ID A0A1E3P3F3_WICAA Unreviewed; 1635 AA.
AC A0A1E3P3F3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=WICANDRAFT_53195 {ECO:0000313|EMBL:ODQ59734.1};
OS Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL
OS Y-366-8) (Yeast) (Hansenula anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=683960 {ECO:0000313|EMBL:ODQ59734.1, ECO:0000313|Proteomes:UP000094112};
RN [1] {ECO:0000313|EMBL:ODQ59734.1, ECO:0000313|Proteomes:UP000094112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8
RC {ECO:0000313|Proteomes:UP000094112};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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}.
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DR EMBL; KV454210; ODQ59734.1; -; Genomic_DNA.
DR RefSeq; XP_019038941.1; XM_019182707.1.
DR STRING; 683960.A0A1E3P3F3; -.
DR GeneID; 30199953; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000094112; 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:UP000094112};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 328..655
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 145..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1635 AA; 182136 MW; DD58A1D3C7CE0F97 CRC64;
MDISKPVGSE ITHVDFGVLS AEDIRKLSAK QITNPTVFDN LGHPISGGLY DLALGAFLRN
LCATCGLDDK FCPGHQGHIE LPIPVYNPLF FNQLYIFLRS ACLYCHHFRL KSTEVHRYAC
KLKLIQYGLL SELEPLDNIH MSGASMEAEE GEEEDNAPDS NPQADRDLIE RREDFVNSAI
AKALSEGRTS ENGVMTTTVL EERKHLIHEF YKKLLSRPKC GNCSMFSPTY RKDGFTKLFE
NPLKEKQVLN NRVKGHARQD MLKTNGKSNG DEMDVDTPAQ PAKKSTGSKY VLSTEVRNIM
RAVFQAESNI LKYLFHSRPK ATEKVNSDIF FLQAIVVPPT RFRLPSKLGD EIHENSQNEL
LSKVLNTSLL IRDLNDQIST VQKDKITAEE RKITFNRLMN AFVTIQNDVN AFIDSTKNQN
ANAARTAAPG IKQALEKKEG LFRKHMMGKR VNYAARSVIS PDPNIETNEI GVPPVFAVKL
TYPEPVTSHN VNELRQAVIN GPDKWPGAIQ IQNEDGSLIS LIGMTTDQRK ALANQLLTPS
GNTSHVLNKK VYRHIKNNDI VIMNRQPTLH KASMMGHKVR VLPGEKTLRL HYANTNAYNA
DFDGDEMNMH FPQNENARAE ALNLANTDSQ YLTPTSGSPL RGLIQDHISA GVWITNKDSF
FTREQYQQYV YGCIRPEDGH STRAKLVTVP PAIFKPIPLW TGKQIITTVL LNITPVNMPG
INLLSKNKIK NEYWGEGSKE NEVLFKNGEL LCGILDKSQY GASQYGIVHS LHEVYGPSVA
GKSLSVLGRL FTNYIQSTAF TCGMDDLRLT AEGNNWRNEI LLTSVDVGRL AATEVTNLDK
NTKSTDPKFL QRLEEVYRDD NKAGILDAVT QSKVNSITSQ VVSKCVPEGT MKRFPYNSMQ
AMALSGAKGS NVNVSQIMCL LGQQALEGRR VPVMVSGKTL PSFKAYETDA RAGGYIKGRF
YSGIRPQEYY FHCMAGREGL IDTAVKTSRS GYLQRCLTKQ LEGVHVSYDN SVRDGDGRLV
QFLYGGDAVD VTKESHMNQF KFCIDNYDAL LTKYNPGALI DHLDTESASR YSKKVRKSMK
KNKDVPHFAQ STKYDPVLSV YNPSKYLGSV SETFQSKLDS FIDGNPDLFS KSGLSDKKFR
ALMQLKYMRS LINPGESVGI IASQSVGEPS TQMTLNTFHF AGHGAANVTL GIPRMREIIM
TASAAIKTPQ MTLPILDEVT DDQADAFCRS IAKVVFSELV DNVTVTETSG NSEDGRGKRS
YDIDLEFFNS EQYHEEYDVS KEQLEQVITT KFLRTLESAI TKELRKQKKI GSESLPEVGK
AVPKSQTQIT SDERISNKSN DNDDDDADDE KSRSKTKQSV SYDEPDDDEI ETMRNAEKSS
DEEMDSDSDS DSDSDSDEEE PTKSAATGEL SKAARDRQSA VLGSHSLITR FNFDDVNGNW
CKFKLELGAG TQKLLMVNIV EEICRKVVVK EVPHIGRCLH PQPEGGKRVL TTEGVNFGAM
WDYDDFIDVN GITSNDVAAV LRTYGVEAAR NTIVNEINNV FGRYAISVSS RHLDLIGDMM
TREGSYLAFN RQGIDSSTST FMKMSYETTC QFLTKAVLDN DREELESPSA RIVLGKLSGV
GTGSFDLLSR MPATA
//
