ID   CFT1_DEBHA              Reviewed;        1342 AA.
AC   Q6BHK3;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Protein CFT1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=CFT1; OrderedLocusNames=DEHA2G17908g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382139; CAG90824.2; -; Genomic_DNA.
DR   RefSeq; XP_462318.2; XM_462318.1.
DR   AlphaFoldDB; Q6BHK3; -.
DR   SMR; Q6BHK3; -.
DR   STRING; 4959.XP_462318.2; -.
DR   EnsemblFungi; CAG90824; CAG90824; DEHA2G17908g.
DR   GeneID; 2905256; -.
DR   KEGG; dha:DEHA2G17908g; -.
DR   VEuPathDB; FungiDB:DEHA2G17908g; -.
DR   eggNOG; KOG1896; Eukaryota.
DR   HOGENOM; CLU_002414_2_1_1; -.
DR   InParanoid; Q6BHK3; -.
DR   OMA; PMTKFKL; -.
DR   OrthoDB; 360328at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF03178; CPSF_A; 1.
PE   3: Inferred from homology;
KW   mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..1342
FT                   /note="Protein CFT1"
FT                   /id="PRO_0000290629"
FT   REGION          156..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1342 AA;  152683 MW;  094BBD935C99F27E CRC64;
     MDAYHEFIQP TRVSQCIGCN FISPTSKSLI VGKATVLQVF EIITTETKTQ QYKLKLVEQF
     KLHGLITDIK AIRTVENSQL DYLLVSSKGA KMSLIKWDHH LNSISTVSLH YYENSIQSST
     YEKLTTTDLV VEPNNNCTCL RFKNLLTFLP FETLDEEEED DDDDEEMNGS SGSDKKATNK
     ENGNSNGEEV SELFESSFMI DGRTLDSRIG DIIDMQFLYN YREPTIAIIF SKAHAWAGNL
     PKVKDNINFI VLSLDLVTKA STTVLKIDNL PFDIDKIIPL PQPLNGSLLM GCNEIIHVDN
     GGITRRLALN QFTSSITTSL KNYHDQSDLN LKLENCSVKP IPNDNKVLMI LNNGDFYYIN
     FKIDGKTIKK FFVEKVSDLN YDDIQLTYPG EIATLDNNLM FISNKNGNNP LLELKYKNFE
     HVIVQENEEN SNPLDNEDEE DDLYEEDEVN KKISINKSSI EFIKHDELLN NGPISNFTLG
     HYSTDKFKSS LPNPNYKEVS IISNSGSHKQ GGLNILTPSV QPIIQSSLSF SQIHRMWTIN
     NEFLITSDDE NFKSEIFQLN KSFARLNSKD FINNESTIGM HELNNSEFFL QVTPKKIFVF
     NKKFKKIISF NKELKKYAND EIIYSTFNDE FLMVFFSSGE VVIYSINTYN ESFTKINIPK
     ILNDTIITTG YITNSSLLNA VSKDINLLIN KNRGTKRKHS GKNTSITSIN TPDSDLGPKS
     KTFILVTGDN RIVAFNRFHN ERCYQLNDVD KFTDHLSLGF FEPRDTYPDP FIKNIIFNEL
     GDEYSKDEYL TILTIGGEIL VYKLFFDGEN FKLVKEKDLI ITGAPDNAYS LGTTIERRLV
     YFPNVNGFTS IFVTGITPYY ISKTTHSVPR IFKFTKLPAV SFAPYSDDKI KNGLIYLDNS
     KNARICEIPV DFNYENNWPI KKIPIKESIK SVTYHELSNT FVISTYEEIP YDCLDEEGKP
     IVGVDKSKPS ANSYKGYIKL ISPYNWSVID TIELVDGEIG MNVQSMVLDV GSSTKKFKNK
     KELIVIGTGK YRMEDLSANG SFKIFEIIDI IPEPGKPETN HKFKEIHQED TKGAVTSICE
     ISGRFLVSQG QKIIIRDLQD DGVVPVAFLD TSVYVSEAKS FGNLLILGDS LKSIWLAGFD
     AEPFRMVMLG KDLQSLDVNC ADFIIKDEEI FILIADNNST LHLVKYDPED PTSSNGQRLI
     HKASFNINST PTCIRSIPKN EEINPSSTEV FQSIGSTIDG SFYTVFPINE ASYRRMYILQ
     QQITDKEYHF CGLNPRLNRF GGLSMTVNDT NTKPLLDYEV IRMFAKLNED RRKNLSMKVS
     SKNVYQDIWK DLIEFDHVLK NL