YTH1_ASHGO
ID YTH1_ASHGO Reviewed; 209 AA.
AC Q758T3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=mRNA 3'-end-processing protein YTH1;
GN Name=YTH1; OrderedLocusNames=AEL331W;
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 [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 [2]
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: Component of the cleavage factor I (CF I) involved in pre-
CC mRNA 3'-end processing. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CPSF4/YTH1 family. {ECO:0000305}.
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DR EMBL; AE016818; AAS52353.1; -; Genomic_DNA.
DR RefSeq; NP_984529.1; NM_209882.1.
DR AlphaFoldDB; Q758T3; -.
DR SMR; Q758T3; -.
DR STRING; 33169.AAS52353; -.
DR EnsemblFungi; AAS52353; AAS52353; AGOS_AEL331W.
DR GeneID; 4620699; -.
DR KEGG; ago:AGOS_AEL331W; -.
DR eggNOG; KOG1040; Eukaryota.
DR HOGENOM; CLU_024513_1_2_1; -.
DR OMA; CKYGAHP; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:EnsemblFungi.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR InterPro; IPR045348; CPSF4/Yth1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR23102; PTHR23102; 1.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 3: Inferred from homology;
KW Metal-binding; mRNA processing; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..209
FT /note="mRNA 3'-end-processing protein YTH1"
FT /id="PRO_0000238531"
FT ZN_FING 28..59
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 61..88
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 89..117
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 118..145
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 147..169
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 209 AA; 24426 MW; 599695317CDD6B5F CRC64;
MSLVHPDTSN YPFRFAPFLR QEYSFSLDPD RPVCQYYNSK EGASSCPNGT LCPNKHVLPI
FQNKIVCKHW LRGLCKKNDQ CEYLHEYNLR KMPECVFFTK NGYCTQSPEC QYLHIDPTSK
VQQCEDYRMG FCPLGTACPC KHVKKIICPK YVTGFCPLGR DCDWEHPPFY VPNELSKIRI
KRDDEINTKK LDEEKERRLN AIINGELVI
