RPC3_HUMAN
ID RPC3_HUMAN Reviewed; 534 AA.
AC Q9BUI4; O15317; Q9Y3R6;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC3;
DE Short=RNA polymerase III subunit C3;
DE AltName: Full=DNA-directed RNA polymerase III subunit C;
DE AltName: Full=RNA polymerase III 62 kDa subunit;
DE Short=RPC62;
GN Name=POLR3C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR3G AND POLR3F, AND VARIANT
RP ARG-243.
RC TISSUE=Cervix carcinoma;
RX PubMed=9171375; DOI=10.1101/gad.11.10.1315;
RA Wang Z., Roeder R.G.;
RT "Three human RNA polymerase III-specific subunits form a subcomplex with a
RT selective function in specific transcription initiation.";
RL Genes Dev. 11:1315-1326(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION AS ANTIGEN IN SYSTEMIC
RP SCLEROSIS.
RX PubMed=12384934; DOI=10.1002/art.10521;
RA Kuwana M., Kimura K., Kawakami Y.;
RT "Identification of an immunodominant epitope on RNA polymerase III
RT recognized by systemic sclerosis sera: application to enzyme-linked
RT immunosorbent assay.";
RL Arthritis Rheum. 46:2742-2747(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Totaro A.;
RT "Genomic structure of human RNA polymerase III subunit (RPC62).";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH GTF3C4.
RX PubMed=10523658; DOI=10.1128/mcb.19.11.7697;
RA Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G.;
RT "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the
RT RNA polymerase III machinery and contains a histone-specific
RT acetyltransferase activity.";
RL Mol. Cell. Biol. 19:7697-7704(1999).
RN [6]
RP IDENTIFICATION IN THE RNA POL III COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12391170; DOI=10.1128/mcb.22.22.8044-8055.2002;
RA Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.;
RT "Characterization of human RNA polymerase III identifies orthologues for
RT Saccharomyces cerevisiae RNA polymerase III subunits.";
RL Mol. Cell. Biol. 22:8044-8055(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION.
RX PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
RA Chiu Y.-H., Macmillan J.B., Chen Z.J.;
RT "RNA polymerase III detects cytosolic DNA and induces type I interferons
RT through the RIG-I pathway.";
RL Cell 138:576-591(2009).
RN [9]
RP FUNCTION.
RX PubMed=19609254; DOI=10.1038/ni.1779;
RA Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A.,
RA Hornung V.;
RT "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA
RT polymerase III-transcribed RNA intermediate.";
RL Nat. Immunol. 10:1065-1072(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP INTERACTION WITH POLR3G AND POLR3GL.
RX PubMed=24107381; DOI=10.1101/gr.161570.113;
RA Renaud M., Praz V., Vieu E., Florens L., Washburn M.P., l'Hote P.,
RA Hernandez N.;
RT "Gene duplication and neofunctionalization: POLR3G and POLR3GL.";
RL Genome Res. 24:37-51(2014).
RN [13] {ECO:0007744|PDB:2XUB, ECO:0007744|PDB:2XV4}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION, INTERACTION WITH POLR3F;
RP POLR3G AND POLR3GL, AND MUTAGENESIS OF 51-LYS-LYS-52; LEU-312; ARG-357;
RP 364-ARG--ARG-367; LYS-389; 445-ASN--ARG-449 AND 466-ARG--ILE-470.
RX PubMed=21358628; DOI=10.1038/nsmb.1996;
RA Lefevre S., Dumay-Odelot H., El-Ayoubi L., Budd A., Legrand P., Pinaud N.,
RA Teichmann M., Fribourg S.;
RT "Structure-function analysis of hRPC62 provides insights into RNA
RT polymerase III transcription initiation.";
RL Nat. Struct. Mol. Biol. 18:352-358(2011).
RN [14] {ECO:0007744|PDB:5AFQ}
RP X-RAY CRYSTALLOGRAPHY (7.00 ANGSTROMS) IN COMPLEX WITH POLR3GL.
