ID   CFT1_YARLI              Reviewed;        1269 AA.
AC   Q6C740;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Protein CFT1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=CFT1; OrderedLocusNames=YALI0E03982g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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: 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; CR382131; CAG79101.1; -; Genomic_DNA.
DR   RefSeq; XP_503522.1; XM_503522.1.
DR   AlphaFoldDB; Q6C740; -.
DR   SMR; Q6C740; -.
DR   STRING; 4952.CAG79101; -.
DR   PRIDE; Q6C740; -.
DR   EnsemblFungi; CAG79101; CAG79101; YALI0_E03982g.
DR   GeneID; 2912174; -.
DR   KEGG; yli:YALI0E03982g; -.
DR   VEuPathDB; FungiDB:YALI0_E03982g; -.
DR   HOGENOM; CLU_002414_2_1_1; -.
DR   InParanoid; Q6C740; -.
DR   OMA; PMTKFKL; -.
DR   Proteomes; UP000001300; Chromosome E.
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   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   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
PE   3: Inferred from homology;
KW   mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..1269
FT                   /note="Protein CFT1"
FT                   /id="PRO_0000290636"
FT   REGION          393..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..415
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1269 AA;  141198 MW;  1DE6648174AF0DE2 CRC64;
     MHIFKNLTEP TAVTHSLSCN FTGERNLVLV KGSQLLQIFR YKDDIPTKDE APRLELITEY
     YLDGTVTGVT RIKTIDNYDL DSLYISVKHA KAVIVAWNAS SFTIDTKSLH YYEKGLVESN
     FFEPECSSVA VSDEANSFYT CLLFQNDRMA FLPIIEKGLD DDEMPESGQV FDPSFIVKAS
     RLDKRIENVM DICFLHEYRE TTMGILFQPK RAWVGMKNIL KDTVSYAIVS VDVHQKNSTV
     IGTLNGLPVD AQKVIPLPAP LGGSLIICAN TILYIDSSAS YTGVMVNNTH RQNSDLIVSR
     DQSTLDLRLE GAEVCFIQEL GNTALLVTED GQFFSLLFNK DGRRVASLEL RPIEPDNFIL
     SQPSSVAAGP DGTIFLGSRA GDSLLVKWYH GEPESQPEET LDDGNESDDD LYGGDTAQTE
     DTTNRPLKLR LADRMLGMGP MQSLALGKNR GSQGVEFVTT TGVGANSALA ILTSALMPYK
     RKSLYKDMPG GQFWSVPVRF EEEGEVAKSR TYVVSSDSEN SYLYYVDAAG VIEDVSLSTK
     KKKTKKHFVS NVTTIFSSSM LDSALLQVCL ETVNIYDAKI GQPHKYSLPQ GTTAVEARVL
     GNYVLVLLSD GQVKILEAVS INKRPFLKAA QVSIEPASES KAIGIYATDS SLTFGAPSKK
     RTRQGSPAQD SRPVVVVCYA DGSLLLQGLN SDDRLILDAS DLSGFIKEKD GQLYDAPLEL
     VDIALSPLGD DHILRDYLVL LTPQQLVVYE PYHYNDKLRF RKIFLERTPT INSDRRLTQV
     PLINGKHTLG VTGETAYILV KTLHTSPRLI EFGETKGAVA FTSWDGKFAY LTQAGEVAEC
     RFDPSFSLET NWPVKHVQLC GETISKVTYH ETMDVYVIAT HKTVPHVVRD EDDEVIESLT
     PDIMPATTYQ GAIRIVNPYS WTVIDSYEFE MPAEAALCCE SVKLSISDRK SQKREVVAVG
     TSILRGEDLA ARGALYLFDV IEIVPEKERP ETNRRLKKLV QDRVRGAFTA VCEVSGRLLA
     VQGQKLLVQA LQDDLTLVPV AFLDMQTYVA VAKSLNSMLL LGDATRSVQF VGFSMDPYQM
     IPFARDLQRV LVTTCDFAIE GENLTFVVAD LQKRLHILEY DPDDPQSYSG ARLLRRSVFY
     SGKVIDSSAM VPINEDRFMV IGVCSDGSVT DVVPCPEDAY RRLYAIQTQI TDKEAHVCGL
     HPRAYRYDPI LPGTGNSPHR PILDGHTLIR FANLPRNKQN VYANRLGQRY QQLIWKDLEL
     ISDLFKKCI