TRF5_ASHGO
ID TRF5_ASHGO Reviewed; 626 AA.
AC Q9HFW3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Poly(A) RNA polymerase protein 1;
DE EC=2.7.7.19 {ECO:0000250|UniProtKB:P53632};
DE AltName: Full=Topoisomerase 1-related protein TRF5;
GN Name=TRF5; OrderedLocusNames=AEL207W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11082049; DOI=10.1242/jcs.113.24.4563;
RA Ayad-Durieux Y., Knechtle P., Goff S., Dietrich F.S., Philippsen P.;
RT "A PAK-like protein kinase is required for maturation of young hyphae and
RT septation in the filamentous ascomycete Ashbya gossypii.";
RL J. Cell Sci. 113:4563-4575(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Catalytic subunit of the TRAMP5 complex which has a poly(A)
CC RNA polymerase activity and is involved in a post-transcriptional
CC quality control mechanism limiting inappropriate expression of genetic
CC information. Polyadenylation is required for the degradative activity
CC of the exosome on several of its nuclear RNA substrates like cryptic
CC transcripts generated by RNA polymerase II and III, or hypomethylated
CC pre-tRNAi-Met. Polyadenylates RNA processing and degradation
CC intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains
CC lacking a functional exosome. TRF5 is also required for proper nuclear
CC division in mitosis and sister chromatid cohesion. Involved in the
CC regulation of histone mRNA levels. May mediate mitotic chromosome
CC condensation (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000250|UniProtKB:P53632};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; AF286114; AAG17722.1; -; Genomic_DNA.
DR EMBL; AE016818; AAS52478.1; -; Genomic_DNA.
DR RefSeq; NP_984654.1; NM_210007.1.
DR AlphaFoldDB; Q9HFW3; -.
DR SMR; Q9HFW3; -.
DR STRING; 33169.AAS52478; -.
DR EnsemblFungi; AAS52478; AAS52478; AGOS_AEL207W.
DR GeneID; 4620836; -.
DR KEGG; ago:AGOS_AEL207W; -.
DR eggNOG; KOG1906; Eukaryota.
DR HOGENOM; CLU_013572_5_0_1; -.
DR InParanoid; Q9HFW3; -.
DR OMA; FGSCATD; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0031499; C:TRAMP complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071044; P:histone mRNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0071050; P:sno(s)RNA polyadenylation; IEA:EnsemblFungi.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IEA:EnsemblFungi.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR045862; Trf4-like.
DR PANTHER; PTHR23092; PTHR23092; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Magnesium; Manganese; Metal-binding; Mitosis;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..626
FT /note="Poly(A) RNA polymerase protein 1"
FT /id="PRO_0000120315"
FT DOMAIN 387..448
FT /note="PAP-associated"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 626 AA; 69752 MW; CF3F60F3FD753F44 CRC64;
MMTASVAGNR SGRSGNIARE RSNRSRGAQK SDKERNLSKG SSRPKSNSSR VKKMRKSSLS
KVQKNFAVFN DSAEHENKYE TLAVAEADEK EVILLDEEED TAMTTETKGV HAEETANVTG
AEGVNAAANA LDDNQDFIGF SDSEEEVASG EENGDADYAV EDAEDESSEP LPTNADYPWI
QNHDHSRQRE IADWLTLEIK DFVSYISPNK TEIQLRNDAL KRIRDAVQDF WPDANLHCFG
SYATDLYLPG SDIDCVVNSK SGDKDNKNAL YSLASYLKRN GLATQVSVIA KARVPIIKFV
EPASQIHIDL SFERTNGVEA AKIIRGWLHD TPGLRELVLI VKQFLHARRL NDVHIGGLGG
FSIICLAYSF LKLHPRIICR DIEPLQNLGV LLIDFFELYG KNFGYDDVGI AVSEGDASYI
NKKEYPELTR NLRGTFNLVI QDPGDPANNI SRGSFNIRDI KKAFAGAFEL LTNRCFELDA
ATFKHRVGKS ILGNVIKYRG AKRDFKDERA LIVNKAIQEN EEFHQRRGRI VHRDTAEFIN
ISDDDDYELQ PPPKRARVPA PAPAPADNVV VLDDPADDYV PAQPVDKLMG LDDTDDYLPA
PASPTDTPKL DKAAKRNYWL SKGQTM
