ID   CFT1_CANGA              Reviewed;        1361 AA.
AC   Q6FSD2;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Protein CFT1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=CFT1; OrderedLocusNames=CAGL0H01463g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380954; CAG59795.1; -; Genomic_DNA.
DR   RefSeq; XP_446862.1; XM_446862.1.
DR   AlphaFoldDB; Q6FSD2; -.
DR   SMR; Q6FSD2; -.
DR   STRING; 5478.XP_446862.1; -.
DR   EnsemblFungi; CAG59795; CAG59795; CAGL0H01463g.
DR   GeneID; 2888551; -.
DR   KEGG; cgr:CAGL0H01463g; -.
DR   CGD; CAL0130563; CAGL0H01463g.
DR   VEuPathDB; FungiDB:CAGL0H01463g; -.
DR   eggNOG; KOG1896; Eukaryota.
DR   HOGENOM; CLU_002414_0_0_1; -.
DR   InParanoid; Q6FSD2; -.
DR   OMA; PMTKFKL; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
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   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; 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..1361
FT                   /note="Protein CFT1"
FT                   /id="PRO_0000290626"
FT   REGION          455..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..474
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1361 AA;  154576 MW;  3B5A42107C82935A CRC64;
     MNVYDDVIDP TVVSHSVCGH FTTTDYLELI VIRTDVLSIY KPIRSGRLYL MEEHKLSGRI
     NDVALIPKHS NGSNGNGINL SYLLLSTGVA KLSLLMYNNM TSSIETISLH FYEDKFESAT
     MLDLARNSQL RIEPNGNYAM LFNNDVLAIL PFYTGINEDE DEDYINNDKS KINDNSKKSL
     FKRKKGKTQN NKVTHPSIII NCSELGPQIK NIKDIQFLCG FTKSTIGVLY QPQLAWCGNS
     QLVPLPTNYA IISLDMKFSI DATTFDKAII SEISQLPSDW HTIAPTLSGS LILGVNEIAF
     LDNTGVLQSI LTLNSYSDKV LPKVRVIDKS SHEVFFNTGS KFALIPSNEN ERSVENILLF
     DENGCIFNVD LKSEGRLLTQ FNITKLPLGE DVLSQKSNPS SVSIIWADGR LDTYTIFIGF
     QSGDATMLKL NHLHSAIEVE EPTFMKDYVN KQASAAYNNE DDDDDDDDFN LYSDEENDQV
     NNKNDRTFGT NESNEPFTAQ ELMELRNIGP INSMCVGKVS SIEDNVKGLP NPNKQEISIV
     CTSGYGDGSH LNAILASVQP RVEKALKFIS ITKIWNLHIK GKDKFLITTD STQSQSNIYE
     IDNNFSQHKQ GRLRRDATTI HIATIGDNKR IVQVTTNHLY LYDLTFRRFS TIKFDYEVVH
     VSVMDPYVLI TLSRGDIKVF ELENRNKKKF VKVPLPEILT EMVITSGLIL KSNMCNEFLS
     GIGKSTIEQL LFTFVTADNQ IIFFTKDHND RIFQLNGIDQ LQDSLYISTY QLPDEIIPDP
     SIKQIMINKL GNNSKDEYLT ILTFGGEIYQ YKKSRSRHSR FYRNVGRNDH PITGAPDNAY
     PKGVSGIERI MHYIPNFDGY SVIFVTGNTP YIIMKEDDSL PRIFPFGNIP IVSMSRWGEG
     SVICIDDIKN ARIYSLNQDN IYYGNKLPIR KIKIGSMLQN YKTLNSIVYH ERTQLYLVSY
     TKEISYEAKA EDGSLLIGYK PELPNAKAFK SGVLLINPKS WEVIDELDLP DNSLVNDMKS
     SFIQIDTRTK RKREYIIVGI GYATMEDVPP TGEFHIYDIT EVVPEPGKPN TNFKLKEIFK
     EDIRGIVSVV NGISGRFLIS QSQKIMVRDV QQDNSVIPVA FLDVPVFVTS LKTFGNLIVI
     GDAMQGIQFV GFDAEPYRMI TLGSSITKFE VISVEFLVNN GDIYFLVTDR DSIMHVLKYA
     PDQPNTLSGQ RLVHCSSFNL HSLNNCTMLL PKNDEFPRDQ RYSRSFQTIT AQVDGSISKI
     VPVKEETYRR LYFIQQQIID KEPQLAGLNP RMERQDNKYY HLGHSLRPML DFNIIKRFKD
     MSMNRRSHIV QKLGKNSNLE VWRDLIDLEF SLRSLKPTDQ N