ID   YTH1_DEBHA              Reviewed;         223 AA.
AC   Q6BTT1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=mRNA 3'-end-processing protein YTH1;
GN   Name=YTH1; OrderedLocusNames=DEHA2C16126g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382135; CAG86470.2; -; Genomic_DNA.
DR   RefSeq; XP_458388.2; XM_458388.1.
DR   AlphaFoldDB; Q6BTT1; -.
DR   STRING; 4959.XP_458388.2; -.
DR   EnsemblFungi; CAG86470; CAG86470; DEHA2C16126g.
DR   GeneID; 2900760; -.
DR   KEGG; dha:DEHA2C16126g; -.
DR   VEuPathDB; FungiDB:DEHA2C16126g; -.
DR   eggNOG; KOG1040; Eukaryota.
DR   HOGENOM; CLU_024513_1_2_1; -.
DR   InParanoid; Q6BTT1; -.
DR   OMA; CKYGAHP; -.
DR   OrthoDB; 1472764at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:InterPro.
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..223
FT                   /note="mRNA 3'-end-processing protein YTH1"
FT                   /id="PRO_0000238537"
FT   ZN_FING         32..63
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         65..92
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         93..121
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         122..149
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         151..173
FT                   /note="C3H1-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          184..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   223 AA;  25709 MW;  0B668AC5D4EC15C6 CRC64;
     MLQLNQVIHP DTRNKRFKFE PFLLKEYNFG LDPDRPVCQF YNPSNPNNSC PNGSLCPHKH
     VSSMYSNKIV CKHWLRGLCK KNDHCEFLHE YNLRKMPECL FYSKNGFCTQ TPECLYLHVD
     PQSKIPPCSS YEKGFCPDGP KCANRHIRKI MCPLWLTGFC PKGAECDYTH PRFEAIIDRL
     RIKPDEDAVE EKEKVANGSD KEDQNMADAT SNGNTEEKDE SGP