQLP LNITRIIESA KRVFNVKAND RSNLRPSDVI PAVQNLLDHM KIVRGTDPIS
QEADANATIL FKGLLRSRLA FKEVVKEHRL NKLAFDHVIG ELQNRWDRAF VSPGEMVGVL
AAQSIGEPAT QMTLNTFHFA GVSSKNVTLG VPRLKEILNL AKNIKTPSMA VYLNTPLARQ
EQAKKLRSMV EYTNLRSVTA VTEIYYDPDI QSTNIPEDMD MVESYFMIPD DTQVSIDQQS
RWLLRITLDR QKLLDKEIRI DDVAQRIKEE YPTDLAVIFS DNNADEQVIR IRTVSAGDKD
EDGDGRMEDD VMLKRLEAHL LDTLTLRGVN GVERAFLTKG TRLVESPNGA LLAIKDDPRC
TQWYLDTSGS ALRDVLAVDG VDASRTYTND LWQVVEVFGI EAARSALVKE LTNVLAFDGS
YVNHRHIALL TDVMTYRGSI SAVTRHGINR ADTGALMRCS FEETVEILLE AAASGELDDC
RGISENVMLG QMAPMGTGNF DVLLDPKMLE TVISDNSRMG LMPGMPVKGG ESEGAATPYD
TGSPMADSGY LSLNSPAAGN FSPIQGAGSD TPAGFGNTEY GFGGSTAMSP YAMRGGTSPF
TTSPTSPFGP GGGYSPTSPN AYSPTSPLVD GGMGRYATSP SFSPSSPSFS PTSPMVRPTS
PASPNYSPSS PNYSPASPSS PRHYSPTSPA QFNSPTSPNY SPASPNYSPA SPNLHAGGTT
SPSYSPASPT WSPTSPEAYS PTSPYQRSPG AQQSPTSPSY SPTSPAFSPR TPGPGSSGNQ
YSPNSPSNE
//
