ID   YTH1_NEUCR              Reviewed;         317 AA.
AC   Q7SGR2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=mRNA 3'-end-processing protein yth-1;
GN   Name=yth-1; ORFNames=NCU08353;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002236; EAA36020.1; -; Genomic_DNA.
DR   RefSeq; XP_965256.1; XM_960163.2.
DR   AlphaFoldDB; Q7SGR2; -.
DR   STRING; 5141.EFNCRP00000006432; -.
DR   EnsemblFungi; EAA36020; EAA36020; NCU08353.
DR   GeneID; 3881396; -.
DR   KEGG; ncr:NCU08353; -.
DR   VEuPathDB; FungiDB:NCU08353; -.
DR   HOGENOM; CLU_024513_1_0_1; -.
DR   InParanoid; Q7SGR2; -.
DR   OMA; CKYGAHP; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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; 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   Pfam; PF00642; zf-CCCH; 2.
DR   SMART; SM00356; ZnF_C3H1; 4.
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..317
FT                   /note="mRNA 3'-end-processing protein yth-1"
FT                   /id="PRO_0000238541"
FT   ZN_FING         51..78
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         93..120
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         121..149
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         150..177
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         179..202
FT                   /note="C3H1-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   317 AA;  35200 MW;  5316EDA3B8D5491B CRC64;
     MATTTQTTTN SLPSGAGGPQ QLVTQMLNHT APHYTFSFTP FLQRTYQHSL PADRPICKAY
     ASGNCPLKSH CPERHVTASS QNTHGGGNTF SGGFGSLVCK HWLRGLCKKG ESCEFLHEYN
     LRKMPECNFF VRNGYCSNGD ECLYLHIDPL SRLPPCPHYE RGFCPLGPRC DKKHFRRKLC
     LYYLAGFCPD GKGCKEGAHP RWTADKDMEK PRAKGEGDQM LLQQQQQQQQ QQHMGDANGM
     GGGMAQATGA NEYMDRERER DRDNREREMM MQGRDRDGGG HDRHKDRFGG GGGGGGGGRG
     RGGWRGRGRG GFRGKGH