YTH1_CANGA
ID YTH1_CANGA Reviewed; 209 AA.
AC Q6FTL0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=mRNA 3'-end-processing protein YTH1;
GN Name=YTH1; OrderedLocusNames=CAGL0G01694g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380953; CAG59361.1; -; Genomic_DNA.
DR RefSeq; XP_446434.1; XM_446434.1.
DR AlphaFoldDB; Q6FTL0; -.
DR SMR; Q6FTL0; -.
DR STRING; 5478.XP_446434.1; -.
DR EnsemblFungi; CAG59361; CAG59361; CAGL0G01694g.
DR GeneID; 2888311; -.
DR KEGG; cgr:CAGL0G01694g; -.
DR CGD; CAL0137715; CAGL0G01694g.
DR VEuPathDB; FungiDB:CAGL0G01694g; -.
DR eggNOG; KOG1040; Eukaryota.
DR HOGENOM; CLU_024513_1_2_1; -.
DR InParanoid; Q6FTL0; -.
DR Proteomes; UP000002428; Chromosome G.
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; IEA:EnsemblFungi.
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; 1.
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_0000238535"
FT ZN_FING 29..60
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 62..89
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 90..118
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 119..146
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 148..171
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 209 AA; 24557 MW; 1D9BA23F405E503C CRC64;
MGSVVHPDTE KYPFKFEPFL RQEYSFALDP DRPVCEDFNY KIGPSSCPNG VFCPKKHVLG
IFQNKIVCKH WLRGLCKKND NCEYLHEYNL RKMPECVFYA KNGFCTQSPE CQYLHIDPLS
KVPPCEDYEM GFCPKGSACE KRHIKKVLCQ RYINGFCPLG RRECDMEHPF FYIPDLSSPL
RIKKDEEINT RKRDEENERR LNAIINGEI