RX PubMed=26394183; DOI=10.1016/j.jsb.2015.09.004;
RA Boissier F., Dumay-Odelot H., Teichmann M., Fribourg S.;
RT "Structural analysis of human RPC32beta-RPC62 complex.";
RL J. Struct. Biol. 192:313-319(2015).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific core component of RNA polymerase III which synthesizes small
CC RNAs, such as 5S rRNA and tRNAs. May direct with other members of the
CC subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the
CC interactions between TFIIIB and POLR3F. May be involved either in the
CC recruitment and stabilization of the subcomplex within RNA polymerase
CC III, or in stimulating catalytic functions of other subunits during
CC initiation. Plays a key role in sensing and limiting infection by
CC intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic
CC DNA sensor involved in innate immune response. Can sense non-self dsDNA
CC that serves as template for transcription into dsRNA. The non-self RNA
CC polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs
CC (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I
CC pathway. Preferentially binds single-stranded DNA (ssDNA) in a
CC sequence-independent manner (PubMed:21358628).
CC {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370,
CC ECO:0000269|PubMed:21358628}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits (By similarity). RPC3/POLR3C, RPC6/POLR3F and
CC RPC7/POLR3G form a Pol III subcomplex (PubMed:9171375,
CC PubMed:12391170). Directly interacts with POLR3G and POLR3GL
CC (PubMed:24107381, PubMed:21358628, PubMed:26394183). Directly interacts
CC with POLR3F/RPC39 (PubMed:26394183). Interacts with GTF3C4
CC (PubMed:10523658). {ECO:0000250, ECO:0000269|PubMed:10523658,
CC ECO:0000269|PubMed:12391170, ECO:0000269|PubMed:21358628,
CC ECO:0000269|PubMed:24107381, ECO:0000269|PubMed:26394183,
CC ECO:0000269|PubMed:9171375}.
CC -!- INTERACTION:
CC Q9BUI4; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-5452779, EBI-5661893;
CC Q9BUI4; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-5452779, EBI-11523526;
CC Q9BUI4; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-5452779, EBI-744115;
CC Q9BUI4; Q96MT8-3: CEP63; NbExp=5; IntAct=EBI-5452779, EBI-11522539;
CC Q9BUI4; P38432: COIL; NbExp=3; IntAct=EBI-5452779, EBI-945751;
CC Q9BUI4; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-5452779, EBI-11988027;
CC Q9BUI4; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-5452779, EBI-744099;
CC Q9BUI4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-5452779, EBI-618309;
CC Q9BUI4; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-5452779, EBI-2514791;
CC Q9BUI4; Q0VD86: INCA1; NbExp=3; IntAct=EBI-5452779, EBI-6509505;
CC Q9BUI4; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-5452779, EBI-715394;
CC Q9BUI4; Q6ZU52: KIAA0408; NbExp=4; IntAct=EBI-5452779, EBI-739493;
CC Q9BUI4; O95198: KLHL2; NbExp=3; IntAct=EBI-5452779, EBI-746999;
CC Q9BUI4; P52294: KPNA1; NbExp=3; IntAct=EBI-5452779, EBI-358383;
CC Q9BUI4; O00505: KPNA3; NbExp=3; IntAct=EBI-5452779, EBI-358297;
CC Q9BUI4; O60684: KPNA6; NbExp=5; IntAct=EBI-5452779, EBI-359923;
CC Q9BUI4; O95678: KRT75; NbExp=3; IntAct=EBI-5452779, EBI-2949715;
CC Q9BUI4; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-5452779, EBI-1216080;
CC Q9BUI4; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-5452779, EBI-10963850;
