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Database: UniProt
Entry: A0A091DFU4_FUKDA
LinkDB: A0A091DFU4_FUKDA
Original site: A0A091DFU4_FUKDA 
ID   A0A091DFU4_FUKDA        Unreviewed;       534 AA.
AC   A0A091DFU4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=H920_07574 {ECO:0000313|EMBL:KFO31024.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO31024.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO31024.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO31024.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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       Specific core component of RNA polymerase III which synthesizes small
CC       RNAs, such as 5S rRNA and tRNAs. {ECO:0000256|RuleBase:RU367076}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. {ECO:0000256|RuleBase:RU367076}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU367076}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RPC3/POLR3C RNA polymerase
CC       subunit family. {ECO:0000256|ARBA:ARBA00007206,
CC       ECO:0000256|RuleBase:RU367076}.
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DR   EMBL; KN122330; KFO31024.1; -; Genomic_DNA.
DR   RefSeq; XP_010627803.1; XM_010629501.2.
DR   RefSeq; XP_010627804.1; XM_010629502.2.
DR   AlphaFoldDB; A0A091DFU4; -.
DR   STRING; 885580.ENSFDAP00000022762; -.
DR   Ensembl; ENSFDAT00000009536; ENSFDAP00000022762; ENSFDAG00000021078.
DR   GeneID; 104865789; -.
DR   CTD; 10623; -.
DR   eggNOG; KOG2587; Eukaryota.
DR   OMA; QHNLLWH; -.
DR   OrthoDB; 2875034at2759; -.
DR   Proteomes; UP000028990; 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; 6.10.140.1450; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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: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.
DR   Pfam; PF20912; RPC3_helical; 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:UP000028990};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU367076}.
FT   DOMAIN          7..66
FT                   /note="RNA polymerase III subunit RPC82-related helix-turn-
FT                   helix"
FT                   /evidence="ECO:0000259|Pfam:PF08221"
FT   DOMAIN          146..345
FT                   /note="RNA polymerase III Rpc82 C -terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05645"
FT   REGION          197..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  60685 MW;  3240DE431BE861EA CRC64;
     MTQAEIKLCS LLLQEHFGEI VEKIGVHLIR TGSQPLRVIV HDTGTSLDQV KKALCVLIQH
     NLVMYQVHKR GVVEYEAHCS RVLRMLRYPR YIYTTKALYG DTGELIIEEL LLNGKMTMSA
     VVKKVADRLT ETVEDGKTMD YAEVSNTFMQ LADTRFVQRC PMVHTPENSD TGPPPPAPNL
     VINEKDMYLV PKLSLIGKGK RRRSSDEDAA GEPKAKRPKH PTDNKEPIPD DGIYWQANLD
     RFHQHFRDQA IVSAVANRMD QTSSEIVRAM LRMSEVTTSS DAPFTQPLSS NEIFRSLPVG
     YNISKQVLDQ YLTLLADDPL EFVGKSGDSG GGMYVINFCK ALASLATATL ESVIQERFGS
     RCARIFRLVL QKKHLEQKQV EDFAMIPAKE AKDMLYKMLS ENFISLQEIP KTPDHAPSRT
     FYLYTVNILS AARMLLHRCY KSVTNLIERR QFETKENKRL LEKSQRVEAI IASVQATGAE
     EAQLQEIEEM ITAPERQQLE TLKRNVNKLD ASEIQVDETI FLLESYIEST MKRQ
//
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