ID   CFT1_ASPOR              Reviewed;        1393 AA.
AC   Q2TZ19;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Protein cft1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=cft1; ORFNames=AO090103000017;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007174; BAE65504.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2TZ19; -.
DR   SMR; Q2TZ19; -.
DR   STRING; 510516.Q2TZ19; -.
DR   EnsemblFungi; BAE65504; BAE65504; AO090103000017.
DR   HOGENOM; CLU_002414_2_1_1; -.
DR   Proteomes; UP000006564; Chromosome 8.
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; -; 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..1393
FT                   /note="Protein cft1"
FT                   /id="PRO_0000290624"
FT   REGION          427..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1393 AA;  153178 MW;  3D74587D1B39B6A7 CRC64;
     MQCYTELLPP TGVTHSLALP FISESANNLV VARTSRLQIF SLLDVGPRPG GIEEQGVPKL
     VLEREYALPG TVTDLCRVKL LNTKSGGEAI LLAFRNAKLA LIEWDPGRYG ICTISIHYYE
     RDDSTSSPWV PDLSSCGSIL SVDPSSRCAV FNFGIRNLAI LPFHQPGDDL VMDDYGELDD
     ERLGSHGLES GTDCDMTKES IAHRAPYSSS FVLPLAALDP SILHPISLAF LYEYREPTFG
     ILYSQVATSN ALLHERKDVV FYTVFTLDLE QRASTTLLSV SRLPSDLFKV VALPPPVGGA
     LLIGSNELVH VDQAGKTNAV GVNEFSRQVS SFSMTDQSDL ALRLEGCIVE RLSETNGDLL
     LVPTTGEIVL VKFRLDGRSV SGISVHPIPP HAGGDIVKSA ASSSAFLGDK RVFLGSEDAD
     SILLGWSVPS SGTKKPRPQA RHTEEDSGGF SDEDQSEDDV YEDDLYATVP EVVVDGRRPS
     AESFGSSLYN FREYDRLLNI GPLKDIAFGR SFTSLGGEEN AGNDSGLELV ASQGWDRSGG
     LAVMKRGLEL QVLNSMRTDL ASCVWTASVA HMEEAVSKTT TQAENRECHQ YVVVSKATSA
     EREQSEVFRV EGQELRPFRA PEFNPNEDVT IDIGTLIGKN RVVQILRSEV RSYDGDLGLA
     QIYPVWDEDT SEERMAISSS LVDPYVAILR DDSTLLLLQA DDSGDLDEVE LNEQIANSKW
     TSCCLYFDKT GIFSSISATS DELAQNSMTL FLMTQDCRLF IYRLPDQKLL AIIEGVDCLP
     PVLSSEPPKR STTREVLTEI VVADLGDSWS SFPYLIIRSR HDDLAVYRPF ISITKSVGEP
     HADLNFLKET NLVLPRITSG VEDQSSTEEV IKSVPLRIVS NISGFSAIFR PGVSPGFIVR
     TSTSSPHFLG LKGGYAQSLS KFQTSECGEG FILLDSKVLC FILLCLTYCI LSFHTGCHSY
     YPWTIQQIPI GEQVDHLAYS SSSGMYVIGT SHRTEFKLPE DDELHPEWRN EMTSFFPEVQ
     RSSLKVVSPK TWTVIDSPAE HVMAVKNMSL EISENTHERK DMIVVGTAFA RGEDIASRGC
     VYVFEVIKVV PDPKRPEMDR KLRLVGKEPV KGAVTALSEI GGQGFLIVAQ GQKCIVRGLK
     EDGSLLPVAF MDVQCHVSVV KELKGTGMCI IADAVKGLWF AGYSEEPYKM SLFAKDLDYL
     EVLAADFLPD GNKLFILVAD SDCNLHVLQY DPEDPKSSNG DRLLSRSKFH TGNFISTLTL
     LPRTSVSSEQ MISDVDAMDV DIKIPRHQML ITSQNGSVGL VTCVSEESYR RLSALQSQLT
     NTIEHPCGLN PRAFRAVESD GTAGRGMLDG KLLFQWLDMS KQRKVEIASR VGANEWEIKA
     DFEAISGEGL GYL