CC Q9BUI4; P26367: PAX6; NbExp=3; IntAct=EBI-5452779, EBI-747278;
CC Q9BUI4; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5452779, EBI-79165;
CC Q9BUI4; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-5452779, EBI-10171633;
CC Q9BUI4; Q9H1D9: POLR3F; NbExp=2; IntAct=EBI-5452779, EBI-710067;
CC Q9BUI4; O15318: POLR3G; NbExp=7; IntAct=EBI-5452779, EBI-12362221;
CC Q9BUI4; Q9BT43: POLR3GL; NbExp=7; IntAct=EBI-5452779, EBI-2855862;
CC Q9BUI4; P78424: POU6F2; NbExp=3; IntAct=EBI-5452779, EBI-12029004;
CC Q9BUI4; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-5452779, EBI-11322432;
CC Q9BUI4; Q13464: ROCK1; NbExp=3; IntAct=EBI-5452779, EBI-876651;
CC Q9BUI4; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-5452779, EBI-1378139;
CC Q9BUI4; P23497-2: SP100; NbExp=3; IntAct=EBI-5452779, EBI-6589365;
CC Q9BUI4; A1L306: TNR; NbExp=3; IntAct=EBI-5452779, EBI-10182881;
CC Q9BUI4; Q12933: TRAF2; NbExp=3; IntAct=EBI-5452779, EBI-355744;
CC Q9BUI4; P14373: TRIM27; NbExp=6; IntAct=EBI-5452779, EBI-719493;
CC Q9BUI4; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-5452779, EBI-11530712;
CC Q9BUI4; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-5452779, EBI-12227803;
CC Q9BUI4; Q9H8Y1: VRTN; NbExp=3; IntAct=EBI-5452779, EBI-12894399;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Antibodies against POLR3C have been found in the sera of
CC patients with systemic sclerosis (SSc).
CC -!- SIMILARITY: Belongs to the eukaryotic RPC3/POLR3C RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; U93867; AAB63675.1; -; mRNA.
DR EMBL; AY091463; AAM12033.1; -; mRNA.
DR EMBL; AJ238221; CAB41919.1; -; Genomic_DNA.
DR EMBL; AJ238222; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238223; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238224; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238225; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238226; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238227; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238228; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238229; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238230; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238231; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238232; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238233; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; AJ238234; CAB41919.1; JOINED; Genomic_DNA.
DR EMBL; BC002586; AAH02586.1; -; mRNA.
DR CCDS; CCDS72864.1; -.
DR RefSeq; NP_001290385.1; NM_001303456.1.
DR RefSeq; NP_006459.3; NM_006468.7.
DR PDB; 2XUB; X-ray; 2.80 A; A=1-534.
DR PDB; 2XV4; X-ray; 2.95 A; S=1-534.
DR PDB; 5AFQ; X-ray; 7.00 A; A/B=1-534.
DR PDB; 7A6H; EM; 3.30 A; O=1-534.
DR PDB; 7AE1; EM; 2.80 A; O=1-534.
DR PDB; 7AE3; EM; 3.10 A; O=1-534.
DR PDB; 7AEA; EM; 3.40 A; O=1-534.
DR PDB; 7AST; EM; 4.00 A; X=1-534.
DR PDB; 7D58; EM; 2.90 A; O=1-534.
DR PDB; 7D59; EM; 3.10 A; O=1-534.
DR PDB; 7DN3; EM; 3.50 A; O=1-534.
DR PDB; 7DU2; EM; 3.35 A; O=1-534.
DR PDB; 7FJI; EM; 3.60 A; O=1-534.
DR PDB; 7FJJ; EM; 3.60 A; O=1-534.
DR PDBsum; 2XUB; -.
DR PDBsum; 2XV4; -.
DR PDBsum; 5AFQ; -.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR AlphaFoldDB; Q9BUI4; -.
DR SMR; Q9BUI4; -.
DR BioGRID; 115868; 89.
DR DIP; DIP-59078N; -.
DR IntAct; Q9BUI4; 49.
DR STRING; 9606.ENSP00000334564; -.
