ID   CFT1_ASHGO              Reviewed;        1305 AA.
AC   Q75EY8;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Protein CFT1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=CFT1; OrderedLocusNames=AAL060W;
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: RNA-binding component of the cleavage and polyadenylation
CC       factor (CPF) complex, which plays a key role in polyadenylation-
CC       dependent pre-mRNA 3'-end formation and cooperates with cleavage
CC       factors including the CFIA complex and NAB4/CFIB. Involved in poly(A)
CC       site recognition. May be involved in coupling transcription termination
CC       and mRNA 3'-end formation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CFT1 family. {ECO:0000305}.
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DR   EMBL; AE016814; AAS50306.1; -; Genomic_DNA.
DR   RefSeq; NP_982482.1; NM_207835.2.
DR   AlphaFoldDB; Q75EY8; -.
DR   SMR; Q75EY8; -.
DR   STRING; 33169.AAS50306; -.
DR   PRIDE; Q75EY8; -.
DR   EnsemblFungi; AAS50306; AAS50306; AGOS_AAL060W.
DR   GeneID; 4618423; -.
DR   KEGG; ago:AGOS_AAL060W; -.
DR   eggNOG; KOG1896; Eukaryota.
DR   HOGENOM; CLU_002414_0_0_1; -.
DR   InParanoid; Q75EY8; -.
DR   OMA; RDTCCIV; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:EnsemblFungi.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IEA:EnsemblFungi.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
KW   mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..1305
FT                   /note="Protein CFT1"
FT                   /id="PRO_0000290620"
FT   REGION          147..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1305 AA;  147305 MW;  36704840AC28A6D4 CRC64;
     MNVFDEVINA TVVNNSVTGH FTTTLREELI ITRTNLLSVL HKDNEGRLVL AYEWKLSGRV
     HGLSLVPHKS GLGRLAVLTG RGRVSIVRFD AENQTLETES LHYYDAKFEE LSALTVGAAP
     RLEQEPAARC LLVHNGDCLA VLPLRGHEEE GEEAEEEEEH PAKRARTDAD GRLVGASTVM
     PASHLHSDIK NVKDMRFLRG LNKSAVGVLY QPQLSWCGNE KLTRQTMKFI ILSLDLDDEK
     STVINMLQGL PNTLHTIIPL SNGCVLAGVN ELLYVDNTGA LQGAISLNAF SNSGLNTRIQ
     DNSKLQAFFE QPLCYFATQS NGRDILLLMD EKARMYNVII EAEGRLLTTF NCVQLPIVNE
     IFKRNMMPTS ICGNMNLETG SLFIGFQSGD AMHVRLNNLK SSLEHKGTVS ETLETDEDYM
     ELYGNNAEKE KKNLETESPF DIECLDRLLN IGPVTSLAVG KASSIEHTVA KLANPNKDEL
     SIVATSGNGT GSHLTILENT IVPTVQQALK FISVTQIWNL KIKGKDKYLV TTDSSQTRSD
     IYSIDRDFKP FKAADFRKND TTVSTAVTGG GKRIVQVTSK GVHLFDINFK RMMTMNFDFE
     VVHVCIKDPF LLLTNSKGDI KIYELEPKHK KKFVKTVLPD ALKEIIITFG VILESNMCNK
     YINGLEKSEE PQLLFTFVTA DNQIVFFTKD HNDRIFQLNG IDDFRQKLFI STYQLPEDIN
     PDPSIKQVII SRLGHKHKQE YLTILTFGGE VYLYRKCIDN PDRFIKCDHE LLITGAPENA
     YPKGVQGVER VAHYIEDYNG YSVIFITGTV PYIIIKEDNS VPRIFPFANI TLVSMTRWGE
     NSVMCVDDVK NARIMTLNLD RDRYYGNKMS LAKIYLEDPL EDFQTLNNIT YHERTQTFIV
     SYAKSIDYVA LSEEDEPLVG YNPDKIHAMG FQSGIILLSP KSWEIIDKIE YGKNSLINDM
     RTMMIQLNSN TKRRREYLVV GNTYVRDEDI GGTGSFYLYD ITEVVPEPGK PDTNYKFKDI
     FQEDIRGTVS TVCEISGRFM ISQSSKAMVR DIQEDNSVVP VAFLDMPVFI TDAKSFGNLM
     IIGDSMQGFS FLGFDAEPYR MLTLGKSVSK LETMCVEFLV NNGDVYFLVT DRNNLMHVLK
     YAPDEPNSLS GQRLVHCTSF NLHSTNTCMR LIKKNDEFGK VSRGFGIYMP SFQCIGSQAD
     GTIFKVVPLS EASYRSLYLI QQQLIDKEVQ LCGLNPRMER LENPFYQMGH ILRPMLDFTV
     LKRFATLSIP TRMTMASKAG RQAHAEIWRD LIDIEYSLTS LNKIT