ID A0A226DKG8_FOLCA Unreviewed; 2207 AA.
AC A0A226DKG8;
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_19458 {ECO:0000313|EMBL:OXA45723.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA45723.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA45723.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA45723.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA45723.1};
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:OXA45723.1}.
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DR EMBL; LNIX01000017; OXA45723.1; -; Genomic_DNA.
DR STRING; 158441.A0A226DKG8; -.
DR OMA; VMELMMV; -.
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; -; 2.
DR Gene3D; 2.40.40.20; -; 3.
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; 2.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 2.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 3.
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; 2.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 3.
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 PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00663; RPOLA_N; 3.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 3.
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 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 239..542
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT DOMAIN 1476..1852
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT DOMAIN 2020..2197
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 154..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2207 AA; 245879 MW; 2C3A9D18A22D5F7F CRC64;
MSEVSDLRVP LRTVKKVQFG ILSPDEIRRM SVTEGGVRFP ELTEDGRPKL CGLMDPRQGV
IDRNSRCLTC TGSQTECPGH FGHIDLAKPV YHPGFLGKTV KVLRCVCFYC SKMLVSPTHP
KMREVVAKTK GQPRRRIDFV YELCKKKSIC DGGDEMDSNP GEEDPNITSK KSGHGGCGRF
QPNIRKVGLE LFAEWKNVNE ADEEKKMAVT AERVLEIFKH VSDEECLVMG MDPKWSRPEW
MIYSVLPVPP LCVRPAVVTF GSAPKQDDLT HKLADIVKAN NELLRYEQSG AAAHIIAENV
KMLQFHVATL TDNEVPSLPR AMQTSGRPLK AINARLKGKE GRIRGNLMGK RVDFSARGAI
TPDPNLRIDE VGVPRSIAQN LTFPEIVTPF NMDKMTELVA RGNNQYPGAK YIIRSNGDRI
DLRFHPKSSD LHLQLGYRVE RHIRDGDLVI FNRQPTLHKM SMMGHRVKVL PWSTFRLNLS
CTAPYNADFD GDEMNLHVPQ SMETRAEVEN LHITTRQIIT PQANKPVMGI VQDTLTGAKK
MTKRDVFLTK EQMMNLLMFL PVWDGRMPMP AIVKPIPLWT GKQLFTLIIP GYVNLVKTHA
THPDDEDDGP YKWISPGDTK VMVEHGELIM GILCKKTLGT SEGSLLHICF TELGHEVAGQ
FYGNIQTVVN NWLMYEGNSI GIGDTIADPQ TYLEIQRTIK KAKEDVIEVI QKAHNMELEP
TPGNTLRQTF ENQVNRILND ARDKTGDSAK KSLTEYNNLK TMVVAGSKGS NINISQVIAC
VGQQNVEGKR IPFGFRKRTL PHFTKDDYGP ESRGFVENSY LAGLTPSEFY FHTMESREGL
VHTAIKTAET GYIQRRLIKA MESVMVHYDG TVRNSTGQLI QLRYGEDGLA AENVEHQTLP
TLKLSNSAFK AGFRFDPTNE RYLRKVFDEE VMQEIVRSAE VISAVEKEWK TLKADRATMR
EIFPSGESHV VLPCNLKRMI WNVQKIFHID KRLPVDLNPI RVIAGVENLL KKCVIVQGED
ALSVQANSNA TLLFGCMVRS MLCTRKVAEE FHLSTEAFEW LIGEIEMRFQ QAMASPGEMV
GALAAQSLGE PVTQMTLNTF HYAGVSNVTL GVPRLKEIIN LSKKPKSPSL TVFLTGDTAR
DAEKAKKVLC RLEHTTLRKM TAHTAIHYDP DPQNTIIAED QDFVSIYYEM PDFNPARISP
WLLRVELDRK RMTDKKLTME HIAEKINSAF GEDLNCIFND DNAEKLILRI RIAHPEDKLD
DDEDNPDHMD DAMLLRCIEA SMLSEMTLQG IETISKVYMH LPQTDAKKRT IITESGEFKQ
IAEWLLETDG TSLMRVLSER DVDHVRTYSN DICEIFMVLG IEAVRKCVEK EINTVLSLPG
LYINYRHLAL LCDVMTAKGQ LPRMGTGCFD LLLDAEKCKF GIEVPTGPGP NGDLGMGSAF
FNLGSKSPMG TPWISGATPA YDNVWSPGGG MMSGGPGFSP SAASDISSFS PGGGRSPLSS
PGSPGSPFYN AGGVSPNYSP TSPGMSPSLP NYSPGSYSPT SPGGGQSPTY SPTSASPQLS
PSYSPTSLNG YSLTSPIYSP PSPSYWPSLP SSPSYSPTSP SYSPTSSSYL TPSPSYSPTS
PSYSPTSPSY SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPSSPTYS PSSPNYSPSS
PRYSPNSPTN SLGRPGSPNY SPSRMTELVA RGNNQYPGAK YIIRSNGDRI DLRFHPKSSD
LHLQLGYRVE RHIRDSDLVI FNRQPTLHKM SMMGHRAKVL PWSTFRINLS CTTPYNADFD
GDEMNLHVPQ SMETRAEVEN LHITTRQIIT PQANKPVMGI VQDTLTGAKK MTKRDVFLTK
DGRMPMPAIV KPIPLWTGKQ LFTLIIPGNL NLVKTHATHP DDEDDGPYKW ISPGDTKVMV
EHGELIMGIL CKKKPGTNEG TSSHLLYRIR STIVNNWLMY EGNSIGIGDT IADPQTYLEI
QRTIKKAKED VIEVIQKAHN MELEPTPGNT LRQTFENQVN WILNDARDKT GGSVKKSLTE
YNHQDDLKHK LSDIIKANNE LLRYDQSGAA AHIIAENVKM LQFHVATLTD NEIPGLPRPM
QTSGRPLKAN KARLKGKDSR IRGNLMCKRV EVLPWSTFRM NLSSLPDEMN LHVPQSMETR
SEVEDLHITT RQIITPQANK PVMGIVQDTL IGVKKTTKRD VFLTKVM
//