DR iPTMnet; Q9BUI4; -.
DR MetOSite; Q9BUI4; -.
DR PhosphoSitePlus; Q9BUI4; -.
DR SwissPalm; Q9BUI4; -.
DR BioMuta; POLR3C; -.
DR DMDM; 60393871; -.
DR EPD; Q9BUI4; -.
DR jPOST; Q9BUI4; -.
DR MassIVE; Q9BUI4; -.
DR MaxQB; Q9BUI4; -.
DR PaxDb; Q9BUI4; -.
DR PeptideAtlas; Q9BUI4; -.
DR PRIDE; Q9BUI4; -.
DR ProteomicsDB; 79088; -.
DR Antibodypedia; 33966; 256 antibodies from 24 providers.
DR DNASU; 10623; -.
DR Ensembl; ENST00000334163.4; ENSP00000334564.3; ENSG00000186141.9.
DR GeneID; 10623; -.
DR KEGG; hsa:10623; -.
DR MANE-Select; ENST00000334163.4; ENSP00000334564.3; NM_006468.8; NP_006459.3.
DR UCSC; uc001eoh.3; human.
DR CTD; 10623; -.
DR DisGeNET; 10623; -.
DR GeneCards; POLR3C; -.
DR HGNC; HGNC:30076; POLR3C.
DR HPA; ENSG00000186141; Low tissue specificity.
DR MIM; 617454; gene.
DR neXtProt; NX_Q9BUI4; -.
DR OpenTargets; ENSG00000186141; -.
DR PharmGKB; PA134870963; -.
DR VEuPathDB; HostDB:ENSG00000186141; -.
DR eggNOG; KOG2587; Eukaryota.
DR GeneTree; ENSGT00390000002799; -.
DR HOGENOM; CLU_023294_1_1_1; -.
DR InParanoid; Q9BUI4; -.
DR OMA; FETNECD; -.
DR OrthoDB; 809282at2759; -.
DR PhylomeDB; Q9BUI4; -.
DR TreeFam; TF103048; -.
DR PathwayCommons; Q9BUI4; -.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; Q9BUI4; -.
DR SIGNOR; Q9BUI4; -.
DR BioGRID-ORCS; 10623; 716 hits in 1093 CRISPR screens.
DR ChiTaRS; POLR3C; human.
DR EvolutionaryTrace; Q9BUI4; -.
DR GeneWiki; POLR3C; -.
DR GenomeRNAi; 10623; -.
DR Pharos; Q9BUI4; Tbio.
DR PRO; PR:Q9BUI4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BUI4; protein.
DR Bgee; ENSG00000186141; Expressed in calcaneal tendon and 177 other tissues.
DR ExpressionAtlas; Q9BUI4; baseline and differential.
DR Genevisible; Q9BUI4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 4.
DR InterPro; IPR013197; RNA_pol_III_RPC82-rel_HTH.
DR InterPro; IPR008806; RNA_pol_III_Rpc82_C.
DR InterPro; IPR039748; RPC3.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12949; PTHR12949; 1.
DR Pfam; PF08221; HTH_9; 1.
DR Pfam; PF05645; RNA_pol_Rpc82; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; DNA-binding; DNA-directed RNA polymerase;
KW Immunity; Innate immunity; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription.
FT CHAIN 1..534
FT /note="DNA-directed RNA polymerase III subunit RPC3"
FT /id="PRO_0000073963"
FT REGION 161..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 243
FT /note="H -> R (in dbSNP:rs1044697)"
FT /evidence="ECO:0000269|PubMed:9171375"
FT /id="VAR_019083"
FT MUTAGEN 51..52
FT /note="KK->EE: Strongly decreased ssDNA-binding. No effect
FT on interaction with POLR3F, POLR3G, nor with POLR3GL."
FT /evidence="ECO:0000269|PubMed:21358628"
FT MUTAGEN 312
FT /note="L->K: Loss of interaction with POLR3G and POLR3GL.
