ID A0A1Z5TE40_HORWE Unreviewed; 1789 AA.
AC A0A1Z5TE40;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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_06750 {ECO:0000313|EMBL:OTA34258.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA34258.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA34258.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA34258.1,
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 -!- 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:OTA34258.1}.
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DR EMBL; MUNK01000062; OTA34258.1; -; Genomic_DNA.
DR STRING; 1157616.A0A1Z5TE40; -.
DR VEuPathDB; FungiDB:BTJ68_06750; -.
DR InParanoid; A0A1Z5TE40; -.
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-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 Pfam; PF05001; RNA_pol_Rpb1_R; 17.
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; 8.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000194280};
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 248..552
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 156..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1590..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 698..725
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1789 AA; 196145 MW; 862EDE677EE838BD CRC64;
MQAAIGGNYT FPLSTAPFKQ IQEIQFGLFS PEEIKNMSVC HIEYPETMDE ARNRPREKGL
NDPKLGSVDR GTMCSTCNEV PEYCPGHFGH IELAQPVFHV GFIAKIKKIL ESVCHNCGKL
KADERNVQFA QALRLRDPKR RFEQVHKICK PIMTCETDEP SPDDQNDDPK AKLKAKGHGG
CGNVQPAVRK EQLRLNGSWK IAKSDDEEGK PEKETRQITP QMALNVFRNI SDIDMAKLGL
NADYARPEWM ILTVLGVPPP AVRPSISVDG TSQGMRSEDD LTYKLSDIIR ANSNVRRCEQ
EGSPQHVQDE FVQLLQFHVA TYMDNDIAGV PKALQKSGRP VKSIRARLKS KEGRLRGNLM
GKRVDFSART VITGDPNLSL DEVGVPRSIA RTLTFPEVVN AYNIHKLQTL VRNGPNVHPG
AKYVIRDTGD RIDLRKAKND VQLAYGWKVE RHVVDGDFII FNRQPSLHKE SMMGHKVRVM
PYSTFRLNLS VTSPYNADFD GDEMNLHVPQ SHETRAEVME LCAVPKNVVS PQKNGPLMGI
VQDTMAGIYM LTRRDVMIDY ENVMNILMWV PGWDGVVPPP AIFKPSPRWT GKQIISLALP
AGLNLQRSDE EATPHIPLKE AKGLLVQNGE LVLGRMTKKI VGASQGGVVH YIFNDMGRDG
PQAAVDFFNA TQRIVCYWLL HNGFSVGIGD TVPDAKMAEE IETAVQKEKA QLQDLVHTVE
NNELETLPGM TIRETFESKA KSFLDNARNN AGDIAFKGMR DCNNVGTMVH SGSKGSTTNV
SQMTAAVGQQ SLEGKRLPFG FKYRTLPHFP KDDYSPASRG FVENSYLRGL TPQEFFFHAM
GGREGLIDTA VKTAETGYIQ RRLVKALEEV MVKYDGTVRN SLGDILQFIY GEDGLDAMYI
EPQPLDIITA STAAFEKKYK IDVINPPSKD LTLTSEMLEM ADEIRGDTDV QRLFDDEFQD
IEESREKIRK GLGPEESDQS RQLPLNIDRM IRNVKDRFKI KDGSRSNLDP RWAIPKIRET
LDNLIIVRGD DALSKEADQN ATLLCKANFR SRLAFKRIVK DDSLTKEALE NILGDLDNRF
SRALASPGEM VGVLAAQSIG EPATQMTLNT FHLAGVTAKT TTKGVPRLKE ILNVADQLKT
PNMRVFQHDE DRLSQEKCKD LRSEIEFTNL RSVTDETEIY YDPDIQSTVI EADRDMVESY
FIIPEDSAEP IELQSKWLLR IVLGRRQLLD KGLTVTDVGQ AVKQFYGADV AVLFSDDNAD
EQVLRIRVLD RGKEDAGDDE APEEADDTLK RLEGHMLDNV RLRGVKGARR AFVSSETVMR
YAEDGSIVKS KNDEMCKEWF LDTDGVNLKE TLAVEGVDPY RTTCNHFGEI FKCFGIEATR
AALMRELSAV LTGDGSYVNY RHMAILCDVM CARGQLMAVT RHGINRADTG ALMRCSFEET
VEILFEAASS GELDDCRGVS ENIILGQLAP SGTGEFDMLL DQEMLKTVVS THKPVGVMTG
AASPMDGSMT PYDMGSPLAE GGYAGGPDYA ASFSPIIDAG QADVGGGFTA YGGGFGGQSP
YTGGMSPGYA PTSPFNAGFS PTSPGYGGYS PTSPAGYSPT SPGFDGATSP AYQVTSPRFS
PASPAYTPTS PTYSPTSPAY SGGNKVSPTS PSYSPTSPSY SPTSPSYSPT SPNYSPTSPA
MHSGSAPGSA TSPKYSPTSP QYSPTSPAYS PTSPAYSPTS PKYGSSSAGA GSMSTSPTSP
GYSPTSPVYS PTSPKYGGGG QGASTSNSPT SPSYSPTSPQ YSPNSPRED
//
