ID A0A9J5W203_SOLCO Unreviewed; 1248 AA.
AC A0A9J5W203;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 8.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
DE Flags: Fragment;
GN ORFNames=H5410_059134 {ECO:0000313|EMBL:KAG5569368.1};
OS Solanum commersonii (Commerson's wild potato) (Commerson's nightshade).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4109 {ECO:0000313|EMBL:KAG5569368.1, ECO:0000313|Proteomes:UP000824120};
RN [1] {ECO:0000313|EMBL:KAG5569368.1, ECO:0000313|Proteomes:UP000824120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZ3.2 {ECO:0000313|EMBL:KAG5569368.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG5569368.1};
RA Cho K.;
RT "De no assembly of potato wild relative species, Solanum commersonii.";
RL Submitted (SEP-2020) 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:KAG5569368.1}.
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DR EMBL; JACXVP010000012; KAG5569368.1; -; Genomic_DNA.
DR OrthoDB; 10248617at2759; -.
DR Proteomes; UP000824120; Chromosome 12.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:InterPro.
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; 2.40.50.150:FF:000002; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1070.20:FF:000001; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000003; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000005; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1110.10:FF:000005; 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; 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:UP000824120};
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 54..463
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 224..415
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 488..552
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 587..648
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 673..724
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 731..1101
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1103..1194
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..39
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAG5569368.1"
SQ SEQUENCE 1248 AA; 142187 MW; E0352B8196B92997 CRC64;
MYGDNEYVDD RDMMQVEDEG GEGRGDGDED EDESQEITQD DAWAVISSYF EEKGLVRQQL
DSFDEFIQNT MQEIVDETAD IEIRPESQHN PSRQPDFVET IYKIKFTQIY LSRPMMTESD
GETNTLFPKA ARLRNLTYSS PLYVDVKKEV IKKGHDYEEV TENQEFTKVF IGKVPIMLRS
SYCSLYNLSE KDLTELGECP YDQGGYFIVN GSEKVLIAQE KMSNNHVYVF KKRQPNKYAY
VAEVRSISEG QNKAPSGMFV RMLSRSNSKG AYGQYIRATL PYIRAEIPII VVFRALGFVA
DKDILAHICY DFADTQMMEL LRPSLEEAFV IQNQQVVALD YIGKRGSTVG FTREKRIKYA
KEILQREMLP HVGTREYCET KKAFYFGYII HRLLLCVLGR RPEDDRDHYG NKRLDLAGPL
LGGLFRMLFR KLTRDVRSYV QKCVDGGKDV NLQFAIKAKT ITSGLKYSLA TGNWGQANAA
GTRAGVSQVL NRLTFASTLS HLRRLNSPIG REGKLAKPRQ LHNSHWGMMC PAETPEGQAC
GLVKNLALMV YITVGSAANP ILEFLEEWST ENFEEISPAV IPQSTKIFVN GCWVGIHRNP
DLLVRTLRQL RRQVDVNTEV GVVRNINLKE LRLYTDYGRC SRPLFIVDKK RLRIKKKDIV
ALQMRESTED SGWHDLVAKG YIEYVDTEEE ETTMIAMTIN DLTNSRLNPD EAYAETYTHC
EIHPSLILGV CASIIPFPDH NQSPRNTYQS AMGKQAMGIY VTNYQFRMDT LAYVLYYPQK
PLVTTRAMEH LHFRQLPAGI NAIVAITCYS GYNQEDSVIM NQSSIDRGFF RSLFFRSYRD
EEKKMGTLVK EDFGRPDREH TMGMRHGNYD KLEDDGFAPP GTRVSGDDVI IGKTTPISQD
EAQGQSARYT RKDHSTSLRH SETGIVDQVL LTTNADGLRF VKIRMRSVRI PQIGDKFSSR
HGQKGTIGMT YTQEDMPWSA EGITPDIIVN PHAIPSRMTI GQLVECIMGK VASHIGREGD
ATPFTDVTVD SISKTLLECG YQMRGFERMY NGHTGRILSA MIFLGPTYYQ RLKHMVDDKI
HSRGRGPVQI LTRQPAEGRS RDGGLRFGEM ERDCMIAHGA AHFLKERLFD QSDAYRVHVC
QQCGLMAIAN LKKTSFECRS CRNKTDNVQV YIPYACKLLI QELMSMAIAP RMLTKELKPS
NGKLFISFNN ILHHRINLKH ISNYSYIALA NSICFQYFDI SHLTRHGN
//
