ID A0A9P0DDN5_PHACE Unreviewed; 1904 AA.
AC A0A9P0DDN5;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=PHAECO_LOCUS1133 {ECO:0000313|EMBL:CAH1117253.1};
OS Phaedon cochleariae (Mustard beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX NCBI_TaxID=80249 {ECO:0000313|EMBL:CAH1117253.1, ECO:0000313|Proteomes:UP001153737};
RN [1] {ECO:0000313|EMBL:CAH1117253.1}
RP NUCLEOTIDE SEQUENCE.
RA King R.;
RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAH1117253.1}
RP NUCLEOTIDE SEQUENCE.
RG ENA_rothamsted_submissions;
RG culmorum;
RA King R.;
RL Submitted (OCT-2022) 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:RU004279}.
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:RU004279};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; OU896707; CAH1117253.1; -; Genomic_DNA.
DR OrthoDB; 6752614at2759; -.
DR Proteomes; UP001153737; Chromosome 1.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_N; 1.
DR FunFam; 2.40.40.20:FF:000019; DNA-directed RNA polymerase II subunit RPB1; 1.
DR FunFam; 1.10.132.30:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 1.10.150.390:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 1.10.274.100:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 3.30.1360.140:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 3.30.1490.180:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 4.10.860.120:FF:000005; DNA-directed RNA polymerase subunit; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 2.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR NCBIfam; NF006336; PRK08566.1; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 12.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 16.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP001153737};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 237..540
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1567..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1880
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1904
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1904 AA; 209754 MW; FCAC66FB6A1F1520 CRC64;
MAASDSKAPL RTVKRVQFGI LSPDEIRRMS VTEGGIRFPE TMEAGRPKLC GLMDPRQGVI
DRNSRCQTCA GNMTECPGHF GHIDLAKPVF HVGFITKTIK ILRCVCFFCS KLLVSPNNPK
IKEVVMKSKG QPRKRLAFVY DLCKGKNICE GGDEMDVGKE GGGEDQGKKQ GHGGCGRYQP
NIRRAGLDLS AEWKHVNEDT QEKKIALSAE RVWEILKHIT DEECFILGMD PKFARPDWMI
VTVLPVPPLS VRPAVVMFGS ARNQDDLTHK LADIIKSNNE LQKNEAAGGA AHIITENVKM
LQFHVATLVD NDMPGMPRAM QKSGKPLKAL KSRLKGKEGR IRGNLMGKRV DFSARTVITP
DPNLRIDQVG VPRSIAQNMT FPEIVTPFNF EKMLELVQRG NSQYPGAKYI IRDNGERIDL
RFHPKPSDLH LQCGYKVERH IRDGDLVIFN RQPTLHKMSM MGHRVKVLPW STFRMNLSCT
SPYNADFDGD EMNLHVPQSM ETRAEVENLH ITPRQIITPQ ANKPVMGIVQ DTLTAVRKMT
KRDVFIEKEQ MMNLLMFLPI WDGKMPRPAI LKPKPLWTGK QIFSLIIPGN VNMIRTHSTH
PDDEDEGPYK WISPGDTKVM VEHGELVMGI LCKKTLGTSA GSLLHICMLE LGHEVCGRFY
GNIQTTINNW LLLEGHSIGI GDTIADPQTY TEIQKAIKKA KEDVIEVIQK AHNMELEPTP
GNTLRQTFEN QVNRILNDAR DKTGGSAKKS LTEYNNLKAM VVSGAKGSNI NISQVIACVG
QQNVEGKRIP FGFRKRTLPH FIKDDYGPES RGFVENSYLA GLTPSEFYFH AMGGREGLID
TAVKTAETGY IQRRLIKAME SVMVHYDGTV RNSVGQLIQL RYGEDGLCGE MVEFQTLRTV
KLSNKAFERK FRFDPSNERY LRRVFGEEVI KQIMGSGEVI SELEREWEQL QKDREAMRQI
FPSGESKVVL PCNLNRMIWN VQKIFHINKR APTDLSPLRV IQGVRELLKK CVIVAGDDRL
SRQANENATL LFQCLVRSTL CTKCVSEEFR LSTEAFEWLI GEIETRFQQA QANPGEMVGA
LAAQSLGEPA TQMTLNTFHF AGVSSKNVTL GVPRLKEIIN ISKKPKAPSL TVFLTGAAAR
DAEKAKNVLC RLEHTTLRKV TANTAIYYDP DPQNTVITED QEFVNVYYEM PDFDPTRISP
WLLRIELDRK RMTDKKLTME QIAEKINAGF GDDLNCIFND DNAEKLVLRI RIMNSDDGKF
GEGADEDVDK MDDDMFLRCI EANMLSDMTL QGIEAIAKVY MHLPQTDSKK RIVITETGEF
KAIAEWLLET DGTSMMKVLS ERDVDPVRTF SNDICEIFSV LGIEAVRKSV EKEMNAVLQF
YGLYVNYRHL ALLCDVMTAK GHLMAITRHG INRQDTGALM RCSFEETVDV LMDAASHAEV
DPMRGVSENI IMGQLPRMGT GCFDLLLDAD KCKQGMPIAQ AHGADLLNAG MFFGSAATPS
SMSPGGGAGG VMTPWNQIGT PYVGSAWSPQ NMMGSGMTPG GAAFSPSAAS DASGMSPAYG
AWSPTPQSPA MSPYLASPHG QSPSYSPSSP AFLPTSPSMT PTSPGYSPSS PGYSPTSPNY
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS
PSYSPTSPSY SPTSPSYSPT SPSYSPTSPN YSPTSPSYSP TSPSYSPTSP NYSPTSPSYS
PSSPRYTPAS PSYSPTSPSY SPSSPQYSPA SPSYSPSSPK YSPTSPSYSP TSPSFSGGSP
QYSPTSPSYS PTSPSYSPSS PQHTPAASSR YSPSSPNYSP SSPSYSPTSP QYSPHSTKYS
PTSPTYTPTS PSYSPASPAY SPAPPRYSPS SPSYSPTSPG QENE
//
