ID A0A7J0GBX2_9ERIC Unreviewed; 1203 AA.
AC A0A7J0GBX2;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 14.
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=Acr_20g0000970 {ECO:0000313|EMBL:GFZ08289.1};
OS Actinidia rufa.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=165716 {ECO:0000313|EMBL:GFZ08289.1, ECO:0000313|Proteomes:UP000585474};
RN [1] {ECO:0000313|EMBL:GFZ08289.1, ECO:0000313|Proteomes:UP000585474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuchu {ECO:0000313|Proteomes:UP000585474};
RA Sugita-Konishi S., Sato K., Mori E., Abe Y., Kisaki G., Hamano K.,
RA Suezawa K., Otani M., Fukuda T., Manabe T., Gomi K., Tabuchi M.,
RA Akimitsu K., Kataoka I.;
RT "De Novo Assembly of kiwifruit Actinidia rufa.";
RL Submitted (JUL-2019) 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 -!- 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:GFZ08289.1}.
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DR EMBL; BJWL01000020; GFZ08289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J0GBX2; -.
DR OrthoDB; 10248617at2759; -.
DR Proteomes; UP000585474; 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:0009536; C:plastid; 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; 2.40.50.150:FF:000005; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000012; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000015; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1800.10:FF:000006; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000585474};
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}.
FT DOMAIN 108..458
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 291..424
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 501..560
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 597..658
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 673..720
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 729..1100
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1102..1200
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1203 AA; 135717 MW; 8E9984187724F217 CRC64;
MWPPDSKEDP EPSGKGGDNL NGVKDMDLDD ILGQPGTSSK GGKLANGDLH MDLDDDDLMD
PTPIRDLGAV TKLTLTMISS KMESRMCLTP LVRSQWSLDM IRPRRGENEW KYASVKFGKV
TLERPRFWTG DKFSADSGKE FLNLLPRHAR LQNMTYSSRM KVQIHVQVYT QNLVRSDKFK
TGKEQYLDKE VISEDDRDVL IGRIPVMVKS DLCWMNGVEK GDCDFDHGGY FLIKGAEKTF
IAQEQICLRR LWVSSSPTWT VAYREVSKRK RVYIKLETPK SEQIRGGEKV LTVYFSATEF
PIWILFFALG VSSDKEVVNL IDCDCNDSSI VNVLIASIHY ADKHCDGFRR GKNALSHVVK
EIEKCRFPPG ESVEDFFGNY LFSNLSGFKR KARFLGYMVN CLLLAYTGRR KVDNRDDFRN
KRLELAGELL ERELRVHVKH AERRMVKAMQ RDLYGDRSLH PIEHYLDASI ITNGLSRAFS
TGAWTHPYKR MERTSGVVAT LRRTNPLQAT ADMRKTRQQV QYTGKVGDAR YPHPSHWGKI
CFLSTPDGEN CGLVKNLAIT GLVSTNIQEP FLDELLDCGM DNLVDDTSTL LSGKDKVFLD
GDWVGVCEDS VSFVAELRRK RRRKEVPPQV EIKRDEKHKE VRIFSDAGRI LRPLLVVENL
RKIKALKGGD YSFRSLLDNG VIELIGAEEE EDCRTAWGIK YLLMENDVKP PVKYTHCELD
MSFLLGLSCA IIPFANHDHA RRVLYQSEKH SQQAIGFSTT NPNIRVDTNT HQLYYPQRPL
FRTMLSDCLG KPGYPLGHSG IVPRPEIFNG QCAIVAVNVH LGYNQEDSLV MNRASLERGM
FRSEHIRSYK ADVDNNEAIG KKPKFEDAVN FGKVQSKIGR VDSLDDDGFP FIGANLQNGD
IVIGKCAESG ADHSIKLKHT ERGMVQKVVL SANDEGKNFA VVSMRQVRTP CLGDKFSSMH
GQKGVLGFLE SQENFPFTIQ GIVPDIVINP HAFPSRQTPG QLLEAALGKG IACGGSQRYA
TPFSTISVDA ITDQLHRAGF SRWGSERVYN GRTGEMIRSL IFMGPTFYQR LTHMAEDKVK
FRNTGPVHPL TRQPVADRKR FGGIKFGEME RDCLIAHGAA ANLHERLFTL SDSSQMHICR
KCQNIANVIQ RAVPGGRKIR GPYCRFCESV EDIVLVNVPY GAKLLAQELF SMGISMKFET
ELG
//
