ID A0A0F8UK09_9EURO Unreviewed; 1255 AA.
AC A0A0F8UK09;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 18-JUN-2025, entry version 42.
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=ARAM_005255 {ECO:0000313|EMBL:KKK19964.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK19964.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK19964.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK19964.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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|RuleBase:RU363031};
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000256|ARBA:ARBA00011730}.
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:KKK19964.1}.
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DR EMBL; JZBS01002141; KKK19964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8UK09; -.
DR STRING; 308745.A0A0F8UK09; -.
DR OrthoDB; 48074at5052; -.
DR Proteomes; UP000034291; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.40.50.150:FF:000002; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000005; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000022; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1110.10:FF:000003; 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; 3.90.1100.10; -; 2.
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; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR NCBIfam; NF007175; PRK09606.1; 1.
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; PF04567; RNA_pol_Rpb2_5; 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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000034291};
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 37..474
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 287..427
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 501..565
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 600..661
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 704..774
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 781..1153
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1155..1247
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
SQ SEQUENCE 1255 AA; 141827 MW; 091162105F0094D9 CRC64;
MADYGDAYDE EYYDDMDEGI TSEDCWTVIS SFFDTKGLVS QQLDSFDEFI SSTMQELVEE
QGQVTLDQTL PPSEDEVDPV VVRRYELKFG TVMLSRPSVT EGDGATTIML PQEARLRNLT
YASPLYLGIT KKIMEGRERL VADRDEDDIA ESNEDRKAAG TYLQWEQKEL PADQAKEETV
FIGKMPIMLK SKYCILKDLS EQALYNWNEC PYDSGGYFII NGSEKVLIAQ ERSAGNTVQV
FKKAPPSPTP YVAEIRSAVE KGSRLLSQLS LKLFAKGDSA KGGFGPTIRS TLPYVKTDIP
IVVVFRALGV VSDEDILNHI CYDRNDTPML EMLKPCIEEG FVIQDREVAL DFIAKRGSSQ
SSMNHERRVR YAREIMQKEL LPHISQSEGS ETRKAFFLGY MVHRLLQCAL GRRDVDDRDH
FGKKRLDLAG PLLANLFRVL FTRVTRDLQR YVQRCVETNR EIYLNIGIKA STLTGGLKYA
LATGNWGEQK KAASAKAGVS QVLSRYTYSS TLSHLRRTNT PIGRDGKIAK PRQLHNTHWG
LVCPAETPEG QACGLVKNLA LMCYITVGTP SEPIIDFMIQ RNMEVLEEFE PQVTPNATKV
FVNGVWVGIH RDPAHLVNTM LSLRRRNMIS HEVSLIRDIR EREFKIFTDA GRVCRPLFVI
DNDPKSENCG SLVLNKEHIR KLEQDKDLPP DLDPEERRER YFGWDGLVKS GVVEYVDAEE
EETIMIVMSP EDLDISKQLQ AGYALPEEEH DPNKRVRSIL SQKAHTWTHC EIHPSMILGI
CASIIPFPDH NQSPRNTYQS AMGKQAMGVF LTNFDQRMET MANILYYPQK PLATTRSMEF
LRFRELPAGQ NAIVAISCYS GYNQEDSVIM NQSSIDRGLF RSLFYRTYTD SEKMVGLTVV
ERFEKPMRSD TIGMRKGTYD KLDEDGIIAP GVRVSGEDII IGKTAPLAPE AEELGQRTKA
HTKLDVSTPL RSTESGIVDQ VLVSTSNDDL KFVKVRMRTT KIPQIGDKFA SRHGQKGTIG
ITYRQEDMPF TREGVSPDLI INPHAIPSRM TIAHLIECQL SKVSALRGFE GDATPFTDVT
VDSVSRLLRE HGYQSRGFEV MFNGHTGRKM VAQVFLGPTY YQRLRHMVDD KIHARARGPT
QILTRQPVEG RARDGGLRFG EMERDCMIAH GASAFLKERL FDVSDPFRVH ICDDCGLMTP
IAKLKKGLFE CRLCNNKHRI SQVHIPYAAK LLFQELAAMN IAARMFTNRS GVSVR
//
