ID W6QND5_PENRF Unreviewed; 650 AA.
AC W6QND5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 Name=rpc82 {ECO:0000313|EMBL:CDM35639.1};
GN ORFNames=PROQFM164_S04g000520 {ECO:0000313|EMBL:CDM35639.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM35639.1};
RN [1] {ECO:0000313|EMBL:CDM35639.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM35639.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792018; CDM35639.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QND5; -.
DR STRING; 1365484.W6QND5; -.
DR OMA; KHRFVRH; -.
DR OrthoDB; 1429291at2759; -.
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 Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU367076}.
FT DOMAIN 9..66
FT /note="RNA polymerase III subunit RPC82-related helix-turn-
FT helix"
FT /evidence="ECO:0000259|Pfam:PF08221"
FT DOMAIN 186..480
FT /note="RNA polymerase III Rpc82 C -terminal"
FT /evidence="ECO:0000259|Pfam:PF05645"
FT REGION 138..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 74138 MW; 1751E80127FB7F2E CRC64;
MMMSQCSTEL CMLLIEDNFG ELFARIFTVL QRYERLTLPR LRFYARLTDR QLHHGLSAMI
QHHLIYHFTS LDDGNTYYEA NPQAAYSLVR SGKILQLVET RLGEYAAQVL EAIMSLGHSS
IAHLETLPEL QSKRQRIPNG VNQGENTVEN TVEDTVDGNG EKEEDSAAPN GNHVVREKPV
HLHPTLKSLA SHGYIHRLRE AHFQSPNDNW IDASRIIASR PDVKQMKGKQ QATEIEEKAK
DLVKERTEGD LSRGLIYNGL PQGAKRKRDH GNSESNKQAP NGTNGVNGDH VEDEGEEDND
WSEDEDGVDS IPMDSNLIVR VNYEKLDVAL RNTRFLDLAK QDAPSASVEI YDCLLRRIEY
QTARCRDSYE IPREGEEGEQ YSAPIQLSSI VEDVDPNLDL TGCIGPMEPS TVLNRGGKRP
LDDETNGVNG DEHEDEPSGQ NRAYGIDQHL SILSQPPLNL TTKHVISGLP TWRVAFRGLA
RKLRHLELER MIESRYGDVA LRVVRVLHAK GKLDEKRLQE ISLLPFKDLR QTLASMQTGG
FVDLQEVPRD AQRQPSKTIY LWYYDPDRVC SSMLEDTYKA MSRCLQRIKF ERGRERDFLE
KTERTDVKGH EEEFLSEAEL EHLRNWKAKE ALLLAEVSRL DDMVAVFRDY
//
