ID E3SH44_9MUSC Unreviewed; 1872 AA.
AC E3SH44;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
DE Flags: Fragment;
GN Name=RpII215 {ECO:0000313|EMBL:ADO24384.1};
OS Drosophila nigromaculata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=198721 {ECO:0000313|EMBL:ADO24384.1};
RN [1] {ECO:0000313|EMBL:ADO24384.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22217779; DOI=10.1603/EN11136;
RA Stump A.D., Jablonski S.E., Bouton L., Wilder J.A.;
RT "Distribution and mechanism of alpha-amanitin tolerance in mycophagous
RT Drosophila (Diptera: Drosophilidae).";
RL Environ. Entomol. 40:1604-1612(2011).
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; GU060492; ADO24384.1; -; Genomic_DNA.
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; 4.
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 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 231..534
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1521..1558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1572..1872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADO24384.1"
FT NON_TER 1872
FT /evidence="ECO:0000313|EMBL:ADO24384.1"
SQ SEQUENCE 1872 AA; 207332 MW; F71072935E9B9C7B CRC64;
KAPLRQVKRV QFGILSPDEI RRMSVTEGGV QFAETLEGGR PKLGGLMDPR QGVIDRTSRC
QTCAGNMTEC PGHFGHIDLA KPVFHIGFIT KTIKILRCVC FYCSKMLVSP HNPKIKEIVM
KSKGQPRKRL AYVYDLCKGK TICEGGEDMD LTKDNQQVDP NKKPGHGGCG HYQPSIRRTG
LDLTAEWKHV NEDSQEKKIV VSAERVWEIL KHITDEECFI LGMDPKYARP DWMIVTVLPV
PPLAVRPAVV MFGAAKNQDD LTHKLADIIK ANNELRKNEA SGAAAHVIQE NIKMLQFHVA
TLVDNDMPGM PRAMQKSGKP LKAIKARLKG KEGRIRGNLM GKRVDFSART VITPDPNLRI
DQVGVPRSIA QNLTFPELVT PFNIDRMQEL VRRGNSQYPG AKYIVRDNGE RIDLRFHPKS
SDLHLQCGYK VERHLRDDDL VIFNRQPTLH KMSMMGHRVK VLPWSTFRMN LSCTSPYNAD
FDGDEMNLHV PQSMETRAEV ENIHITPRQI ITPQANKPVM GIVQDTLTAV RKMTKRDVFI
TREQVMNLLM FLPTWDGKMP QPCILKPRPL WTGKQIFSLI IPGNVNMIRT HSTHPDEEDD
GPYKWISPGD TKVMVEHGEL IMGILCKKTL GTSAGSLLHI CFLELGHDIA GRFYGNIQTV
INNWLLLEGH SIGIGDTIAD PQTYTEIQTA IKKAKDDVIN VIQKAHNMEL EPTPGNTLRQ
TFENKVNRIL NDARDKTGGS AKKSLTEYNN LKAMVVSGSK GSNINISQVI ACVGQQNVEG
KRIPYGFRKR TLPHFIKDDY GPESRGFVEN SYLAGLTPSE FYFHAMGGRE GLIDTAVKTA
ETGYIQRRLI KAMESVMVNY DGTVRNSVGQ LIQLRYGEDG LCGELVEFQN MPTVKLSNKV
FEKRFKFDWS NERYMRKVFT DDVIKEMTDS SDAIQELEGE WDKLVTDRDN LRTIFPNGDS
KVVLPCNLQR MIWNVQKIFH INKRLPTDLS PMRVIRGVQE LLERCVIVTG NDRISKQANE
NATLLFQCLI RSTLCTKYVA EEFRLSTEAF EWLIGEIETR FQQAQANPGE MVGALAAQSL
GEPATQMTLN TSHFAGVSSK NVTLGVPRLK EIINISKKPK APSLTVFLTG GAARDAEKAK
NVLCRLEHTT LRKVTANTAI YYDPDPQRTV IAEDQEFVNV YYEMPDFDPT RISPWLLRIE
LDRKRMTDKK LTMEQIAEKI NVGFGEDLNC IFNDDNADKL VLRIRIMNNE ENKFQDEDEA
VDKMEDDMFL RCIEANMLSD MTLQGIEAIG KVYMHLPQTD SKKRIVITET GEFKAIGEWL
LETDGTSMMK VLSERDVDPI RTSSNDICEI FQVLGIEAVR KSVEKEMNAV LQFYGLYVNY
RHLALLCDVM TAKGHLMAIT RHGINRQDTG ALMRCSFEET VDVLMDAAAH AETDPMRGVS
ENIIMGQLPK MGTGCFDLLL DAEKCRFGIE IPNSLGSSML GGAAMFIGGG STPSMTPPMT
PWVNCHTPRY FSPPGHVSAM TPGGPSFSPS AASDASGMSP SWSPAHPGSS PSSPGPSMSP
YFPASPSVSP SYSPTSPNYT ASSPGGASPN YSPSSPNYSP TSPMYAATSP RYASATPNFN
PQSTGYSPSS SGYSPTSPVY SPTSNFQSSP SFAGSGSNMY SPGNAYSPSS SNYSPNSPSY
SPMSPSYSPS SPSYSPTSPC YSPTSPSYSP TSPNYTPVTP SYSPTSPNYS ASPHYSPASP
AYSQTGVKYS PTSPTYSPPS PSYDGSPGSP QYTPGSPQYS PASPKYSPTS PLYSPSSPQH
SPSNQYSPTG STYSATSPRY SPNISIYSPG STKYSPTSPT YTPTARNYSP TSPMYSPTAP
SHYSPTSPAY SP
//
