CFT1_CANAL
ID CFT1_CANAL Reviewed; 1420 AA.
AC Q5AFT3; A0A1D8PLK6; Q5AF46; Q5AF47; Q5AF48;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protein CFT1;
DE AltName: Full=Cleavage factor two protein 1;
GN Name=CFT1; OrderedLocusNames=CAALFM_C402430WA;
GN ORFNames=CaO19.10274, CaO19.10275, CaO19.10276, CaO19.2760;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017626; AOW29012.1; -; Genomic_DNA.
DR RefSeq; XP_720510.2; XM_715417.2.
DR AlphaFoldDB; Q5AFT3; -.
DR SMR; Q5AFT3; -.
DR STRING; 237561.Q5AFT3; -.
DR PRIDE; Q5AFT3; -.
DR GeneID; 3637848; -.
DR KEGG; cal:CAALFM_C402430WA; -.
DR CGD; CAL0000179267; orf19.10276.
DR VEuPathDB; FungiDB:C4_02430W_A; -.
DR eggNOG; KOG1896; Eukaryota.
DR HOGENOM; CLU_002414_2_1_1; -.
DR InParanoid; Q5AFT3; -.
DR OrthoDB; 360328at2759; -.
DR PRO; PR:Q5AFT3; -.
DR Proteomes; UP000000559; Chromosome 4.
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; 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..1420
FT /note="Protein CFT1"
FT /id="PRO_0000290625"
FT REGION 161..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..480
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1420 AA; 161940 MW; 315406750D5D52C7 CRC64;
MDAYREFIDP SKVNNCVGCN FISSTKKNLI VGKGSLLQIF ETIQLKQSTI NKPQYRLKLI
DQFKLQGTIT DLKSIRTIEN PNLDYLMVST KYAKFSIIKW DHHLNTIATV SLHYYEHCIQ
NSTFEKLAVS ELILEPTYNS VSCLRFKNLL CFLPFEVIED DEDEEEEEEE DEEDEDEGEE
NIDDTKEKKD KKQSKTDTIE EDKNSTTTNQ EPRLFYDSSF IIDATTLDSS IDTVVDMQFL
HNYREPTIAV LSSKQEVWAG NLIKSKDNIQ FQVLTLDLNL KSTISVFKID NLPYEIDRII
PLPSPLNGTL LVGCNELIHV DNGGVLKRIA VNKFTRLITA SFKSFQDQSD LNLKLENCSV
VPIPDDHRVL LILQTGEFYF INFELDGKSI KRIHIDNVDK KTYDKIQLNH PGEVAILDKN
MLFIANSNGN SPLIQVRYRD SSKTSDTKES KLNKIEEKED NKDDDDNDDD DEDDLYKEEE
EEETQKTISK SHIEFLYHDE LINNGPSSTF TLGICSKEKF KCNLPNPNYN EVSILSNAGT
DSQTKLNIIT PTIQPSISSS LTFSQVNRMW NLNQKYLITS DDVNYKSEIF QIEKSYARMK
SKHFINNELT INMHELNNGK FILQVTPKQI VLYDNKFKKR FTLNDEIKDD EILSSILRDE
FLMIFLASGD VMIFVINTYN ESYDKIEIPK LLDDTIITTG YITNSYLLSA VSKNVNLLLD
NNTSSNKRKR KHSALSNSEG SKKNTGKSQP STAAPPPPPK VNKVKTFVLV TGDNRIVAFN
RFHGEKCYQL NHVDKFTENL SLGFFDPNQS TVDPFIKQIM LNELGDKFDT KDEYLTILTI
GGEIYMYKLY FDGENYFFKK EKDLTITGAP DNAFPYGTSI ERRLVYFPNL NGFTSIFVTG
VIPYLILKTV HSIPRIFQFS KIAAMSISAF SDSKIKNGLI FLDNQQNARI CELPLDFNYE
FNLPMKHVDI GESIKSIAYH ETSDTVVLST FKQIPYDCLD EEGKPIAGII KDIKDTPAMS
FKGSIKLVSP YNWTVIETIE LEDNEVGMTL KSMILDVGSE SGSTLGSDPN SLIKKYNKKK
REYIVIGIGK YRMEDLAANG IFKIYEIIDI IPEPGKPETN HKFKEIFKEE TRGAITSICE
LSGRFLVSQG QKVIVRDLQD DGTVPVAFLD TPVYVSESKS FGNLLILGDP LKGCWLVGFD
AEPFRMIMLG KDTQHISVEC ADFIINDDEI FVLVADNNNV LHLLNYDPDD PQSINGTKLL
TKASFELNST ISCLRSLPLI DIEESVQTDA LTNIAVPPPL PPNTTSNYFQ VIGSTQDGSF
FNVFPINEAA YRRMYILQQQ LIDKEFHYCG LNPRLNRIGS IKLQNNETNT KPILDYDLIR
RFTKLSDDRK RNLANKVSGK GIYQDIWKDI IRFEHTLNDL
