ID A0A0D2JUB7_9EURO Unreviewed; 1231 AA.
AC A0A0D2JUB7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 47.
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=Z520_10120 {ECO:0000313|EMBL:KIX94094.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX94094.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX94094.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX94094.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-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|ARBA:ARBA00048552,
CC ECO:0000256|RuleBase:RU363031};
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. {ECO:0000256|ARBA:ARBA00011206}.
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}.
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DR EMBL; KN848089; KIX94094.1; -; Genomic_DNA.
DR RefSeq; XP_016628217.1; XM_016780614.1.
DR AlphaFoldDB; A0A0D2JUB7; -.
DR STRING; 1442371.A0A0D2JUB7; -.
DR GeneID; 27715866; -.
DR VEuPathDB; FungiDB:Z520_10120; -.
DR OrthoDB; 10248617at2759; -.
DR Proteomes; UP000053411; 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; 2.40.270.10: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; 3.90.1100.10:FF:000009; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000021; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1110.10:FF:000006; 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; 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};
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:UP000053411};
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..486
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 263..445
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 524..587
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 624..685
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 706..739
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 753..1128
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1130..1218
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1231 AA; 137318 MW; 14DBEB18A47C01C4 CRC64;
MPAKRKTDGG VGAPSHAARK TVAKTTSVRK APAKEGPPAD ASAAKDSLPD QTTKENPKIG
RQSRRPHHHA DSFDAALEPF YYDKSLTDPI DTARDKWNLL PAFLKVKGLV KQHVDSFNHF
VDVELKKIID AEPIITSDID PKFYIKYENI YIGKPCRNDE MEKLYRREFK ESSVTPNECR
LRDLTYAAPI LVDIRYTKTK DAFRTKAVPI GRLPLMLRSN KCVLANKSEA EMCAMDECPL
DPGGYFIVNG TEKVILVQEQ LSKNRIIVEA DPKKDLITAS VTSSTHARKS KSYIVLRKDL
LYMKHNILKE DIPICVLLKA MGVSSDMDMM NIVAGPDPTL QDDFAINFEE TIKNQIHTQQ
QALEYIGARL KITAKSTPFG QARRNFVQEA VEAISTVFIA HVPIEDLNFR PKALYVAHMA
RRALMAKRNP ALVDDRDYVG NKRLELAGQL LSLLFEDLFK KFNYDVKMKI DKELRKQNKT
ALADPVRIMV GASGNITQGM NRAIATGNWN LKRFRMDRAG VTHLLSRLSF IASLGMMTRI
SSQFEKTRKV SGPRALQPSS FGMLCPADTP EGEACGLVKN LALMTHITTD DEEAPIKRLI
FMLGAEDIVT VGGSELYATG SYLVLLNGTP VAATRQPSHF LSSFRRLRRS GRISEFVSIF
INHHHNTIQV ATDEGRICRP LIIVEDKKSK VTKRYLKSLR QGSMDFDDFL ARGLVEYLDV
NEENDSNIAM YESDINSTTT HLEIEPFTIL GAVAGLIPYP HHNQSPRNTY QCAMGKQAIG
FIANNQFLRI DTLLYLMVYP QKPLVKTRTI ELVKYDKLPA GQNATVAVMS YSGYDIEDAL
VLNKASVDRG FGRCQVLRKY PVTIKTYANE SSDVVYPPSK NDDGTIARGH ALLDSDGVAS
VGEKISSGEI YVNKYVPRNA NSSGLSENGS DSPRAFGWDP QPQKYRLPDP SYIDKVMVTE
TEAGNKVIKI QTRQTRVPEV GDKFSSRHGQ KGVVGIIAEQ VDMPFSDLGI TPDIIMNPHG
FPSRMTVGKM LELVSGKAGI LKGKFEYGTA FGGSKLEDMS RALIEAGYSY DGKDYLTSGI
TGEPLPAYVF TGPIYYQKLK HMVQDKMHSR SRGPRAILTR QPTEGRSRDG GLRLGEMERD
CLIAYGASQL LRERLMLSSD QHQVDVCENC GFMAFARWCQ RCSKAGEPGS NVVRMTLPYA
FKLLLNELGS MNVNTRLIVS DEFPADGSRR A
//
