ID   CFT1_ASPNC              Reviewed;        1383 AA.
AC   A2R919;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Protein cft1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=cft1; ORFNames=An16g09140;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270382; CAK47110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2R919; -.
DR   SMR; A2R919; -.
DR   PaxDb; A2R919; -.
DR   PRIDE; A2R919; -.
DR   EnsemblFungi; CAK47110; CAK47110; An16g09140.
DR   HOGENOM; CLU_002414_2_1_1; -.
DR   Proteomes; UP000006706; Chromosome 5R.
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; 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..1383
FT                   /note="Protein cft1"
FT                   /id="PRO_0000290623"
FT   REGION          441..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..467
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1383 AA;  151748 MW;  8BD2612713474721 CRC64;
     MQCYTEILPP TGVTHALAVP FLAATSDDLI VVRTSLLQIY SLHKVASHAE GADAQQESTK
     LLLEKEYSLS GTVTGLCRVK VLNSKSGGEA VLVAFRNAKL SLIEWDPERR GISTISIHYY
     ERDDLTRSPW VPDLNNCGSI LSVDPSSRCA IFNFGIRNLA IIPFHQPGDD LVMDDYGSDL
     GEGISTDHDL GGGTVADKAK EGIVYQTPYA PSFVLPLTTL DPSILHPISL AFLYEYREPT
     FGILYSQVAT SSALLPERKD VVFYTVFTLD LEQQASTVLL SVSRLPSDLF RVVALPPPVG
     GALLIGSNEL VHIDQAGKTN AVGVNEFSRQ VSSFSMTDQS DLALRLENCI VECLGDSSGD
     MLLVLTTGEM AIVKFKLDGR SVSGISVHLL PAHAGLTSIY SAAAASTFIG DGKIFLGSED
     GDSVLLGYSY SSSSTKKHRL QAKQVIDDSA DMSEEDQSDD DVYEDDLYST SPDTTLTGRR
     PSGESSAFGL YDFRIHDKLI NIGPLRDITM GKRLSTNLEK TGDRTNSTSP ELQIVASQGS
     HKSGGLVVMA REIDPHVVAS ISLESVDCIW TASLTREEEA VSGTSEKMGQ QSQRCYVIAT
     EVKGSDREES LIFVVDGHDL KPFRAPDFNP NEDVTISVGT QESRKRVVQV LKNEVRSYDF
     DLSLTQIYPI WDDDTNDERM AVSASLADSC LAILRDDSTL LFLQADDSGD LDEVVFGEDV
     ASGKWISCCL YSDKTGMFSS IDRTLSEPVK NDMFLFLLSH DCKLFVYRVR DQKLLSIIEG
     TDGLSPLLSS EPPKRSGTRE NLIEAIVADL GETWSASPYL ILRSETDDLI IYKPFVVSTG
     PVEGIHSLKF SKETNSVLPR IPPGVSSTQP SGSDYRARPL RILPDISGLS AVFMPGASAG
     FIIRTSASAP HFLRLRGENS RSSTVRFCKL PPMTRFDYQW TLKRVHLGEQ VDHLAYSTSS
     GMYVLGTCHA TDFKLPEDDE LHPEWRNEAI SFFPSARGSF IKLVWDHHLQ RQDSVILIFH
     LHSFSLGADE YVMAIKNISL EVSENTHERK DMIVVGTAFA RGEDIPSRGC IYVFEVVQVV
     PDPDHPETDR KLKLIGKEPV KGAVTALSEI GGQGFVLVAQ GQKCMVRGLK EDGSLLPVAF
     MDMQCYVSVV KELKGTGMCI LGDAVKGVWF AGYSEEPYKM SLFAKDLDYL EVCAAEFLPD
     GKRLFIVVAD SDCNIHVLQY DPEDPKSSNG DRLLSRSKFH MGNFASTLTL LPRTMVSSEK
     MVSSSDGMDI DNQSPLHQVL MTTQNGSLGL ITCIPEESYR RLSALQSQLT NTLEHPCGLN
     PRAFRAVESD GTAGRGMLDG NLLFKWIDMS KQRKTEIAGR VGAREWEIKA DLEAISGDGL
     GYL