ID T1JVI2_TETUR Unreviewed; 1815 AA.
AC T1JVI2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=107371525 {ECO:0000313|EnsemblMetazoa:tetur02g04700.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur02g04700.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur02g04700.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; CAEY01000795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015795120.1; XM_015939634.1.
DR STRING; 32264.T1JVI2; -.
DR EnsemblMetazoa; tetur02g04700.1; tetur02g04700.1; tetur02g04700.
DR GeneID; 107371525; -.
DR KEGG; tut:107371525; -.
DR eggNOG; KOG0262; Eukaryota.
DR HOGENOM; CLU_000487_2_3_1; -.
DR OMA; NREDYQQ; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR CDD; cd01435; RNAP_I_RPA1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 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; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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 SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 320..637
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1387..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1452
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1780..1806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1815 AA; 204814 MW; 44F3C9123D5C7783 CRC64;
MNISLLSQFS LATVSFKPYS RQELKKSSVL EVTNPVSFDA LGHPTKGGLH DPVLGPSRRD
DICETCNLGG HGKDECPGHF GHISLPVPIY NPFFIRQMFQ MLSMCCFSCH HLLFHPANLQ
VVLYQLQALD YGLDYLVDEL QSVANDLSNI KSDKGPEFID FLKAKLSECI ENALKQNSTN
SKNDVSQVRN VIDRKQNLMK ALLQGKLVKI IKNCAHCNNK KFNMSLVNNS MVLMSQPKSL
PKHYGFTASN ETPETSGSVL KDKVQEVDSS GKSFLTPLVA RDHLRQLYKN ETETLKRMLK
LIHTEEGLED ALEGDDSAID VFFMDMIPVT PPRFRPLHMM GGKSYEDETT TMLTQVILAS
EGLKNSLKSL QNLDQTSVKE KTQEMTKLHS AWGRLQILCN RIYDSEMDKL PEKKAPGVRQ
ILEKKEGLFR KNMMGKRVNY AARSVISPDP YISVDEIGIP EIFATRLSYP QPVTPWNVEV
MKKAVINGPD IHPGALSVTL EDGSVMRLRA NDPEQRARIA NLLGQHKPGS RTVNRHLING
DILLLNRQPT LHKPSIMAHK ARVLKREKTL RLHYSNCKCY NADFDGDEMN AHFPQSELAR
SEAYNIVSVN KQYLVPKDGS PLGGLIQDHI VSATLLTMKG NFFNRKDYQQ LVFSALFNQK
TPIKLVKPTI WRPVPLWSGK QIITTLIINL VPPDKTPPTL YISSKVNSKT LSSGNFRDIT
VSKYYTPEEL DDSTVIIRQG EVLQGLIDKA NIGPTPYGLI HICYELYGGE VSNSLLTAIA
RLCTVYLQVH GGVTLGIEDI IVNENADRKR SEIIRASTTV GDEAATQAVG LPITCEKSVL
VKRLREWHAS QDPVLMKTLD SCMKSKTDEV NDGITKVCLP AGLIKKFPHN NLQLMIQSGA
KGGTVNALQI SCLLGQIELE GKRVPLMMSG RTLPSFVPYD TSPKAGGFVT GRFLTGIRPQ
EFFFHCMAGR EGLIDTAVKT SRSGYLQRCL IKHLEGLTVQ YDSTVRDIDG SLVQLQYGED
GIDVLKSQLL KPKAMPLLIH NRAVLMPTDE ELSRLQLSPD ILAKIEEYRQ NISDWEEINE
MDRLKRRIGS GFQEYFEVKL RDYKNNLPES VGPTELSQED YSTIIDSWFQ LSKNDKRQLN
FYFLPCPGPL SIDFRPNHHF GVLPEKMEYQ IQNYVKSSPD GLVFDPSVDV GDESWKGKQI
VTITELKNLI NSRFMKSLAD PGESVGLLAA QSIGEPSTQM TLNTFHFAGR GDMNVTLGIP
RLREILMTAS PKIATPNMDI PFRSDFDENR IDAVRKRMSS VKLCDVLETI DVKEILTINE
KTCARYYDIV FKFLPYQTYK KKFNAKPAKI LSYMESTFIK NLINAIKRAQ IIQRKYNSLY
DHSMHHREAK GGDENEGAPS APTRENPDAV SSDEEDNAVE EDTHAVRTKA HRNQELDYEE
PEEEEIEANK EPEEDQTDNI TTLEPDEEVH PKVDEDEELQ QQNEQESAES QKEKQPETNE
RQDDDWNPLL TKTLEKEKKE KEMLAKKALT ESLVKEKSSF IDLYDYDEVK KEWCRVVLKF
PLNTDKVDIA SIVEEEARKS YIFKIGSIDK VFLVEDREAS KRGVSHGKMI KTEGVGFFDL
VNMQSIFDLN RVYSNDIHAI ANTYGIEAAR KAITIEIANV FAVYGIEVDP RHLSLIADYM
TFNGTIKGMN RISMAGSSSP LQQMTFETTA AFLKSALLLD FKDELKSPSA RIFAGRPPLV
GTGILGLMQD GTVEYKPSQH LRFKNIKNDS KISPKSGRKF GPRNRTSNRF GNLKRKHQSP
NISIEKPLNK RTKFD
//
