ID   YTH1_ASPOR              Reviewed;         255 AA.
AC   Q2URI6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=mRNA 3'-end-processing protein yth1;
GN   Name=yth1; ORFNames=AO090005000813;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE55829.1; -; Genomic_DNA.
DR   RefSeq; XP_001817831.1; XM_001817779.2.
DR   AlphaFoldDB; Q2URI6; -.
DR   SMR; Q2URI6; -.
DR   STRING; 510516.Q2URI6; -.
DR   EnsemblFungi; BAE55829; BAE55829; AO090005000813.
DR   GeneID; 5989776; -.
DR   KEGG; aor:AO090005000813; -.
DR   VEuPathDB; FungiDB:AO090005000813; -.
DR   HOGENOM; CLU_024513_1_1_1; -.
DR   OMA; CKYGAHP; -.
DR   Proteomes; UP000006564; Chromosome 1.
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   Pfam; PF00642; zf-CCCH; 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..255
FT                   /note="mRNA 3'-end-processing protein yth1"
FT                   /id="PRO_0000238533"
FT   ZN_FING         41..68
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         91..113
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         114..142
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         143..170
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         172..194
FT                   /note="C3H1-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          221..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   255 AA;  28944 MW;  BE14F17364840102 CRC64;
     MSAEVSHAAS QILASGSERD PSYNDFSFIP FLRNSFGFGL ACDVPVCKAY SEGHCPLGPA
     CPDRHPTPSR VTTSTTTASG LAPSTTHGSL VCKHFLKGLC KKGLKCEYLH EYNLRRMPEC
     QSFSRSGYCP NGDDCLYQHV REQARLPPCE HYDRGFCPLG PLCAKRHVRR RLCQYYLAGF
     CPEGKGCADA HARWIENLPK PSIRVEKTEE ELERERILIR EEQEREKERE REWRSERGRG
     GGFMRGRFRG RGRGL