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Database: UniProt
Entry: M7UBB5_BOTF1
LinkDB: M7UBB5_BOTF1
Original site: M7UBB5_BOTF1 
ID   M7UBB5_BOTF1            Unreviewed;       629 AA.
AC   M7UBB5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=BcDW1_7457 {ECO:0000313|EMBL:EMR83933.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR83933.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
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; KB707975; EMR83933.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7UBB5; -.
DR   STRING; 1290391.M7UBB5; -.
DR   HOGENOM; CLU_023294_0_0_1; -.
DR   Proteomes; UP000012045; 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; 1.
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; 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          124..462
FT                   /note="RNA polymerase III Rpc82 C -terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05645"
FT   REGION          93..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  71064 MW;  AD4A600597F215BB CRC64;
     MNALKRHTQL TTRQLKLGLT VLVRQNLVYH NSEGSDTHYE ANIDAAYALV RSGKILEIAE
     ERFGSVAAEI MGQLVLLGHA KISDIIAELN KNHEPHANGN SNETNGATNG NGVHSYPSGQ
     LNHTLIQLLE EGFIQPVGQN MFRSPTDSYN AVEKALLQDS YGGATRGTKQ KDELRMRIRG
     QLQELRAQVP NWKPVGYNRS STNGHTNDIA SKRRRLSHSG GATNGYDFGD DESSKLDGNL
     VLRINHEKCT VFMRNRRLVE LANSRIGVTT SYIYAELLRL MAEQIPRCRP DPRIDDAVDD
     ADGPSIIITT QELTDALSKT INVSTGIGKA TSQKIDTSRL DKLQNGRKRK AQDEAEVEGV
     ASSDEESEDD HKPFTNGNGH AMDVDEDDPF SDQPGANTSK RAVTFKDRDR TPPPTESRQA
     RMMHVMSHLQ LLAADDCQLL RKCGARQMGE WTVDFERVID RLRESELDSI IYENFGQIGH
     RLVRVMRKMG KLEEKHIAKL ALIKQQDSRT TLVNMQMHGM VDIQEVPRDT GRMIVRTIHL
     WFCDEDRVTS LLLDRTYKAM SRCLQRLDVE KRRKANIIAL SERTDVQGQE EAFLRPEQMN
     QLREIRAKEE DLLGQICRLD ELVGIFQDY
//
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