ID A0A1Z5SQY9_HORWE Unreviewed; 1741 AA.
AC A0A1Z5SQY9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=BTJ68_14505 {ECO:0000313|EMBL:OTA23253.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA23253.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA23253.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA23253.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-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:OTA23253.1}.
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DR EMBL; MUNK01000309; OTA23253.1; -; Genomic_DNA.
DR STRING; 1157616.A0A1Z5SQY9; -.
DR VEuPathDB; FungiDB:BTJ68_14505; -.
DR InParanoid; A0A1Z5SQY9; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000194280; 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; 1.10.150.390; -; 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:UP000194280};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 385..717
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 144..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1741 AA; 191923 MW; AFC3E0B384B9B628 CRC64;
MNISAPVSNQ LTSVSFTHLT STDIHALSAR RITSSTTLDT LLNPIPGGLY TPELGQFGDN
ACATCGLKNP QCPGHCGHIE MPVPCYHPTF LDQVLRLVRA SCVYCYRLKM GRVAVHRFGA
KLRLVECGLI QELRELDEIT ASSATSKDIA AESGSEDEES GEEGDSEAKG LIDQRERFVK
SAIARARKED RLSTQKTEAT TNARRAIISE FMGSITKGKK CNNCKGINHS YRKDRFVKIF
RKPLSEKDRY AMIQSGHKAK DPIIELRKKQ RAERSRKRKR DEKDEGIVAD IVGEEEEEPE
EEEGDDVNMD EESEGDVAIA GGDMVADAAG EATKKKTAKD QEEYLNPSRI HAQLTALFER
EQPILSAVYG HNRQSNKAAA PLTPDMFFLK DILVPPNRYR PEARTGSNEI AEAQENTLYK
NILTACDTLN TIQRELSGKE SRDARYRVRN YGDFETTWIT LQDAVNSLID RDRNPIQGAA
AKRNPEGIKQ KLEKKEGMFR KYMMGKRVNF AARTVISPDP NIETNEIGVP PVFAVKLTYP
EPVTSWNVEE LQEAVRNGPF VWPGAVAIES ETGQVINLER KNAEERTALA NQLLAPSSTI
GAAGTRGTRN KKVHRHLNNG DIVIMNRQPT LHKPSMMCHR ARVLPGEKTL RMHYANCNTY
NADFDGDEMN LHFPQNELAR SEALSIADTD HQYLSSTAGN PLRGLIQDHV SMGVALTSRD
TLFERGEYMQ LLYSALRPEH GHCAQGRIVT VPPAIFKPKM LWTGKQVVTS VLKNLIQEGY
EGLTMSGKST TDPNLWGLAG AKEEGVVVFR DGYLCQGILD KKQIGPSSGG FVNAVYEVYG
HTVAGRLLSV MGRLLTRLEN MRAFSCGVED LIFTREGEEK RRDALQGAET LGTRVAAKYV
GLVDGEEQEK ELVVDPIELR KRMEGVLREE EQQAGLDSLM NSTTAKELSS LVTNSCLPTA
LVRAFPANQM QAMTSSGAKG SKVNANQISC NLGQQVLEGR RVPVMVSGKT LPCFKPFEPS
VRAGGYIVDR FLTGVRPQEY FFHAMAGREG LIDTAVKTSR SGYLQRCLIK GMEGLKVEYD
SSVRDADGSV IQFLYGEDGL DVAKSKYLSD FKFAAENLPS LLGGLGVRGD FDKVISHEAS
EYMKQAEKAY RKSGDLGASD PALSLYSPSR YAGSMSESVY AAARKYVDEN PDKVIRNKKK
GIEGARGVTK TNFNAILDLR YLKSVVEAGE AVGVVAGQSV GEPSTQMTLN TFHLAGHSAK
NVTLGIPRLR EIVMTAAKNI ATPTMTLRLI EEMSTDEAKK FAKGISKLAL SEILDKATVT
ETVGKGTAYT EAKKYQIRLD FFPSKEYMKE YAITVEDVVS TIEHRLLPRL QAMTRKELKK
RGDEKSVKAG DKAKASDAMP EIGKSAGATE QDDAEGDDDA TRDKAKSNRQ QAGYEAYEDE
EENMLAARNQ REDEIEEPED EGFGGSNKGS PEPDSSEDEE DAADERKARR SAAKDRENRI
KTDRKTNDIV KFAFDDISGD SCTFTLEYDS ATAKILMLHL VENAARSSLI QSVPGISGAM
LDTAATEEAK GTPILAASGV NLPAMWDYQH IINPHHLYTN SVYDILTHYG VEAARAAIVL
ELQSVFGGHG ISVDPRHLTL IADYMTRDGG YQAFSRMGYR GNASPFMKMS FETTVGFLRD
AVTEGDWDDL TNPSARIVTG RLGKIGTGGF DVFLPVRNGE SGEEKREVVE EDGDGDVEME
G
//
