ID A0A4U0TXW5_9PEZI Unreviewed; 1203 AA.
AC A0A4U0TXW5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
GN ORFNames=B0A54_16967 {ECO:0000313|EMBL:TKA26902.1};
OS Friedmanniomyces endolithicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA26902.1, ECO:0000313|Proteomes:UP000310066};
RN [1] {ECO:0000313|EMBL:TKA26902.1, ECO:0000313|Proteomes:UP000310066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA26902.1,
RC ECO:0000313|Proteomes:UP000310066};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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:RU363031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC diphosphate; 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:ARBA00048552,
CC ECO:0000256|RuleBase:RU363031};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|RuleBase:RU000434}.
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:TKA26902.1}.
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DR EMBL; NAJP01000134; TKA26902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0TXW5; -.
DR STRING; 329885.A0A4U0TXW5; -.
DR OrthoDB; 10248617at2759; -.
DR Proteomes; UP000310066; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR FunFam; 2.40.270.10:FF:000006; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 2.40.270.10:FF:000011; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1070.20:FF:000002; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1110.10:FF:000006; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1800.10:FF:000002; DNA-directed RNA polymerase subunit beta; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1070.20; -; 1.
DR Gene3D; 3.90.1100.10; -; 1.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU363031};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU363031}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000310066};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363031};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 108..481
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 251..438
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 517..580
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 617..678
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 746..1109
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1111..1196
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..23
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..58
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1203 AA; 133995 MW; 0F5678D9AA166CA8 CRC64;
MSRLMLSKAT TKASKKAPTR RVKAKEPAET ETAPTIDSTA SLNHAASTTA PPAAAEPAKQ
SLKKRAPVVR DDMDALLKPF YYSKHLTDPI NTARDKWNLL PAFLRVKGLV KQHIDSYDYF
TDVALKEIIK ANHMVKSDTN RDKFIMFTDI RVGKPNRQDE RNTGYVDSSV TPNECRLRDM
TYAAPVYVDV VYSKQSGKAS KRNILVGRLP IMLRSSKCVL HGKSETDMGL LSECSIDPGG
YFIVRGQEKV ILVQEQLSKN RIIVESAKGI LQASVTSHTS HVKTKTYVLL KKGLLYLRHN
TLNEDVPVAI VLRAMGVQSD HEILLITAGN DATYQDEFAP NLEQAALEGI FTQEQALDYV
ASKLKADRFP SFGRVPKSPK QQALEKLAET IIPHVEVKGM NFRPKALYIA FMTRRVLMTM
HDPKLVDDRD YVGNKRLELA GQMLALLFED LFKDFTRQIK VSMDKILKKP NPTKEFDPTD
LILQFEHRIT SGMERAISTG NWTLKRFRMD RAGITHVLSR LSYISALGMM TRITSQFEKT
RKVSGPRALQ PSQFGMICTS DTPEGESCGL VKNLALMTHI TTSDDEDAVK RIVFILGAED
VEGASGMEVY GAGAYIVFMN GTPVALTRHP KQFLVAFRKF RRMGRISEFV SVYINHHHSG
VHIATDEGRI CRPLIVVEKS KSKVTARFLD SLRKGTMDFD DALSRGIVEY LDVNEENDSN
TAVYEDAITQ HTTHLEIEPF TILGAVAGLI PYPHHNQSPR NTYQCAMGKQ AIGAIAYNQF
ERIDTLLYLM VYPQKPMVST RAIELVKYDK LPAGQNAIVA VMSYSGYDIE DALVLNKASC
DRGFGRCQVF KKISHPLKAY GNGAADRMSD RDPKNSKHKK LGADGIVEVG AQLESGDMFM
LKETPMHQTT QVAPSVQKWS PQHMAYKLPD YCYADKVMIT TNEGSTTIIK IQTRQTRRPE
IGDKFSSRHG QKGVVGIIAE QADMPFSDSG ITPDIIMNPH GFPSRMTVGK MLELVSGKAG
VLEGKQEYGT AFGGSKVEDM GNALVRHGFS YSGKDFVTSG ITGESLPAYV FFGPIYYQKL
KHMVQDKMHA RATGPYAILT RQPTEGRSRA GGLRLGEMER DCLIAYGASQ LLLERLMLSS
DAHQVDVCET CGVMGYNNWC QSCKSSGGVV KMTMPYAAKL LIQELMSMNI KAKLCLEDEF
PRG
//
