ID A0A2B7ZV77_9EURO Unreviewed; 1697 AA.
AC A0A2B7ZV77;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=GX50_00076 {ECO:0000313|EMBL:PGH37093.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH37093.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH37093.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH37093.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-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:PGH37093.1}.
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DR EMBL; PDND01000001; PGH37093.1; -; Genomic_DNA.
DR STRING; 73230.A0A2B7ZV77; -.
DR VEuPathDB; FungiDB:EMCG_02817; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000226031; 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; -; 2.
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:UP000226031};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 372..699
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1697 AA; 189682 MW; 5B24A51CB439335D CRC64;
MASFTRPISS SIGEVDFGVL SNEEIKSISV KRIYNTPTLD SLNNPVPGGL YDPALGAWGD
HVCTTCRLNS WSCNGHSGHI ELPVHVYNVT FFDQLFRLLR AQCVYCHRFR MSRADIKSYT
CKLRLLQYGL VEEAAAIDNM EARRGKDNNA GSGSEDSEDE DEEDFIRRRD AYVKRCIQQV
LARNKDQEFL HGAKNPVAVE RRRNIVRAFL KDITAVKKCA SCSGISPPFR RDKYSKIFKK
PLPPKAKVAM TEAGFHVPNP LLLIKEANDL SKKHDHPPQD SHMNGYPDDD NASVSTDSHG
AEQQITMGNA VLAQVEEKGS RNKPSEQGAQ QFMPSPEVYA ALRLLFEKEQ EVLDLVYDSR
PRSKHRPRVT PDMFFIKQIL VPPNKYRPIA ANGSNDIIEA QQNTSFTRII KLCDQINQIS
RERQGDSTES VTRLRDYRDL LQTIVQLQDA VNSLIDRDRN PNQGAAGIQN EDGIKQRLEK
KDGLFRKNMM GKRVNFAARS VISPDPNIET NEIGVPLVFA KKLTYPEPVT NHNYWELKQA
VINGPDIYPG AAAVENEVGQ VVSLKFKSVD ERIAIANMLL APSNFKMKRS RNKKVYRHLT
TGDVVLMNRQ PTLHKPSIMG HRARVLTGER TIRMHYANCN TYNADFDGDE MNLHFPQNEL
ARAEAMQLAD TDHQYLSATA GKPLRGLIQD HISMGTWFTS RDTFFDKDDY YQLLYNCLRP
ENSHTVTDKI LLMEPTILRP QKLWTGKQVI STIMMNITPA RLHGLNLTGK SSTRGDHWGE
GSEEGQVIFQ DGELLCGILD KAQLGPSAGG LIHSVHEIYG HVVAGKLIGV IGRLMTKFLH
MRAFTCGMDD LRLTKKGNED RKGKLQEAEG VGRQIALKYV TLDQTTVEDE EAELKRRLED
ALRDEEKQAG LDTVFNSQTA IISSDITAAC LPIGLEKSFP WNQMQAMTTS GAKGTVVNAN
LISCNLGQQV LEGRRVPVMI SGKTLPSFRP FETSLMAGGY VSGRFLTGIK PQEYYFHAMA
GREGLIDTAV KTSRSGYLQR CLIKGMEGLK AEYDNSVRET SDGSVIQFLY GEDGLEITKQ
KHLQDFPFLA RNFWSVVEEL NGSDEFNRVK SDKAGDWNQN AIKKFRKTGK LDCVDPALSL
FPPGSCYGST SESFAIALKK YQKENPDKML KDKGKVENGI SKRDFVRVMN MKYMRSVVEP
GESVGIVAGQ SIGEPSTQMT LNTFHLAGHS TKNVTLGIPR LREIVMTASN QILTPTMTGV
LNKQLTEKDG RVFAKAISKL TLAEVVDTLR VHERISSGPG RGKAKIYDLE IDFFPPEEYT
EEYAIQIEDI LKTLQDKFVP RLVKLTRAEL KKRTDEKSLS TFSAAQPAIG TSAGVVEEST
RRFGREARDA DADANDDDDE EDQDDAKRAM ANMNRSNQVS YEAPDEGEED IIRRQDSPEP
DSEDEADGDR QEERTATEDV NMQDADSDSD SEKIQKSKES EDTVIGKHAE VTKFKFSLKN
GRSCHIQLRY DISTPKLLLL PLVEDAARTS VIQFVKGLGT CTYVEANGKD PAHIVTDGVN
LLAMRDYQDY VYPHSLYTNS IADMLAMYGV EAARACIIRE MAAVFDGHSI SVDNRHLNLI
GDVMTHAGGF RAFNRMGLVK DSTSPFMKMS FETTVGFLRD AVLERDWDNL NGPSSRIVMG
RVGMVGTGAF DVLAPVA
//