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Database: UniProt
Entry: A0A2P5HLP7_9PEZI
LinkDB: A0A2P5HLP7_9PEZI
Original site: A0A2P5HLP7_9PEZI 
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
//
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