ID D0Z769_DROME Unreviewed; 1887 AA.
AC D0Z769;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=RpII215-RA {ECO:0000313|EMBL:ACZ54678.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ACZ54678.1};
RN [1] {ECO:0000313|EMBL:ACZ54678.1}
RP NUCLEOTIDE SEQUENCE.
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (NOV-2009) 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=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); 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:ARBA00024550,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT100316; ACZ54678.1; -; mRNA.
DR RefSeq; NP_511124.1; NM_078569.3.
DR SMR; D0Z769; -.
DR DNASU; 32100; -.
DR EnsemblMetazoa; FBtr0073542; FBpp0073387; FBgn0003277.
DR GeneID; 32100; -.
DR KEGG; dme:Dmel_CG1554; -.
DR CTD; 5430; -.
DR VEuPathDB; VectorBase:FBgn0003277; -.
DR HOGENOM; CLU_000487_1_1_1; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 169836at2759; -.
DR PhylomeDB; D0Z769; -.
DR BioGRID-ORCS; 32100; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32100; -.
DR Bgee; FBgn0003277; Expressed in cleaving embryo and 25 other cell types or tissues.
DR ExpressionAtlas; D0Z769; baseline and differential.
DR Genevisible; D0Z769; DM.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' 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 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 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 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; 8.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
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 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 238..541
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 156..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 691..718
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 927..961
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1530..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1887 AA; 209168 MW; 4EC68C7708A167A3 CRC64;
MSTPTDSKAP LRQVKRVQFG ILSPDEIRRM SVTEGGVQFA ETMEGGRPKL GGLMDPRQGV
IDRTSRCQTC AGNMTECPGH FGHIDLAKPV FHIGFITKTI KILRCVCFYC SKMLVSPHNP
KIKEIVMKSR GQPRKRLAYV YDLCKGKTIC EGGEDMDLTK ENQQPDPNKK PGHGGCGHYQ
PSIRRTGLDL TAEWKHQNED SQEKKIVVSA ERVWEILKHI TDEECFILGM DPKYARPDWM
IVTVLPVPPL AVRPAVVMFG AAKNQDDLTH KLSDIIKANN ELRKNEASGA AAHVIQENIK
MLQFHVATLV DNDMPGMPRA MQKSGKPLKA IKARLKGKEG RIRGNLMGKR VDFSARTVIT
PDPNLRIDQV GVPRSIAQNL TFPELVTPFN IDRMQELVRR GNSQYPGAKY IVRDNGERID
LRFHPKSSDL HLQCGYKVER HLRDDDLVIF NRQPTLHKMS MMGHRVKVLP WSTFRMNLSC
TSPYNADFDG DEMNLHVPQS METRAEVENI HITPRQIITP QANKPVMGIV QDTLTAVRKM
TKRDVFITRE QVMNLLMFLP TWDAKMPQPC ILKPRPLWTG KQIFSLIIPG NVNMIRTHST
HPDEEDEGPY KWISPGDTKV MVEHGELIMG ILCKKSLGTS AGSLLHICFL ELGHDIAGRF
YGNIQTVINN WLLFEGHSIG IGDTIADPQT YNEIQQAIKK AKDDVINVIQ KAHNMELEPT
PGNTLRQTFE NKVNRILNDA RDKTGGSAKK SLTEYNNLKA MVVSGSKGSN INISQVIACV
GQQNVEGKRI PYGFRKRTLP HFIKDDYGPE SRGFVENSYL AGLTPSEFYF HAMGGREGLI
DTAVKTAETG YIQRRLIKAM ESVMVNYDGT VRNSVGQLIQ LRYGEDGLCG ELVEFQNMPT
VKLSNKSFEK RFKFDWSNER LMKKVFTDDV IKEMTDSSEA IQELEAEWDR LVSDRDSLRQ
IFPNGESKVV LPCNLQRMIW NVQKIFHINK RLPTDLSPIR VIKGVKTLLE RCVIVTGNDR
ISKQANENAT LLFQCLIRST LCTKYVSEEF RLSTEAFEWL VGEIETRFQQ AQANPGEMVG
ALAAQSLGEP ATQMTLNTFH FAGVSSKNVT LGVPRLKEII NISKKPKAPS LTVFLTGGAA
RDAEKAKNVL CRLEHTTLRK VTANTAIYYD PDPQRTVISE DQEFVNVYYE MPDFDPTRIS
PWLLRIELDR KRMTDKKLTM EQIAEKINVG FGEDLNCIFN DDNADKLVLR IRIMNNEENK
FQDEDEAVDK MEDDMFLRCI EANMLSDMTL QGIEAIGKVY MHLPQTDSKK RIVITETGEF
KAIGEWLLET DGTSMMKVLS ERDVDPIRTS SNDICEIFQV LGIEAVRKSV EKEMNAVLQF
YGLYVNYRHL ALLCDVMTAK GHLMAITRHG INRQDTGALM RCSFEETVDV LMDAAAHAET
DPMRGVSENI IMGQLPKMGT GCFDLLLDAE KCRFGIEIPN TLGNSMLGGA AMFIGGGSTP
SMTPPMTPWA NCNTPRYFSP PGHVSAMTPG GPSFSPSAAS DASGMSPSWS PAHPGSSPSS
PGPSMSPYFP ASPSVSPSYS PTSPNYTASS PGGASPNYSP SSPNYSPTSP LYASPRYAST
TPNFNPQSTG YSPSSSGYSP TSPVYSPTVQ FQSSPSFAGS GSNIYSPGNA YSPSSSNYSP
NSPSYSPTSP SYSPSSPSYS PTSPCYSPTS PSYSPTSPNY TPVTPSYSPT SPNYSASPQY
SPASPAYSQT GVKYSPTSPT YSPPSPSYDG SPGSPQYTPG SPQYSPASPK YSPTSPLYSP
SSPQHSPSNQ YSPTGSTYSA TSPRYSPNMS IYSPSSTKYS PTSPTYTPTA RNYSPTSPMY
SPTAPSHYSP TSPAYSPSSP TFEESED
//
