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RPC3_ASPNC
ID   RPC3_ASPNC              Reviewed;         627 AA.
AC   A2QUS7;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=DNA-directed RNA polymerase III subunit rpc3;
DE            Short=RNA polymerase III subunit C3;
GN   Name=rpc82; Synonyms=rpc3; ORFNames=An09g06640;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; AM270211; CAK40457.1; -; Genomic_DNA.
DR   RefSeq; XP_001393979.1; XM_001393942.1.
DR   AlphaFoldDB; A2QUS7; -.
DR   SMR; A2QUS7; -.
DR   PaxDb; A2QUS7; -.
DR   EnsemblFungi; CAK40457; CAK40457; An09g06640.
DR   GeneID; 4984201; -.
DR   KEGG; ang:ANI_1_870084; -.
DR   VEuPathDB; FungiDB:An09g06640; -.
DR   HOGENOM; CLU_023294_0_0_1; -.
DR   Proteomes; UP000006706; Chromosome 1L.
DR   GO; GO:0005666; C:RNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 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   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12949; PTHR12949; 1.
DR   Pfam; PF08221; HTH_9; 1.
DR   Pfam; PF05645; RNA_pol_Rpc82; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription;
KW   Zinc.
FT   CHAIN           1..627
FT                   /note="DNA-directed RNA polymerase III subunit rpc3"
FT                   /id="PRO_0000351025"
FT   REGION          131..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..575
FT                   /note="Leucine-zipper"
FT   COMPBIAS        142..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..288
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..419
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  71806 MW;  28B458894442B68A CRC64;
     MTSQYAAELC ALLVEDNFGE LFARIFSTLQ RYDRLSLPRL KFYSRLSDRQ LRHGLSAMIQ
     HHLVYHYTSY DDGVTYYEPN LQAAYYLVRS GKILEFIEER LGKYAATLME TIMFLGHAQV
     GYLETLPELQ PAPPKANGVK QEAEGGESEE QMNGDDVHTS DQPALLHPTL KALASHGYIF
     RVRDAQFQSY ADNALDAERA IKSRPDVKQL KGKKLDETVL EGTVTLLKER LDGDLTRGLM
     HNGLPRGAKR RHGTGSADAT NKKARMDYVD ADEDEDEEEN EWSDDEMGGD TTPMELAIVV
     RVNYEKLDVA LRNRRFLDLA EMNSSPVTAQ VYEGLLRRIE YQTKQCRDSA EIPREGEEGE
     QYSVPIALSA VTEEVDPQLD LAGSIGPMEI SQAINKRGKR PLEDSVNGTD REGSEAPSRT
     YEVDQHLSLL SQPPYNLTSK RVLSGLITWT VEFRHLARKL RHLELERMIE ARYGDVALRV
     IRVLHAKGKL DEKRLQEISL LPFKDLRQVL ASMQSGGFVD LQEVPRDAQR QPSRTIYLWY
     YDPDRIRSSI LEDTYKAMSR CMQRLRFERN RLKEFLEKTE RSDVKGNEER YLSQAELTLL
     EQWKAKEALL LGEVARLDEM VAVMRDY
 
 
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