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Database: UniProt
Entry: A0A1L9SCF5_9EURO
LinkDB: A0A1L9SCF5_9EURO
Original site: A0A1L9SCF5_9EURO 
ID   A0A1L9SCF5_9EURO        Unreviewed;       635 AA.
AC   A0A1L9SCF5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA-directed RNA polymerase III subunit RPC3 {ECO:0000256|RuleBase:RU367076};
DE            Short=RNA polymerase III subunit C3 {ECO:0000256|RuleBase:RU367076};
GN   ORFNames=ASPZODRAFT_17782 {ECO:0000313|EMBL:OJJ44866.1};
OS   Penicilliopsis zonata CBS 506.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicilliopsis.
OX   NCBI_TaxID=1073090 {ECO:0000313|EMBL:OJJ44866.1, ECO:0000313|Proteomes:UP000184188};
RN   [1] {ECO:0000313|Proteomes:UP000184188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 506.65 {ECO:0000313|Proteomes:UP000184188};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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. {ECO:0000256|ARBA:ARBA00025127,
CC       ECO:0000256|RuleBase:RU367076}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. {ECO:0000256|ARBA:ARBA00011206,
CC       ECO:0000256|RuleBase:RU367076}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU367076}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|RuleBase:RU367076}.
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DR   EMBL; KV878346; OJJ44866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9SCF5; -.
DR   STRING; 1073090.A0A1L9SCF5; -.
DR   VEuPathDB; FungiDB:ASPZODRAFT_17782; -.
DR   OrthoDB; 1429291at2759; -.
DR   Proteomes; UP000184188; Unassembled WGS sequence.
DR   GO; GO:0005666; C:RNA polymerase III complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
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:SF0; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC3; 1.
DR   PANTHER; PTHR12949; RNA POLYMERASE III DNA DIRECTED -RELATED; 1.
DR   Pfam; PF08221; HTH_9; 1.
DR   Pfam; PF05645; RNA_pol_Rpc82; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU367076}; Nucleus {ECO:0000256|RuleBase:RU367076};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184188};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU367076}.
FT   DOMAIN          8..64
FT                   /note="RNA polymerase III subunit RPC82-related helix-turn-
FT                   helix"
FT                   /evidence="ECO:0000259|Pfam:PF08221"
FT   DOMAIN          172..468
FT                   /note="RNA polymerase III Rpc82 C -terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05645"
FT   REGION          240..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  72820 MW;  C89905C05F6D572C CRC64;
     MTSQYATELC SLLIEDNFGE LFARIFSTLQ RYDRLTLPRL RFYSRLSDRQ LHHGLAAMVQ
     HHLIYHYTSL EDGNTYYETN LQSAYYLVRS GKILEMIEDR LGKYAATVMS TIMFLGHAQI
     AHLETLPELK PQRSHANGVG EEMKEEAEGQ ANGVDGEHEL DELVENAAIH STLKALAAHG
     YVIQVRDAQF QSPNDNVLDA QRVLKARPDV KEMKGKKQEQ FLLENTERIV KERTDGDLSR
     GLMFNGVPQG VKRKHSQKPN EERREYVDID EDEENEWSDD DFGGNSPMDS NLVVRVNYPK
     LDVALRNRRL VELVDQESSS ATAQVYDCLL RRIEYQTPRC RDIAEIPREG EESEQYSVPI
     RLSALVDDID PYLDLSGSIG PMEVPQGPAR RGKRPLENGV HGDTDDREGQ PSSTTNGTSS
     SSSGASRTYE VDQHLCLLAQ PPYNFTSKRM IGGLINWTVE YRHLARKLRH TELERIIEAR
     YGDVALRVVR VLHAKGKLDE KRLQEISLLP FKDLRQVLAS MQAGGFVDLQ EVPRDAQRQP
     SRTIYLWFYD PDRVAAGILE DTYKAMSRCL QRIRFERARL REFLDKTERS DVKGNEERYL
     SEGELKTLHQ WRAKEALLLG EVSRLDDMVA VFRDY
//
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