ID A0A226DLU3_FOLCA Unreviewed; 1848 AA.
AC A0A226DLU3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=Fcan01_18875 {ECO:0000313|EMBL:OXA46492.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA46492.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA46492.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA46492.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA46492.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) 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 -!- 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:OXA46492.1}.
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DR EMBL; LNIX01000015; OXA46492.1; -; Genomic_DNA.
DR STRING; 158441.A0A226DLU3; -.
DR OMA; QAFPIPH; -.
DR Proteomes; UP000198287; 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: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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000198287};
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 242..545
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 154..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1848 AA; 207601 MW; FEED46C2C68B9335 CRC64;
MSEVSDLRIP LRTVKKVQFG ILSPDEIRRM SVTEGGIRFT EITEGGRPKL CGLMDPRQGV
IDRNSRCLTC TGTQTECPGH FGHIDLAKPV YHPGFLGKTV KVLRCVCFYC SKMLVSPTHP
KMREVVAKTK GQPRRRIDFV YELCKKKSIC DGGDEMDGNQ GEEDPNITVS PSKKSGHGGC
GRFQPNIRKV GLELFAEWKN VNEADQEKKM AVTAERVLEI LKHISDEESL VMGMDPKWSR
PDWMIYSVLP VPPLPVRPAV VTFGSARNQD DLTHKLADIV KANNELLRND QSGAAAHIIA
ENVKMLQFHV ATLTDNEIPG LPRAMQTSGR PLKAIKARLK GKEGRIRGNL MGKRVDFSAR
TVITPDPNLR IDQVGVPRSI AQNLTFPEIV TPFNMDKMTE LVARGNNQYP GAKYIIRSNG
DRIDLRFHPK SSDLHLQLGY RVERHIRDGD LVIFNRQPTL HKMSMMGHRV KVLPWSTFRM
NLSCTTPYNA DFDGDEMNLH VPQSMETRAE VENLHITTRQ IITPQANKPV MGIVQDTLTG
AKKMTKRDVF LTKEQMMNLL MFLPIWDGRM PMPAIVKPIP LWTGKQLFTL IIPGNVNLVK
THATHPDDED DGPYKWISPG DTKVMVEHGE LIMGILCKKT LGTSEGSLLH ICFTELGHEV
AGQFYGNIQT VVNNWLMYEG HSIGIGDTIA DPQTYLEIQR TIKKAKEDVI EVIQKAHNME
LEPTPGNTLR QTFENQVNRI LNDARDKTGG SAKKSLTEYN NLKTMVVAGS KGSNINISQV
IACVGQQNVE GKRIPFGFRK RTLPHFIKDD YGPESRGFVE NSYLAGLTPS EFYFHAMGGR
EGLVDTAIKT AETGYIQRRL IKAMESVMVD YDGTVRNSTG QLIQLRYGED GLAAENVEHQ
TLPTVKLSNS AFEERFRFDP TNERYLRKVF DEEVMREIVG SAEVLSAVEK EWKTLKADRA
TMREIFPSGE SHVVLPCNLK RMIWNVQKIF HIDKRLPVDL NPIRVIEGVE NLLKKCVIVQ
GEDALSVQAN SNATLLFCCM VRSMLCTRKV AEEFHLSTEA FEWLIGEIET RFQQAMASPG
EMVGALAAQS LGEPATQMTL NTFHFAGVSS KNVTLGVPRL KEIINLSKKP KSPSLTVFLT
GGAARDAEKA KKVLCRLEHT TLRKMTAHTA IHYDPDPQNT IIAEDQDFVS IYYEMPDFNP
ARISPWLLRV ELDRKRMTDK KLTMEQIAEK INSAFGEDLN CIFNDDNAEK LILRIRITHP
EDKLDDDDEN PDQMDDSMFL RCIESSMLSE MTLQGIETIA KVYMHLPQTD AKKRTIITDS
GEFKQIAEWL LETDGTSLMR VLSERDVDHV RTYSNDICEI FMVLGIEAVR KCVEKEMNTV
LSFYGLYVNY RHLALLCDVM TAKGHLMAIT RHGINRQDTG PLMRCSFEET VDVLMDAAVH
AEVDPMRGVS ENIMLGQLPR MGTGCFDLLL DAEKCKFGIE VPTGPGPNGD LGMGSAFFNL
GSKSPMDTPW ISGATPAYDN LFTWRRSFAA QFTWKPRQSI LHSWWSVAEL FAHIAWDESL
VAELFSWILF SYKSEWRSES DLFSNESELF ATTESIVLAD EPKLLTDEPN LFADESELLA
FKPKLFANES ILLADEPILL ANKSELFTDQ SVVFSDESII LTYEPVLFAD EPKLFTDESI
LFADKPILLA GKSELFAYQS IILSHESKLF ANQPIVLSDK SILLSDESIL LAIEPNLFSF
VAELQSFEVP RGTLQTVRLT RSDGPDRPIT ALRAQVIVQR RQVIHPGIHL GFSPSSPTYS
PQPSVSSYSP TSPSYSPASP TYSPSSPTYS PDEDENKKPG GKKGRKNK
//