FT No effect on interaction with POLR3F."
FT /evidence="ECO:0000269|PubMed:21358628"
FT MUTAGEN 357
FT /note="R->E: Strongly decreased ssDNA-binding. No effect on
FT interaction with POLR3F, POLR3G, nor with POLR3GL."
FT /evidence="ECO:0000269|PubMed:21358628"
FT MUTAGEN 364..367
FT /note="RIFR->EIFE: Strongly decreased ssDNA-binding. No
FT effect on interaction with POLR3F, POLR3G, nor with
FT POLR3GL."
FT /evidence="ECO:0000269|PubMed:21358628"
FT MUTAGEN 389
FT /note="K->E: Strongly decreased ssDNA-binding. No effect on
FT interaction with POLR3F, POLR3G, nor with POLR3GL."
FT /evidence="ECO:0000269|PubMed:21358628"
FT MUTAGEN 445..449
FT /note="NLIER->ALIEE: Strongly decreased ssDNA-binding. No
FT effect on interaction with POLR3F, POLR3G, nor with
FT POLR3GL."
FT /evidence="ECO:0000269|PubMed:21358628"
FT MUTAGEN 466..470
FT /note="RVEAI->EVEAF: Mild decrease in ssDNA-binding. No
FT effect on interaction with POLR3F, POLR3G, nor with
FT POLR3GL."
FT /evidence="ECO:0000269|PubMed:21358628"
FT CONFLICT 85..86
FT /note="ML -> IV (in Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="SA -> CT (in Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..237
FT /note="KRPKYTTDNKEPIPDDGIYWQA -> RDQNILQITRXPFQMMGFIGRP (in
FT Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="S -> F (in Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> R (in Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="F -> C (in Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..389
FT /note="PAK -> LQ (in Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="E -> G (in Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 436..437
FT /note="LH -> FD (in Ref. 1; AAB63675)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="D -> E (in Ref. 3; CAB41919)"
FT /evidence="ECO:0000305"
FT HELIX 3..31
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2XUB"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 88..113
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:2XUB"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:7DU2"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 239..258
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:2XUB"
FT TURN 273..277
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:7DU2"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 338..358
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 360..371
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:7D59"
FT HELIX 428..456
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 458..472
FT /evidence="ECO:0007829|PDB:2XUB"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:7AE3"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:2XUB"
FT HELIX 493..529
FT /evidence="ECO:0007829|PDB:2XUB"
SQ SEQUENCE 534 AA; 60612 MW; 0E4CFEE295EE1A55 CRC64;
MTQAEIKLCS LLLQEHFGEI VEKIGVHLIR TGSQPLRVIA HDTGTSLDQV KKALCVLVQH
NLVSYQVHKR GVVEYEAQCS RVLRMLRYPR YIYTTKTLYS DTGELIVEEL LLNGKLTMSA
VVKKVADRLT ETMEDGKTMD YAEVSNTFVR LADTHFVQRC PSVPTTENSD PGPPPPAPTL
VINEKDMYLV PKLSLIGKGK RRRSSDEDAA GEPKAKRPKY TTDNKEPIPD DGIYWQANLD
RFHQHFRDQA IVSAVANRMD QTSSEIVRTM LRMSEITTSS SAPFTQPLSS NEIFRSLPVG
YNISKQVLDQ YLTLLADDPL EFVGKSGDSG GGMYVINLHK ALASLATATL ESVVQERFGS
RCARIFRLVL QKKHIEQKQV EDFAMIPAKE AKDMLYKMLS ENFMSLQEIP KTPDHAPSRT
FYLYTVNILS AARMLLHRCY KSIANLIERR QFETKENKRL LEKSQRVEAI IASMQATGAE
EAQLQEIEEM ITAPERQQLE TLKRNVNKLD ASEIQVDETI FLLESYIECT MKRQ
