ID A0A2P5HLP7_9PEZI Unreviewed; 1723 AA.
AC A0A2P5HLP7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=DHEL01_v210432 {ECO:0000313|EMBL:POS71175.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS71175.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS71175.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS71175.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {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:POS71175.1}.
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DR EMBL; MAVT02001350; POS71175.1; -; Genomic_DNA.
DR STRING; 158607.A0A2P5HLP7; -.
DR InParanoid; A0A2P5HLP7; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000094444; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR CDD; cd01435; RNAP_I_RPA1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.357.120; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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 SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000094444};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 368..697
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 249..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..302
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1407
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1459
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1723 AA; 189511 MW; EAAE5FF4AFF53673 CRC64;
MNISQPVSSS VDRVEFTFLT KEEIHAVSVK KIENDTTFDT LLNPVRGGLY DPALGSWGDS
ICTTCNLGQQ SCPGHAGHID LPVPVYHPTF MDQVLRLVRA QCVYCHRLRL ARRDIHRYVC
IFRLLQYGLL KEAGMVDALG ENFHGLAMPD VPQADIADSD SEDQAGVADG VMRARDAYVH
RVLQECRPAL GRRKHEGAAE LRTALVGEFF KDIVKTRVCA SCRGISPIYR KDRYVKIFER
ALSGKEQARM AQAGLKRSEG IPSQTSKKSD RRSGHGSDEG VADLSSTDEE GNASDEGSGD
ALDEDGNVVP RKATRKQPSE HEDIAQRYLS PAEVQYRLTT LFEKEQEVLA LVYCRQPRAK
TTPLLASNMF FLETILVPPN RFRPEARTGD SQIAEAQQNS LYKNIIRASA QLASIYRQLQ
DQSRGVVDPR GQRSMTALHE AWTELQDSVN ALIDRNLNPV QGAAAKRNEE GIKQKLEKKE
GLFRKNMMGK RVNYAARSVI SPDPNIETNE IGVPPVFARK LTFPEPVTSH NFKDMQQAVI
NGVEKWPGAS AIENENGQTI NLRNKSLEDR IALANQLLAP TNNTSSGLRN KKVHRHLANG
DVVLMNRQPT LHKPSIMGHR VRVLPGEKTI RMHYANCNTY NADFDGDEMN MHFPQNEVAR
AEALQLADTD HQYISGTAGK PLRGLIQDHL SVSVALCDKD TLFDRQAYQQ LIYGALRPES
GHILGERIEM VPPAIIKPRA RWTGKQVITT ILKNIRPPNC GDLWMSGKTQ IPAARWGPDS
EEGAVLFQDG EFICGILDKS QLGPSSGGFI HSVHEVYGPA VAGKLLSSMG RLLTRYLNMR
AFTCGMDDLR LTREGEEKRK ATLADAPHIG LRVAAKYVTL DDRKPGPSDP ELLSRLEEVM
RDDSKQEGLD ALMNKGSSDL SSAVTQACLP NGLEKHFPKN QMQSMTTSGA KGSLVNANLI
SCNLGQQILE GRRVPLMVSG KSLPSFRPYD TDVRAGGYIV NRFLTGIRPQ EYYFHHMAGR
EGLIDTAVKT SRSGYLQRCL IKGMEGLTVG YDSSVRDSDG TLVQFLYGED GLDIAKQKYL
TNFGFVLRNF ESQLAQTHFN EATALGLFDH KDEFLKRNKL AVKKAKADLV NTDEPVNCAV
ASARHAFATS EKFYEAMSEY VKSNPDALIR DKKDKDESRR PVGATTLPRK QAEKILAAKY
LRSLVEPGEA VGIVAGQSVG EPSTQMTLNT FHLAGHSAKN VTLGIPRLRE ILMTASANIS
TPAMTLVLNE ELSADDGEMF AKAISVLPLS HVLDKVSVSE RVGKGIGYAL AKVFRIRLKF
FPSHEYTEAY NIGISDVLDT VENKFLSQLA RDIKKEIKKK TSGATSATPV VGVKSGTIEM
ADPSREVDSP AGGDNGDGDD DDDDGGGDGD ATTAKRRANR GEEASYGPND ADDDAIQQRM
DREADLDSDD EDEGLVESPA AENDDVPAVE KGASASRSDE GTSRESRVKE KTPNVTEFRC
DESKGEWCDF VLEYDVNVPK ILMLNLVESA VRKTLIQQIP GVGQCIFVAK DKVYDARAGG
EVEAAVVHTA GANLQAMQKY SDYINPNKIS TNDIAAVLAV YGVEAARNNI IRELSNVFGG
HGISVDNRHL NLIGDHMTRN GGFSPFNRMG LRGNVSPFTK MSFETTLAVL KDALLDGDWD
DLSTPSGRLV LGRLGKAGTG SFDVYTAAPM RHFDPMRADA MEE
//